Research
Aboytes Torres, R., Y. Liang, and Schulze T. I.
(1996). Analisis de la expresion in vitro del gene de la hemaglutinina del
virus de la influenza aviar via un marcador citoquimico y microscopia confocal
de rayo laser. [Analysis of the in vitro expression of the Ha gene from an
avian influenza virus, by using cytochemistry and confocal microscopy]. In:
Reunion Nacional de Investigacion Pecuaria, Cuernavaca, Morelos [Mexico], p.
49.
Abstract: El estudio fue disenado para
desarrollar un nuevo sistema de deteccion de la expresion in vitro de la
molecula de HA, utilizando como marcador citoquimico una fetoproteina y un
sistema de deteccion mediante microscopia confocal. El gene de la HA del virus
de la influenza aviar A/DW/WI/1938/80 (H1N1), fue insertado en el vector pREP10
y clonado en E. coli DH5 alfa. Monoestratos de celulas MDBK y MDCK con indices
de confluencia de entre 30 y 50% fueron transformados mediante la tecnica de
transfeccion con liposomas. La seleccion de celulas transformadas se llevo a
cabo con el tratamiento de los cultivos con higromicina como marcador de
seleccion (600 micro l/ml en medio DME completocon 10% v/v suero bovino fetal)
por un periodo de 3 a 4 semanas. Los cultivos celulares transformados en forma
estable fueron crecidos en cubreobjetos y fijados en paraformaldehido (3.7% en
PBS pH 7.2). La expresion temporal o constitutiva del gene de la HA en celulas
mamiferas transformadas fue monitoreada con las tecnicas estandarizadas de IFI
(con anticuerpos mono y policlonales), hemoadsorcion y hemoaglutinacion. La
nueva tecnica alternativa desarrollada se baso en la reaccion de acoplamiento
mediada por la alta afinidad entre el sitio de reconocimiento del recptor,
situado en los polipeptidos de la molecula de HA y el acido sialico de la
fetoproteina bovina (0.2% acido acetilneuroamidico) conjugada con oro coloidal
(10nm). Los ensayos incluyeron los analisis de la reaccion a nivel de
citoplasma y de superficie. Para este efecto se utilizaron monoestratos
permeabilizados con el detergente Tween 20 (0.05%) y monoestratos no
permeabilizadas. Los controles incluyeron celulas infectadas con virus
homologos y heterologos (WSN). Se concluye que la nueva tecnica descrita,
ofrece una alta especificidad y sensibilidad analitica en la deteccion de HA
expresada in vitro a la vez que es rapida y sencilla. Ademas, el potencial de
esta tecnica puede ser extrapolado en ensayos utilizando microscopia optica.
Descriptors: avian influenza virus,
cytochemistry, cell structure, confocal microscopy, influenza virus, viruses.
Air, G.M., L.R. Ritchie, W.G. Laver, and P.M. Colman
(1985). Gene and protein sequence of an influenza neuraminidase with
hemagglutinin activity. Virology 145(1): 117-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: An influenza virus neuraminidase (NA) of the
N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R.
G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology 137, 314-323). To
determine sequence relationships between this NA and other known NA and HA
subtype sequences, and as a necessary step toward a complete structure
determination, we have cloned a full-length copy of the coding sequence of the
N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using
SalI linkers. The gene was sequenced by directed subcloning into the
single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy
procedure. Most of the NA sequence was also obtained by direct protein
sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared
to N1 or N2 sequences, respectively. There is no significant homology to any
known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the
other NA molecules, the N9 NA is anchored in the membrane by an N-terminal
hydrophobic region, from which biologically active heads can be released by
pronase.
Descriptors: genes viral, hemagglutinins viral, influenza
A virus avian enzymology, influenza A virus enzymology, neuraminidase genetics,
amino acid sequence, base sequence, cloning, molecular, influenza A virus avian
genetics, avian immunology, influenza A virus genetics, influenza A virus
immunology.
Akhmatullina, N.B. and K.G. Mustafin (1982). Biologicheski
aktivnye ribonukleoproteidy kletok, zarazhennykh virusom chumy ptits.
[Biologically active ribonucleoproteins of cells infected with fowl plague
virus]. Voprosy Virusologii (1): 29-32. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The results of studies of physico-chemical
and biological properties of virus-specific ribonucleoproteins (RNP) in
influenza infection are presented. Particular attention is given to the
infectious properties of RNP. The earliest infectivity was found to be
associated with RNP structures sedimenting from nuclear extract in a zone of
30-40S.
Descriptors: nucleoproteins pharmacology,
ribonucleoproteins pharmacology, cell nucleus microbiology, chemistry,
physical, chick embryo, cytoplasm microbiology, influenza A virus avian
pathogenicity, ribonucleoproteins isolation and purification, species
specificity, time factors, virus cultivation.
Akkina, R.K. (1990). Antigenic reactivity and
electrophoretic migrational heterogeneity of the three polymerase proteins of
type A human and animal influenza viruses. Archives of Virology
111(3-4): 187-97. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Antigenic reactivity of the three polymerase
proteins PB1, PB2, and PA of type A influenza viruses of animal and human
origin were analysed by radioimmunoprecipitation using monospecific antisera.
Each of the polymerase monospecific antisera made against the polymerase
proteins of the human A/WSN/33 (H1N1) influenza virus reacted efficiently with
the homologous proteins of all the known thirteen HA subtype viruses of avian
influenza virus, three subtypes of human influenza virus, swine and equine
influenza viruses. This broad reactivity of each of the antisera indicated that
the polymerase proteins are antigenically related among the type A influenza
viruses and therefore can be considered as type specific antigens similar to
the other viral internal proteins nucleoprotein (NP) and matrix protein (M). No
electrophoretic migrational heterogeneity was found among the PB2 proteins of
different subtype viruses, whereas PB1 protein exhibited minor variation.
However, PA protein from among various viral subtypes showed considerable
heterogeneity. Each of the polymerase antisera also immunoprecipitated
additional antigenically related polypeptides with distinct electrophoretic
mobilities from cells infected with each of the influenza viral subtypes.
Descriptors: DNA directed RNA polymerases immunology,
influenza A virus human enzymology, influenza A virus enzymology, viral
proteins immunology, antigens, viral immunology, human immunology, influenza A
virus immunology, precipitin tests.
Alexander, D.J., M.S. Collins, and M. Parkinson.
(1981). Plaque-forming ability in MDCK cells and structure of the
haemagglutinin of influenza A viruses which differ in virulence for chickens.
In: Proceedings of the First International Symposium on Avian Influenza,
Beltsville, Maryland, USA, p. 148-156.
NAL
Call Number:
aSF995.6.I6I5 1981a
Descriptors: avian influenza A virus, virulence,
hemagglutinin, cells, chickens.
Alexander, D.J., G. Parsons, and R.J. Manvell (1986).
Experimental assessment of the pathogenicity of eight avian influenza A
viruses of H5 subtype for chickens, turkeys, ducks and quail. Avian
Pathology 15(4): 647-662. ISSN:
0307-9457.
NAL
Call Number: SF995.A1A9
Descriptors: avian influenza virus, chickens,
turkeys, ducks, quails, chickens, immune
response, disease transmission, clinical signs, mortality.
Alexander, D.J., G.F. Wood, M.S. Collins, J. Banks,
and R.J. Manvell (1996). Recent work on the pathogenicity of avian influenza
viruses and the pathogenicity and antigenicity of Newcastle disease virus. Proceedings
of the Western Poultry Diseases Conference 45: 1-4.
NAL
Call Number: SF995.W4
Descriptors: Newcastle disease virus, avian influenza
virus, influenza virus, orthomyxoviridae, paramyxoviridae, viruses.
Almeida, J.D. and C.M. Brand (1975). A
morphological study of the internal component of influenza virus. Journal of General Virology 27(3):
313-8. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Rapid treatment of influenza virus directly
on the microscope grid with non-ionic detergent had allowed better
visualization of the internal component. Many micrographs show that this
ribonucleoprotein (RNP) is present as a continuous stand of 6 nm diam. arranged
in the form of a double coil or helix. In spite of the minimal treatment to
which the virus was subjected most helices still showed signs of degradation.
The findings that we have obtained lead us to suggest that the RNP component of
influenza virus must be very sensitive to both chemical and physical
manipulations, any of which could cause it to fracture from one continuous
strand into several pieces, although such breakages could possibly occur at
specific points along its length.
Descriptors: orthomyxoviridae ultrastructure, RNA, viral,
viral proteins, chick embryo, cyprinidae, influenza A virus avian
ultrastructure, microscopy, electron, phosphotungstic acid, recombination,
genetic, surface active agents, tissue culture.
Almeida, J.D. and A.P. Waterson (1967). Some
observations on the envelope of an influenza virus. Journal of General
Microbiology 46(1): 107-10. ISSN:
0022-1287.
NAL
Call Number: 448.3 J823
Descriptors: influenza A virus avian, lipoproteins
analysis, microscopy, electron, viral proteins analysis.
Almond, J.W. (1977). A single gene determines the
host range of influenza virus. Nature 270(5638): 617-8. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: genes viral, influenza A virus avian
genetics, virus replication, cell line, DNA directed RNA polymerases genetics,
DNA directed RNA polymerases metabolism, avian physiology, RNA viral genetics,
viral proteins genetics, viral proteins physiology.
Almond, J.W. and R.D. Barry (1979). Genetic
recombination between two strains of fowl plague virus: construction of genetic
maps. Virology 92(2): 407-15.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus avian
genetics, RNA viral genetics, electrophoresis, polyacrylamide gel, avian
analysis, viral analysis, recombination, genetic, viral proteins analysis,
viral proteins biosynthesis.
Almond, J.W. and V. Felsenreich (1982). Phosphorylation
of the nucleoprotein of an avian influenza virus. Journal of General
Virology 60(Pt. 2): 295-305. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: High resolution polyacrylamide gel
electrophoresis (PAGE) of chick embryo fibroblast cells infected with the avian
influenza virus FPV-Rostock revealed two distinct polypeptides migrating in the
region of the nucleoprotein (NP). One-dimensional fingerprinting of these
polypeptides showed that they were both nucleoprotein, and [32P]orthophosphate
labelling revealed that they differed with respect to their state of
phosphorylation. Pulse-chase studies using [35S]methionine indicated that
phosphorylation of a certain proportion of NP occurs rapidly after synthesis
and is associated with transport to the nucleus. Nucleoprotein which remained
in the cytoplasm was predominantly non-phosphorylated. Both the phosphorylated
and the non-phosphorylated types of NP were found in ribonucleoprotein
complexes (RNPs) of different densities isolated on renografin gradients, but
RNPs isolated from the nucleus contained much more phosphorylated NP than those
from the cytoplasm. The kinase responsible for nucleoprotein phosphorylation
appears to be influenced by temperature of incubation of the infected cells.
Descriptors: influenza A virus avian metabolism,
nucleoproteins metabolism, viral proteins metabolism, cell line, cell nucleus
analysis, cell nucleus metabolism, chick embryo, cytoplasm analysis,
fibroblasts, phosphorylation, protein kinases metabolism, ribonucleoproteins
analysis, temperature.
Almond, J.W., D. McGeoch, and R.D. Barry (1977). Method
for assigning temperature-sensitive mutations of influenza viruses to
individual segments of the genome. Virology 81(1): 62-73. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes, influenza A virus avian growth and development,
mutation, chick embryo, avian analysis, avian radiation effects, peptides
analysis, RNA viral analysis, recombination, genetic, temperature, tissue
culture, ultraviolet rays, viral proteins analysis, virus replication.
Almond, J.W., D. McGeoch, and R.D. Barry (1979). Temperature-sensitive
mutants of fowl plague virus: isolation and genetic characterization. Virology
92(2): 416-27. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus avian
genetics, recombination, genetic, avian analysis, mutation, temperature, viral
proteins analysis, viral proteins biosynthesis.
Altmuller, A., W.M. Fitch, and C. Scholtissek (1989).
Biological and genetic evolution of the nucleoprotein gene of human
influenza A viruses. Journal of General Virology 70(Pt. 8): 2111-9.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: There is a significant difference in the
ability of human influenza A virus H1N1 strains isolated up to 1977 and those
isolated later to rescue temperature-sensitive mutants of fowl plague virus
with a defect in the nucleoprotein (NP) gene. Therefore the NP genes of five
human H1N1 and H3N2 influenza A virus strains, isolated between 1950 and 1978, have
been sequenced. By comparison with previous and more recent isolates, an
evolutionary pathway has been established. Three amino acid replacements were
found which might be responsible for the functional difference between the USSR
(1977) and the Brazil (1978) strains. The California (H1N1) strain isolated in
1978 had acquired by reassortment the NP gene of a human H3N2 virus circulating
at about 1977 as had been previously suggested by investigations involving
RNase fingerprint or hybridization techniques.
Descriptors: evolution, genes viral, influenza A virus
human genetics, nucleoproteins genetics, viral core proteins, viral proteins
genetics, amino acid sequence, base sequence, chick embryo, chickens, influenza
A virus avian genetics, molecular sequence data, mutation, sequence homology,
nucleic acid.
Altmuller, A., M. Kunerl, K. Muller, V.S. Hinshaw,
W.M. Fitch, and C. Scholtissek (1992). Genetic relatedness of the
nucleoprotein (NP) of recent swine, turkey, and human influenza A virus (H1N1)
isolates. Virus Research 22(1): 79-87. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The sequences of nucleoprotein (NP) genes of
recent human and turkey isolates of influenza A viruses, which serologically
could be correlated to contemporary swine viruses, were determined. These
sequences were closely related to the NPs of these swine viruses and they
formed a separate branch on the phylogenetic tree. While the early swine virus
from 1931 resembled the avian strains in consensus amino acids of the NP and in
its ability to rescue NP ts mutants of fowl plague virus in chicken embryo
cells, the later strains on that branch were different: at 15 positions they
have their own amino acids and they rescued the NP ts mutants only poorly. Of
the NPs of the human New Jersey/76 isolates analysed, one clustered with the
recent H1N1 swine viruses of the U.S.A., the other one with contemporary human
strains. Since the NP is one of the main determinants of species specificity it
is concluded that, although the H1N1 swine isolates from the U.S.A. form their
own branch in the phylogenetic tree, they can be transmitted to humans and
turkeys, but they do not spread further in these populations and so far have
not contributed to human pandemics. It is not very likely that they will do so
in future, since its branch in the phylogenetic tree develops further away from
the human and avian branch.
Descriptors: influenza A virus avian genetics, human
genetics, porcine genetics, nucleoproteins genetics, fowl plague microbiology,
influenza microbiology, phylogeny, sequence homology, nucleic acid, turkeys.
Anisimova, E., Y. Ghendon, and S. Markushin (1980). Ultrastructural
changes in cells induced by temperature-sensitive mutants of fowl plague virus
at permissive and non-permissive temperature. Journal of General
Virology 47(1): 11-8. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Ultrastructural changes developing in chick
embryo fibroblast cultures infected with a wild-type strain of fowl plague virus
(FPV) or one of six FPV temperature-sensitive (ts) mutants belonging to
different complementation groups were studied. Cells infected with wild-type
FPV and incubated at optimal (36 degrees C) or nonpermissive temperature (42
degrees C) displayed changes similar to those described for orthomyxoviruses.
The same patterns of changes were observed at 36 degrees C in cells infected
with ts mutants belonging to five of the complementation groups. Mutant ts 303,
possessing mutation-altered haemagglutinin, induced at 36 degrees C the
formation of virions carrying a considerably reduced number of spikes on their
surfaces. At 42 degrees C, cells infected with ts mutant 131, with a defective
primary transcription stage, showed no morphological changes and no formation
of electron-dense inclusions. Cells infected with ts mutants with defective
secondary transcription or replication displayed nuclear inclusions but no
formation of filamentous cytoplasmic structures or virions. Mutant ts 5 with
defective late morphogenesis induced formation of considerably enhanced numbers
of nuclear inclusions.
Descriptors: cell transformation, viral, influenza A virus
avian, cell nucleus ultrastructure, cultured cells, chick embryo, fibroblasts
ultrastructure, inclusion bodies, viral ultrastructure, microscopy, electron,
mutation, temperature, virion ultrastructure.
Anonymous (1998). From the Centers for Disease
Control and Prevention. Isolation of avian influenza A(H5N1) viruses from
humans--Hong Kong, May-December 1997. JAMA the Journal of the American
Medical Association 279(4): 263-4.
ISSN: 0098-7484.
NAL
Call Number: 448.9 Am37
Descriptors: influenza epidemiology, influenza A virus
avian isolation and purification, adolescent, adult, child, child, preschool,
Hong Kong epidemiology, influenza virology, middle aged.
Anonymous (1998). From the Centers for Disease
Control and Prevention. Update: isolation of avian influenza A(H5N1) viruses
from humans--Hong Kong, 1997-1998. JAMA the Journal of the American
Medical Association 279(5): 347-8.
ISSN: 0098-7484.
NAL
Call Number: 448.9 Am37
Descriptors: influenza epidemiology, influenza virology,
influenza A virus avian isolation and purification, Hong Kong epidemiology,
seroepidemiologic studies.
Anschutz, W., C. Scholtissek, and P. Rott (1972). Genetic
relationship between different influenza strains. Medical Microbiology
and Immunology 158(1): 26-31. ISSN:
0300-8584.
Descriptors: influenza strains, influenza A virus, genetic
relationships, Hong Kong.
Armstrong, S.J. and R.D. Barry (1974). The
topography of RNA synthesis in cells infected with fowl plague virus. Journal
of General Virology 24(3): 535-47.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, autoradiography, cell nucleus enzymology, cell nucleus
metabolism, cultured cells, chick
embryo, cytoplasm enzymology, DNA directed RNA polymerases metabolism,
deoxyadenosines pharmacology, fibroblasts, avian enzymology, avian growth and
development, mycotoxins pharmacology, Newcastle disease virus growth and
development, Newcastle disease virus metabolism, time factors, tritium, uracil
nucleotides metabolism, uridine metabolism,
virus replication.
Armstrong, S.J., M.C. Outlaw, and N.J. Dimmock (
1990). Morphological studies of the neutralization of influenza virus by
IgM. Journal of General Virology 71(Pt. 10): 2313-9.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Quantitative relationships between
neutralization, aggregation and attachment to monolayers of chick embryo
fibroblast (CEF) cells have been studied using a constant amount of influenza
A/fowl plague virus/Rostock/34 (H7N1) and varying amounts of purified mouse
polyclonal IgM directed against the haemagglutinin, the major viral
neutralization antigen. There are two major types of interaction. (i) At low
concentrations of IgM there is aggregation of virus, but no neutralization
provided that the aggregates are dispersed by vortexing and dilution. Maximum
aggregation occurs at less than seven molecules of IgM per virion and the IgM
is probably bound in the 'staple' or 'crab' conformation at these
concentrations. (ii) At higher concentrations there is neutralization and this
coincides with inhibition of attachment of virus to CEF cells. Neutralization
of 50% infectivity requires about 35 molecules of IgM per virion. The maximum
neutralization observed was only 87%. Quantitative data and electron microscopy
observations suggest that molecules of IgM at the higher concentrations adopt a
planar stance approximately perpendicular to the viral surface. It appears that
IgM neutralizes fowl plague virus in vitro primarily by interfering with its
attachment to cells; the fraction of neutralized virus that does attach is
known not be internalized.
Descriptors: antibodies, viral immunology, immunoglobulin
M immunology, influenza A virus avian immunology, antigen antibody complex,
immunohistochemistry, avian ultrastructure, microscopy, electron,
neutralization tests.
Asadullaev, T.A. and A.G. Bukrinskaia (1976). Kharakteristika
RNK, vydelennoi iz iadernogo RNK-sinteziruiushchego kompleksa virusa grippa.
[Characteristics of RNA isolated from the nuclear RNA-synthesizing complex of
influenza virus]. Voprosy Virusologii (6): 656-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: When Ehrlich ascitic carcinoma cells infected
with classical fowl plague virus and treated with actinomycin D were pulse
labeled for 10 min with 3H-uridine, it was mainly incorporated into nucleoplasm
structures sedimenting in sucrose gradients at 120S. At 2-hr exposure of the
infected cells to 3H-uridine radioactivity was found in nucleoplasm in the area
of 65S and in the cytoplasm in 30-40S zone. The analysis of RNA isolated from
these structures gave the following results. The RNA isolated from 120S
structures sedimented in two zones of sucrose gradient: 11S and 16-23S. The 11S
RNA was resistant to RNA-ase, while 16-23S RNA was sensitive to RNA-ase. A
similar (16-23S) RNA was isolated from virus-specific structures 65S and
30-40S.
Descriptors: influenza A virus avian, RNA viral
biosynthesis, viral isolation and purification, virus replication, carcinoma,
Ehrlich tumor analysis, carcinoma, Ehrlich tumor microbiology, catalysis, cell
nucleus metabolism, centrifugation, density gradient, ribonucleases,
transcription, genetic, uridine metabolism.
Asadullaev, T.A., A.K. Gitel'man, and A.G.
Bukrinskaia (1975). Abortivnaia infektsiia miksovirusov v kletkakh astsitnoi
kartsinomy Erlikha. Analiz virusspetsificheskikh struktur v astsitnoi
zhidkosti. [Abortive myxovirus infection of Ehrlich ascites carcinoma cells.
Analysis of virus-specific structures in the ascitic fluid]. Voprosy
Virusologii (3): 278-82. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: In the course of classical fowl plague virus
reproduction in Ehrlich ascites carcinoma cells both hemagglutinins and
S-antigen accumulate and titers of the infectious activity increase. However
virus reproduction does not terminate in formation of virus, and subviral
structures are found in the liquid fraction of the infected cells. Analysis of
these structures has shown them to have a sedimentation coefficient of 350-370S
and buovant density 1.29 g/ml. The rapidly sedimenting structure has
complement-fixing hemagglutinating activity but bow infectivity.
Descriptors: carcinoma, Ehrlich tumor microbiology,
influenza A virus avian growth and development, virus replication, amino acids,
antigens, viral analysis, carcinoma, Ehrlich tumor analysis, centrifugation,
density gradient, complement fixation tests, hemagglutinins viral analysis,
methionine, sulfur radioisotopes, tritium.
Assadullaeff, T., A.K. Gitelman, and A.G. Bukrinskaya
(1975). Influenza virus RNA-synthesizing complex in the nucleoplasm of
infected cells. Journal of General Virology 29(1): 137-42. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: An RNA-synthesizing complex was found in the
nucleoplasm of fowl plague virus-infected chicken fibroblast and Ehrlich tumour
cells. The complex sedimented at 120 S and banded in caesium chloride at 1-39
to 1-41 g/ml. It contained an influenza nucleocapsid protein as a major protein
constituent. The complex functioned late in infection, and RNA synthesis in it
was resistant to actinomycin D, the properties expected of influenza virus replicative
complex.
Descriptors: cell nucleus metabolism, influenza A virus
avian metabolism, RNA viral biosynthesis, carcinoma, Ehrlich tumor, chick
embryo, dactinomycin pharmacology, fibroblasts, avian growth and development,
mice, tissue culture, viral proteins biosynthesis, virus replication.
Astapovich, L.G., G.A. Ivanova, and S.B. Logginov
(1968). Elektronnomikroskopicheskoe izuchenie shtammov virusa klassicheskoi
chumy ptits. [An electron microscopic study of strains of the virus of classic
fowl plague]. Veterinariia 45(9): 24-6. ISSN: 0042-4846.
NAL
Call Number: 41.8 V6426
Descriptors: influenza A virus avian cytology, chick
embryo, microscopy, electron.
Atsev, S., I. Gagov, and I. Mikhailov (1981). Vurkhu
tsitologichite razlichiia v kletuchni kulturi, zarazeni s virusa na
klasicheskata chuma po ptitsite i gripen virus tip A. [Cytological differences
in cell cultures infected with classical fowl plague virus and influenza virus
type A]. Acta Microbiologica Bulgarica 9: 79-86. ISSN: 0204-8809.
NAL
Call Number: QR1.A37
Descriptors: influenza A virus avian pathogenicity,
cattle, cytopathogenic effect, viral, time factors, virus cultivation, virus
replication.
Austin, F.J., Y. Kawaoka, and R.G. Webster (1990). Molecular
analysis of the haemagglutinin gene of an avian H1N1 influenza virus. Journal
of General Virology 71(Pt. 10): 2471-4.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: This study presents the first nucleotide
sequence and deduced primary amino acid sequence of a subtype H1 haemagglutinin
from the avian influenza virus A/duck/Alberta/35/76 (H1N1). The molecule is
structurally, antigenically and molecularly similar to H1 haemagglutinins of
human viruses but sequence homology differences indicate that there has not
been a recent transfer of haemagglutinin genetic information between them.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, amino acid sequence, base sequence, genes, structural,
viral, avian immunology, molecular sequence data.
Austin, F.J. and R.G. Webster (1986). Antigenic
mapping of an avian H1 influenza virus haemagglutinin and interrelationships of
H1 viruses from humans, pigs and birds. Journal of General Virology
67(Pt. 6): 983-92. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Monoclonal antibodies to the haemagglutinin
(HA) of the avian H1 influenza virus A/duck/Alberta/35/76 were used to
construct an operational antigenic map of the HA molecule and to study the
interrelationships of H1 viruses from different hosts. Haemagglutination
inhibition tests between the monoclonal antibodies and variants selected by
them provided evidence of four antigenic regions which overlap to varying
degrees. Avian H1 influenza viruses displayed a spectrum of reactivities to the
monoclonal antibody panel. Representatives of the epidemic strains of human H1
influenza viruses and early swine influenza viruses showed little or no
reactivity with the monoclonal antibodies but swine influenza-like viruses
isolated from pigs and humans in the last decade reacted with 11 of 17
antibodies. The antigenic similarity of these viruses to many avian isolates
suggests that there has been a transfer of HA genetic information between
mammalian and avian H1 influenza viruses.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, antibodies, monoclonal diagnostic use, epitopes, human
immunology, porcine immunology, species specificity.
Avery, R.J. (1975). Abortive infection of L cells
by influenza virus: absence of virion RNA synthesis. Journal of Virology
16(2): 311-4. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Influenza virus multiplies productively in
chick cells and abortively in L cells. The infecting influenza virus RNA
genomes are less stable in infected L cells than in infected chick cells.
However, transcription of the virus genome in L cells, while reduced in rate,
is not decreased in extent. There is no detectable synthesis of virion RNA in L
cells, and this is the most likely cause of the abortive infection.
Descriptors: influenza A virus avian metabolism, L cells
cell line, RNA viral biosynthesis, chick embryo, fibroblasts, avian growth and
development, mice, nucleic acid hybridization, phosphorus radioisotopes, tissue
culture, transcription, genetic, virus replication.
Avery, R.J. (1974). The subcellular localization
of virus-specific RNA in influenza virus-infected cells. Journal of
General Virology 24(1): 77-88. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian growth and
development, RNA viral analysis, virus replication, base sequence, cell nucleus
analysis, chick embryo, cytoplasm analysis, nucleic acid hybridization, RNA,
ribosomal analysis, ribonucleases, time factors, tritium, uridine.
Aymard, M., A.R. Douglas, M. Fontaine, J.M. Gourreau,
C. Kaiser, J. Million, and J.J. Skehel (1985). Antigenic characterization of
influenza A (H1N1) viruses recently isolated from pigs and turkeys in France.
Bulletin of the World Health Organization 63(3): 537-42. ISSN: 0042-9686.
NAL
Call Number: 449.9 W892B
Descriptors: antigens, viral analysis, influenza A virus
avian immunology, porcine immunology, immunology, swine microbiology, turkeys
microbiology, France, avian isolation and purification, porcine isolation and
purification.
Baez, M., R. Taussig, J.J. Zazra, J.F. Young, P.
Palese, A. Reisfeld, and A.M. Skalka (1980). Complete nucleotide sequence of
the influenza A/PR/8/34 virus NS gene and comparison with the NS genes of the
A/Udorn/72 and A/FPV/Rostock/34 strains. Nucleic Acids Research
8(23): 5845-58. ISSN: 0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: The nucleotide sequence of the NS gene of the
human influenza virus A/PR/8/34 was determined and found to be the same length
(890 nucleotides) as the NS gene of another human influenza virus A/Udorn/72
and of the avian isolate A/FPV/Rostock/34. Comparison of the sequences of the
NS genes of the two human influenza viruses shows an 8.9% difference whereas the
NS gene of the avian isolate differs by only 8% from that of the human strain
A/PR/8/34. The extensive sequence similarity among these three genes does not
support the notion of species specific homology groups among NS genes of avian
and human influenza virus strains. The primary sequence of the A/PR/8/34 NS
gene is consistent with the findings that the influenza virus NS gene may code
for two overlapping polypeptides. In addition, an open reading frame
potentially coding for a polypeptide 167 amino acids in length was found in the
negative strand RNA of the A/PR/8/34 virus NS gene.
Descriptors: genes viral, influenza A virus avian
genetics, human genetics, RNA viral genetics, amino acid sequence, base
sequence, cloning, molecular, peptides genetics, species specificity.
Baigent, S.J., R.C. Bethell, and J.W. McCauley (
1999). Genetic analysis reveals that both haemagglutinin and neuraminidase
determine the sensitivity of naturally occurring avian influenza viruses to
zanamivir in vitro. Virology 263(2): 323-38. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: antiviral agents pharmacology, genes viral
physiology, hemagglutinins viral metabolism, influenza A virus avian drug
effects, neuraminidase antagonists and inhibitors, neuraminidase metabolism,
sialic acids pharmacology, amino acid sequence, base sequence, cultured cells,
chick embryo, chickens blood, chickens virology, dogs, erythrocytes virology,
genes viral genetics, glycosylation,
hemagglutination, viral drug effects, hemagglutinins viral genetics,
avian enzymology, avian genetics, avian physiology, inhibitory concentration
50, lactose analogs and derivatives, lactose metabolism, molecular sequence
data, mutation genetics, neuraminidase chemistry, neuraminidase genetics,
reassortant viruses drug effects, reassortant viruses enzymology, reassortant
viruses genetics, reassortant viruses physiology, sialic acids metabolism,
substrate specificity, virus replication, drug effects.
Baigent, S.J. and J.W. McCauley (2001). Glycosylation
of haemagglutinin and stalk-length of neuraminidase combine to regulate the
growth of avian influenza viruses in tissue culture. Virus Research
79(1-2): 177-85. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The influence on virus replication in culture
of the presence and location of glycosylation sites on the haemagglutinin (HA)
glycoprotein of avian influenza viruses and differences in length of the stalk
region of their neuraminidase (NA) glycoprotein was examined using reassortant
viruses. Plaque size was measured in the presence or absence of bacterial
neuraminidase (CPNA) and/or an influenza virus NA inhibitor, zanamivir, to
assess the relative contribution of the NA to replication efficiency in tissue
culture. The following conclusions were drawn, (1) HA lacking glycosylation at
158 gives inefficient growth when combined with short-stalked NAs, and
efficient growth when combined with long-stalked NAs. (2) Glycosylation at 158
of HA makes the virus less dependent on NA for release from its receptors. (3)
HA with glycosylation at 158 gives efficient growth when combined with
short-stalked NAs but, when combined with long-stalked NAs, growth is very
efficient and excess NA activity is disadvantageous. (4) HA having
glycosylation at 158 combined with short-stalked NAs, or HA lacking
glycosylation at 158 combined with long-stalked NAs may represent optimal
combinations. The results reinforce the importance of a balance of HA and NA
activity for efficient virus exit from, and entry into cells.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, influenza A virus avian growth and development, neuraminidase
metabolism, antiviral agents pharmacology, chick embryo, C lostridium
perfringens enzymology, enzyme inhibitors pharmacology, glycosylation,
hemagglutinin glycoproteins, influenza virus chemistry, hemagglutinin
glycoproteins, influenza virus genetics, avian drug effects, avian genetics,
avian physiology, neuraminidase antagonists and inhibitors, plaque assay,
protein structure, tertiary, sialic acids pharmacology.
Baker, A.T., J.N. Varghese, W.G. Laver, G.M. Air, and
P.M. Colman (1987). Three-dimensional structure of neuraminidase of subtype
N9 from an avian influenza virus. Proteins 2(2): 111-7. ISSN: 0887-3585.
NAL
Call Number: QP551.P698
Abstract: Neuraminidases from different subtypes of
influenza virus are characterized by the absence of serological
cross-reactivity and an amino acid sequence homology of approximately 50%. The
three-dimensional structure of the neuraminidase antigen of subtype N9 from an
avian influenza virus (A/tern/Australia/G70c/75) has been determined by X-ray
crystallography and shown to be folded similarly to neuraminidase of subtype N2
isolated from a human influenza virus. This result demonstrates that absence of
immunological cross-reactivity is no measure of dissimilarity of polypeptide
chain folding. Small differences in the way in which the subunits are organized
around the molecular fourfold axis are observed. Insertions and deletions with
respect to subtype N2 neuraminidase occur in four regions, only one of which is
located within the major antigenic determinants around the enzyme active site.
Descriptors: influenza A virus avian enzymology,
neuraminidase immunology, neuraminidase metabolism, amino acid sequence,
antigens, viral, binding sites, avian classification, models, molecular,
molecular sequence data, n acetylneuraminic acid, protein conformation, sialic
acids metabolism.
Banbura, M.W., Y. Kawaoka, T.L. Thomas, and R.G.
Webster (1991). Reassortants with equine 1 (H7N7) influenza virus
hemagglutinin in an avian influenza virus genetic background are pathogenic in
chickens. Virology 184(1): 469-471.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Reassortants possessing the hemagglutinin
(HA) gene from A/Equine/London/1416/73 (H7N7) [Eq/Lond) and five or more genes
from A/Chicken/Pennsylvania/1370/83 (H5N2) [Ck/Penn] were lethal in chickens.
This result demonstrates that horses can maintain influenza viruses whose HAs
are capable of promoting virulence. Thus, reassortment of equine and avian
influenza virus genes could generate viruses that might be lethal in domestic
poultry.
Descriptors: fowls, horses, avian influenza virus, equine
influenza virus, hemagglutinins, genes, amino acids, virulence, pathogenicity,
mortality, molecular sequence data, EMBL m58657, GENBANK m58657.
Bankowski, R.A. (1975). Interferon and its role in
poultry health. American Journal of Veterinary Research 36(4):
494-497. ISSN: 0002-9645.
NAL
Call Number: 41.8 Am3A
Descriptors: interferon, viral diseases, poultry.
Banks, J., E.C. Speidel, J.W. McCauley, and D.J.
Alexander (2000). Phylogenetic analysis of H7 haemagglutinin subtype
influenza A viruses. Archives of Virology 145(5): 1047-58. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A 945 nucleotide region (bases 76-1020) of
the HA1 part of the HA gene was obtained for 31 influenza viruses of H7 subtype
isolated primarily from Europe, Asia and Australia over the last 20 years.
These were analysed phylogenetically and compared with sequences of the same
region from 23 H7 subtype viruses available in Genbank. The overall results
showed two geographically distinct lineages of North American and Eurasian
viruses with major sublineages of Australian, historical European and equine
viruses. Genetically related sublineages and clades within these major groups
appeared to reflect geographical and temporal parameters rather than being
defined by host avian species. Viruses of high and low virulence shared the
same phylogenetic branches, supporting the theory that virulent viruses are not
maintained as a separate entity in waterfowl.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian classification, avian genetics, amino acid
sequence, fowl plague virology, genes viral, avian isolation and purification,
phylogeny, poultry, sequence homology, amino acid.
Banks, J., E.S. Speidel, E. Moore, L. Plowright, A.
Piccirillo, I. Capua, P. Cordioli, A. Fioretti, and D.J. Alexander (2001). Changes
in the haemagglutinin and the neuraminidase genes prior to the emergence of
highly pathogenic H7N1 avian influenza viruses in Italy. Archives of
Virology 146(5): 963-73. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Outbreaks of avian influenza due to an H7N1
virus of low pathogenicity occurred in domestic poultry in northern Italy from
March 1999 until December 1999 when a highly pathogenic avian influenza (HPAI)
virus emerged. Nucleotide sequences were determined for the HA1 and the stalk
region of the neuraminidase (NA) for viruses from the outbreaks. The HPAI
viruses have an unusual multibasic haemagglutinin (HA) cleavage site motif,
PEIPKGSRVRRGLF. Phylogenetic analysis showed that the HPAI viruses arose from low
pathogenicity viruses and that they are most closely related to a wild bird
isolate, A/teal/Taiwan/98. Additional glycosylation sites were present at amino
acid position 149 of the HA for two separate lineages, and at position 123 for
all HPAI and some low pathogenicity viruses. Other viruses had no additional
glycosylation sites. All viruses examined from the Italian outbreaks had a 22
amino acid deletion in the NA stalk that is not present in the N1 genes of the
wild bird viruses examined. We conclude that the Italian HPAI viruses arose
from low pathogenicity strains, and that a deletion in the NA stalk followed by
the acquisition of additional glycosylation near the receptor binding site of
HA1 may be an adaptation of H7 viruses to a new host species i.e. domestic
poultry.
Descriptors: fowl plague virology, hemagglutinins viral
genetics, influenza A virus avian genetics, neuraminidase genetics, poultry
diseases virology, amino acid motifs, amino acid sequence, birds virology,
chickens virology, disease outbreaks, evolution, molecular, fowl plague
epidemiology, genes, structural, viral, glycosylation, influenza A virus avian
isolation and purification, influenza A virus avian pathogenicity, Italy
epidemiology, molecular sequence data, phylogeny, poultry diseases
epidemiology, protein processing, post translational, sequence deletion,
sequence homology, turkeys virology, virulence genetics.
Bano, S., K. Naeem, and S.A. Malik (2003). Evaluation
of pathogenic potential of avian influenza virus serotype H9N2 in chickens.
Avian Diseases 47(Special Issue): 817-822. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Recently seven isolates of avian influenza
virus (AIV) serotype H9N2 recovered from an outbreak of AI were analyzed on the
basis of their biological and molecular characteristics. All the isolates
belonged to the low-pathogenicity group of AIV. To further evaluate their
pathogenic potential in association with other organisms, an isolate was
inoculated experimentally in chickens using different routes and subsequently
challenged with infectious bronchitis virus, Ornithobacterium rhinotracheale
or Escherichia coli. The virus isolation and seromonitoring data
revealed a significant role of Escherichia coli in aggravating the
clinical condition of the birds earlier infected with AIV (H9N2). The
AIV-antigen was detected in lung, trachea, kidney, and cloacal bursa among the
infected birds, using immunofluorescent antibody technique. In another
experiment, chickens that were immunosuppressed chemically showed high
mortality when challenged with AIV H9N2. The results indicated that this low
pathogenicity AIV (H9N2) isolate could produce severe infection depending on
the type of secondary opportunistic pathogens present under field conditions.
This may explain the severity of infection with the present H9N2 outbreak in
the field. A prolonged antibacterial therapy in flocks infected with AIV H9N2
and use of oil-based vaccine at an early age in new flocks has helped to control
this infection and the disease.
Descriptors: epidemiology, infection, avian influenza,
infectious disease, respiratory system disease, viral disease,
immunofluorescence, immunologic techniques, laboratory techniques, viral
isolation, disease outbreak, secondary opportunistic pathogens, seromonitoring
data.
Barich, N.L., E.A. Evteeva, and N.V. Kaverin (1992). Svoistva
vnutrikletochnykh virus-spetsificheskikh ribonukleoproteidov, soderzhashchikh
negativnye i pozitivnye RNK virusagrippa A. [Properties of intracellular
virus-specific ribonucleoproteins containing negative and positive hepatitis A
virus RNA]. Molekuliarnaia Genetika, Mikrobiologiia i Virusologiia
(9-10): 15-9. ISSN: 0208-0613.
NAL
Call Number: QH506.M65F2
Abstract: The characteristics of the intracellular
virus-specific nucleocapsids containing either a negative or a positive RNA
strand were studied. The immunosorption of nucleocapsids by the monoclonal
antibodies against the three epitopes of NP protein failed to reveal any
antigenic difference between the negative strand or positive strand-containing
nucleocapsids. On the other hand, the sensitivity of virus-specific RNA in the
nucleocapsids to digestion by the pancreatic ribonuclease proved to be lower
for the positive strand-containing nucleocapsids.
Descriptors: influenza A virus avian genetics, RNA viral
chemistry, ribonucleoproteins analysis, chick embryo, epitopes immunology,
ribonucleoproteins immunology.
Barry, R.D. and P. Davies (1970). The effects of
UK2054 on the multiplication of influenza viruses. Journal of Hygiene
68(1): 151-8. ISSN: 0022-1724.
NAL
Call Number: 449.8 J82
Descriptors: isoquinolines pharmacology, orthomyxoviridae
drug effects, chick embryo, fetal membranes, hemagglutination tests, immune
sera, influenza A virus avian drug effects, orthomyxoviridae growth and
development, virus inhibitors pharmacology.
Basak, S. and R.W. Compans (1983). Studies on the
role of glycosylation in the functions and antigenic properties of influenza
virus glycoproteins. Virology 128(1): 77-91. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The biological and antigenic roles of
glycosylation were investigated in the influenza hemagglutinin (HA)
glycoprotein using the glycosylation inhibitor tunicamycin (TM). Under conditions
where only the nonglycosylated form of HA was detected by immunoprecipitation
and gel electrophoresis, the migration of glycoproteins to the cell surface was
observed by immunofluorescence using either monospecific or monoclonal antibody
to the HA polypeptide. Analysis of the surface fluorescence in TM-treated
infected cells by a fluorescence-activated cell sorter (FACS) showed that all
cells exhibited fluorescence in the complete absence of glycosylation. The
relative amount of HA antigen on cell surfaces was found to be reduced by only
30-40% in TM-treated cells, and this reflected a similar reduction in
intracellular synthesis. Electron microscopic studies using ferritin labeling
also demonstrated that the nonglycosylated HA glycoprotein was present in
significant amounts on surfaces of infected cells. Virions with nonglycosylated
glycoproteins were purified, and were found to have an approximate 30-fold
decrease in both hemagglutinin and neuraminidase specific activities. The
possible role of oligosaccharides in antigenic variation among various H1N1
strains was investigated. Immunoprecipitation reactions involving five
different monoclonal antibodies and five antigenic variants of A/USSR/90/77
revealed no major antigenic differences between the glycosylated and
nonglycosylated forms of HA.
Descriptors: cell membrane analysis, hemagglutinins viral
analysis, influenza A virus avian analysis, human analysis, antibodies,
monoclonal immunology, antibodies, viral immunology, epitopes immunology, hemagglutination,
viral, hemagglutinin glycoproteins, influenza virus, hemagglutinins viral
immunology, neuraminidase metabolism, tunicamycin pharmacology.
Bashiruddin, J.B., A.R. Gould, and H.A. Westbury
(1992). Molecular pathotyping of two avian influenza viruses isolated during
the Victoria 1976 outbreak. Australian Veterinary Journal 69(6):
140-2. ISSN: 0005-0423.
NAL
Call Number: 41.8 Au72
Descriptors: chickens, disease outbreaks veterinary, fowl
plague microbiology, influenza A virus avian classification, RNA viral
analysis, amino acid sequence, base sequence, DNA, viral chemistry, fowl plague
epidemiology, hemagglutinins viral chemistry, hemagglutinins viral genetics,
influenza A virus avian genetics, molecular sequence data, polymerase chain
reaction, viral chemistry, Victoria epidemiology.
Baum, L.G. and J.C. Paulson (1990). Sialyloligosaccharides
of the respiratory epithelium in the selection of human influenza virus
receptor specificity. Acta Histochemica. Supplement Band 40:
35-8. ISSN: 0567-7556.
NAL
Call Number: 384 AC8
Abstract: Human H3 strains of influenza A virus
preferentially bind cell-surface oligosaccharides containing the sequence NeuAc
alpha 2,6Gal, while avian influenza strains preferentially recognize the
sequence NeuAc alpha 2,3Gal. The distribution of these two types of sialic acid
linkages on host respiratory epithelium, the target of influenza infection, may
be a factor in the selection of the different receptor specificities observed
in human and avian influenza strains. To examine the distribution of these two
structures on human tracheal epithelial cells, two sialic acid specific lectins
were used. The Sambucus nigra lectin (SNA), which recognizes the sequence NeuAc
alpha 2,6Gal/GalNac, primarily binds to the surface of the ciliated tracheal
epithelial cells, and only weakly binds to mucins in the surface goblet cells.
In contrast, the Maackia amurensis lectin (MAL), which is specific for the
NeuAc alpha 2,3Gal sequence, binds strongly to mucus droplets in goblet cells,
but not to the surface of ciliated cells. Thus, human ciliated tracheal cells
appear to contain sialyloligosaccharides preferentially recognized by human
influenza strains. These findings suggest that human H3 influenza strains may
have evolved a receptor specificity which favors binding to ciliated cells, and
minimizes binding inhibition by respiratory mucus.
Descriptors: influenza A virus human metabolism,
oligosaccharides metabolism, receptors, virus metabolism, trachea
ultrastructure, epithelial cells, epithelium metabolism, epithelium
ultrastructure, fluorescent antibody technique, fluorescent dyes diagnostic
use, histocytochemistry, protein binding, receptors, virus ultrastructure,
trachea cytology, trachea metabolism.
Bean, W.J. (1984). Correlation of influenza A
virus nucleoprotein genes with host species. Virology 133(2):
438-42. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The RNAs coding for the nucleoproteins of a
panel of influenza isolates from human and nonhuman hosts were compared by
RNA-RNA hybridization to determine the extent of genetic diversity of this
protein and to determine if related nucleoproteins (NP) are consistently found
in viruses from certain hosts. Five nucleoprotein groups were defined. Group 1
contains nearly all of the avian influenza viruses, group 2 includes only
certain viruses isolated from gulls, group 3 includes all recent equine
influenza strains, group 4 contains only equine/Prague/1/56, and group 5
contains all human and swine influenza isolates. The maintenance of specific
nucleoproteins in viruses from certain species suggests that these proteins
have evolved functionally significant differences that favor their replication
in a specific host.
Descriptors: cell transformation, viral, genes,
structural, genes viral, influenza A virus genetics, nucleoproteins genetics,
human genetics, porcine genetics, nucleic acid hybridization, RNA viral
genetics, species specificity.
Bean, W.J., Y. Kawaoka, J.M. Wood, J.E. Pearson, and
R.G. Webster (1985). Characterization of virulent and avirulent
A/chicken/Pennsylvania/83 influenza A viruses: potential role of defective
interfering RNAs in nature. Journal of Virology 54(1): 151-60. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: In April 1983, an influenza virus of low
virulence appeared in chickens in Pennsylvania. Subsequently, in October 1983,
the virus became virulent and caused high mortality in poultry. The causative
agent has been identified as an influenza virus of the H5N2 serotype. The
hemagglutinin is antigenically closely related to tern/South Africa/61 (H5N3)
and the neuraminidase is similar to that from human H2N2 strains (e.g.,
A/Japan/305/57) and from some avian influenza virus strains (e.g.,
A/turkey/Mass/66 [H6N2]). Comparison of the genome RNAs of chicken/Penn with
other influenza virus isolates by RNA-RNA hybridization indicated that all of
the genes of this virus were closely related to those of various other
influenza virus isolates from wild birds. Chickens infected with the virulent
strain shed high concentrations of virus in their feces (10(7) 50% egg
infective dose per g), and the virus was isolated from the albumin and yolk of
eggs layed just before death. Virus was also isolated from house flies in
chicken houses. Serological and virological studies showed that humans are not
susceptible to infection with the virus, but can serve as short-term mechanical
carriers. Analysis of the RNA of the viruses isolated in April and October by
gel migration and RNA-RNA hybridization suggested that these strains were very
closely related. Oligonucleotide mapping of the individual genes of virulent
and avirulent strains showed a limited number of changes in the genome RNAs,
but no consistent differences between the virulent and avirulent strains that could
be correlated with pathogenicity were found. Polyacrylamide gel analysis of the
early (avirulent) isolates demonstrated the presence of low-molecular-weight
RNA bands which is indicative of defective-interfering particles. These RNAs
were not present in the virulent isolates. Experimental infection of chickens
with mixtures of the avirulent and virulent strains demonstrated that the
avirulent virus interferes with the pathogenicity of the virulent virus. The
results suggest that the original avirulent virus was probably derived from
influenza viruses from wild birds and that the virulent strain was derived from
the avirulent strain by selective adaptation rather than by recombination or
the introduction of a new virus into the population. This adaptation may have
involved the loss of defective RNAs, as well as mutations, and thus provides a
possible model for a role of defective-interfering particles in nature.
Descriptors: chickens microbiology, influenza A virus
avian pathogenicity, RNA viral analysis, antigens, viral analysis, defective
viruses genetics, Diptera microbiology, ducks microbiology, avian
genetics, avian immunology, swine microbiology, viral interference, virus
replication.
Bean, W.J., S.C. Threlkeld, and R.G. Webster (1989). Biologic
potential of amantadine-resistant influenza A virus in an avian model. Journal
of Infectious Diseases 159(6): 1050-6.
ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: Amantadine has been accepted for both the
treatment and prophylaxis of influenza A virus infections. Although
amantadine-resistant mutants have been shown to be readily generated both in
the laboratory and in children treated with rimantadine, little is known about
their biologic properties, such as genetic stability, transmissibility, or
pathogenicity, compared with the parental virus. This study examined these
properties using an avian influenza virus, A/chicken/Pennsylvania/1370/83
(H5N2). Variants that were amantadine-resistant, virulent, and capable of
competing with wild-type virus for transmission to susceptible hosts in the
absence of the drug were selected. These amantadine-resistant variants were
also genetically stable, showing no reversion to wild-type after six passages
in birds over a period of greater than 20 d. Thus, these virus variants had no
detectable biologic impairment. The mutations conferring drug resistance were
in the M2 polypeptide and were identical to mutations previously described in
human amantadine-resistant virus. These results suggest that resistant mutants
may have the potential to threaten the effective use of amantadine and
rimantadine for the control of epidemic influenza.
Descriptors: amantadine pharmacology, fowl plague
microbiology, influenza A virus avian drug effects, amantadine therapeutic use,
chickens, drug resistance, microbial, fowl plague drug therapy, fowl plague
transmission, avian genetics, avian pathogenicity, mutation, RNA viral
genetics, virulence.
Beard, C.W., M. Brugh, and R.G. Webster (1987). Emergence
of amantadine-resistant H5N2 avian influenza virus during a simulated layer
flock treatment program. Avian Diseases 31(3): 533-7. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: An experiment was designed to simulate field
conditions in which preventive treatment is not initiated until after some
chickens in a flock are infected with avian influenza (AI). Twelve hens began
to receive amantadine hydrochloride on the day they were inoculated (day 0)
with highly pathogenic AI virus, A/chicken/Pa/1370/83. These hens remained
clinically normal through 8 days postinoculation (PI), but five died after day
9; mean death time (MDT) was 18 days. Three of 12 hens given amantadine
beginning 1 day PI died (MDT 5.4 days), seven of 12 hens given amantadine
beginning 3 days PI died (MDT 3.7 days), and all 12 inoculated hens not given
amantadine died (MDT 4.9 days). The delayed mortality in the day 0 treatment
group was likely due not to the original inoculum but to the emergence of a
drug-resistant virus population. Virus isolated from a dead hen from that group
was resistant to the actions of amantadine in both in ovo and in vivo tests.
The lack of late mortality due to the drug-resistant virus in the day 1 and day
3 treatment groups, which were in close contact with the day 0 treatment group,
was attributed to their becoming infected before treatment with the drug and to
the development of protective immunity.
Descriptors: amantadine pharmacology, chickens, fowl
plague prevention and control, influenza A virus avian drug effects, amantadine
therapeutic use, chick embryo, drug resistance, microbial, fowl plague drug
therapy.
Becht, H. (1971). Cytoplasmic synthesis of an
arginine-rich nuclear component during infection with an influenza virus. Journal
of Virology 7(2): 204-7. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Descriptors: arginine metabolism, cultured cells
metabolism, cytoplasm metabolism, influenza A virus avian pathogenicity,
proteins biosynthesis, autoradiography, cell line, cell nucleus metabolism,
chick embryo, ethanol, fibroblasts, hamsters, hydrochloric acid, kidney,
precipitation, solvents, trichloroacetic acid, tritium.
Becht, H. (1969). Induction of an arginine-rich
component during infection with influenza virus. Journal of General
Virology 4(2): 215-20. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: arginine metabolism, influenza A virus avian
metabolism, tissue culture, autoradiography, cell nucleus metabolism, chick
embryo, cytoplasm metabolism, dactinomycin pharmacology, fibroblasts, leucine
metabolism, lysine metabolism, tritium, virus replication.
Becht, H. (1968). Properties of erythrocytes
stabilized with sulfosalicylic acid and their use in an indirect hemagglution test
with influenza virus RNP-antigen. Journal of Immunology 101(1):
18-22. ISSN: 0022-1767.
NAL
Call Number: 448.8 J8232
Descriptors: antigens, erythrocytes, hemagglutination
tests, indicators and reagents, orthomyxoviridae, salicylic acids, sulfonic acids,
complement fixation tests, immune sera, influenza A virus avian,
nucleoproteins, sheep.
Becht, H. (1971). Untersuchungen uber die
Biosynthese und uber den serologischen Nachweis des Ribonucleoproteid-Antigens
von Influenzaviren. I. Untersuchungen uber die Bildung des RNP-Antigens und die
Rolle des Zellerns bei seiner Synthese. [Studies on biosynthesis and
serological demonstration of ribonucleoprotein antigen of influenza viruses. I.
Studies on biosynthesis of RNP antigen and the role of cell nucleus in its
synthesis]. Zeitschrift Fur
Medizinische Mikrobiologie Und Immunologie 156(4): 309-30. ISSN: 0044-3077.
NAL
Call Number: 449.8 Z3
Descriptors: antigens biosynthesis, influenza A virus
avian immunology, antigens, viral biosynthesis, arginine, autoradiography, AZO
compounds pharmacology, cell nucleus metabolism, chick embryo, fibroblasts,
hemagglutinins viral biosynthesis, membranes, nucleoproteins biosynthesis,
ribose, serotyping, viral proteins biosynthesis.
Becht, H. and R. Drzeniek (1968). The effect of
azo dyes on myxovirus neuraminidase and on virus multiplication. Journal
of General Virology 2(2): 261-8.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: azo compounds pharmacology, influenza A virus
avian drug effects, neuraminidase antagonists and inhibitors, Newcastle disease
virus drug effects, arboviruses drug effects, arboviruses growth and
development, chick embryo, complement fixation tests, Congo red pharmacology,
hemagglutination tests, avian growth and development, neuraminidase metabolism,
Newcastle disease virus growth and development.
Becht, H., H. Gruschkau, and R. Rott (1979). The M
protein of influenza viruses has no immunizing effect. Medical
Microbiology and Immunology 167(4): 285-8.
ISSN: 0300-8584.
Abstract: Influenza A virus M protein was prepared by
electrophoresis in SDS polyacrylamide gel from virus particles which had been
pretreated with octylglucoside to remove the surface glycoproteins; M antigens
from the influenza virus strains A/Victoria/3/75 (H3N2), A/FPV/Rostock (Hav1N1)
and A/chick/Germany/49 (Hav2Neq1) did not protect mice against a lethal
challenge infection with the virulent Victoria strain.
Descriptors: antigens, viral immunology, influenza A virus
avian immunology, human immunology, viral proteins immunology, antibodies,
viral biosynthesis, hemagglutination inhibition tests, immunization, influenza
immunology, influenza prevention and control, mice.
Becht, H. and B. Malole (1975). Comparative
evaluation of different fixation procedures and different coupling reagents for
the demonstration of influenza virus-specific antibodies by the indirect
hemagglutination test. Medical Microbiology and Immunology 162(1):
43-53. ISSN: 0300-8584.
Abstract: The indirect hemagglutination technique has
been improved by fixing the carrier erythrocytes successively with
glutaraldehyde and sulfosalicylic acid. Sensitization by covalent conjugation
of influenza virus antigens to the erythrocytes with various coupling reagents,
which resulted in stable and highly sensitive test cells, has been defined. An
economical affinity chromatography procedure using antibody-coated agarose has
been developed to prepare sufficiently pure antigens from fowl plague virus-infected
choriollantoic membranes.
Descriptors: antibodies, viral analysis, erythrocytes
immunology, hemagglutination tests methods, antibody specificity, blood
preservation, chromatography, affinity, cytological techniques, glutaral,
hemagglutinins viral isolation and purification, influenza A virus avian
immunology, salicylic acids.
Becht, H., R. Rott, and H.D. Klenk (1972). Effect
of Concanavalin A on cells infected with enveloped RNA viruses. Journal
of General Virology 14(1): 1-8.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: agglutination drug effects, lectins
pharmacology, RNA viruses, agglutination tests, arboviruses, cattle, cell line,
cell membrane drug effects, cultured cells microbiology, chick embryo,
concanavalin A pharmacology,
fibroblasts, hamsters, HeLa cells microbiology, influenza A virus avian,
kidney, cell line microbiology, Newcastle disease virus, orthomyxoviridae,
polioviruses, Semliki Forest virus, simian virus 40, sindbis virus, vesicular
stomatitis Indiana virus, virus diseases.
Bektemirov, T.A., S.A. Moisiadi, E.N. Kantorovich,
N.V. Kaverin, and O.N. Berezina (1974). Nekotorye biologicheskie svoistva
"nepol'nogo" virusa grippa. [Biological properties of
"incomplete" influenza virus]. Voprosy Virusologii (2):
181-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: defective viruses pathogenicity, orthomyxoviridae
pathogenicity, influenza A virus avian, interferons biosynthesis, mice, viral
interference, virus replication.
Belshe, R.B. (1995). A review of attenuation of
influenza viruses by genetic manipulation. American Journal of
Respiratory and Critical Care Medicine 152(4, Pt. 2): S72-5. ISSN: 1073-449X.
Descriptors: genetic engineering methods, influenza A
virus human genetics, influenza B virus genetics, influenza vaccine genetics,
adult, infant, avian immunology, human immunology, human pathogenicity,
influenza B virus immunology, influenza B virus pathogenicity, influenza
vaccine immunology, vaccines, attenuated genetics, vaccines, attenuated
immunology, vaccines, combined genetics,
vaccines, combined immunology.
Bergelson, L.D., A.G. Bukrinskaya, N.V. Prokazova,
G.I. Shaposhnikova, S.L. Kocharov, V.P. Shevchenko, G.V. Kornilaeva, and E.V.
Fomina Ageeva (1982). Role of gangliosides in reception of influenza virus.
European Journal of Biochemistry FEBS 128(2-3): 467-74. ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: The ganglioside composition of Ehrlich
ascites carcinoma (EAC) cells and the role of the individual gangliosides in
binding and penetration into the cell of influenza virus were determined. EAC
gangliosides identical with or close to GM3, GM2, GM1, GT1a and GT1b were
characterized by thin-layer chromarography, compositional analyses, methylation
analysis and mass-spectrometry. The ganglioside uptake capacity of native and
neuraminidase-treated EAC cells was studied with tritium-labeled gangliosides
of definite structure and the binding of influenza virus to cells was
determinated by using [3H]uridine-labeled virus and by hemagglutination
studies. Treatment of the cells with Vibrio cholerae neuraminidase largely
decreased binding of the virus. Exogenous gangliosides with a terminal
galactose unit or a penultimate galactose masked by neuraminic acid were able
to restore the virus-binding capacity of neuraminidase-treated cells, however,
the main ganglioside of EAC cells, GM2, which carbohydrate chain is terminated
by N-acetylgalactosamine, was completely ineffective. The common carbohydrate
sequence of the gangliosides showing binding activity (formula; see text) is
proposed to be the main recognition structure of the influenza virus receptor
on the surface of EAC cells. Penetration of labeled influenza virus into the
nuclei of EAC cells was evaluated by measuring the radioactivity of the nuclei
of neuraminidase-treated ganglioside-loaded cells after exposition to the
labeled virus. Of all gangliosides tested only trisialogangliosides of the GT1b
type were able to induce increased entry of the virus into the cells and
accumulation of its radioactive component into the nuclei. It is suggested that
GT1b gangliosides react specifically with the virus protein responsible for
membrane fusion (apparently the hemagglutinin HA2 subunit) and thus are
involved in virus penetration and delivery of the virus genome to the nuclei.
Descriptors: carcinoma, ehrlich tumor microbiology,
gangliosides metabolism, influenza A virus avian physiology, receptors, virus
metabolism, carbohydrate sequence, hemagglutination tests, kinetics, mice,
neuraminidase pharmacology, receptors, virus drug effects, structure activity
relationship, vibrio cholerae enzymology.
Berting, A., C. Fischer, S. Schaefer, W. Garten, H.D.
Klenk, and W.H. Gerlich (2000). Hemifusion activity of a chimeric influenza
virus hemagglutinin with a putative fusion peptide from hepatitis B virus. Virus
Research 68(1): 35-49. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: Entry of enveloped viruses is often mediated
by an aminoterminal hydrophobic fusion peptide of a viral surface protein. The
S domain of the hepatitis B virus surface protein contains a putative fusion
peptide at position 7-18, but no systems are available to study its function
directly. We tested the functionality of this peptide and a related peptide
from another hepadnavirus in the context of the well-characterized influenza
virus hemagglutinin H7 using gene mutation. The chimeric hemagglutinins could
be expressed stably in CV 1 cells and were transported to the cell surface. The
chimeras were incompletely cleaved by cellular proteases but cleavage could be
completed by trypsin treatment of the cells. The chimeras did not differ in
receptor binding, i.e. erythrocyte binding. Hemifusion and fusion pore
formation were detected with membrane or cytosolic fluorescent dye-labeled
erythrocytes as target structures of the hemagglutinin. Five of six different
chimeras mediated hemifusion in 20-54% of the hemagglutinin-expressing cells,
complete fusion and syncytium formation was not observed. The data suggest that
the sequence 7-18 of the hepatitis B S domain may indeed initiate the first
step of viral entry, i.e. hemifusion.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, hepatitis B virus metabolism, membrane fusion, viral fusion
proteins metabolism, amino acid sequence, cell line, chimeric proteins
genetics, chimeric proteins metabolism, hemagglutinin glycoproteins, influenza
virus genetics, hepatitis B virus genetics, molecular sequence data, peptides
chemistry, peptides genetics, receptors, virus metabolism, viral fusion
proteins chemistry, viral fusion proteins genetics.
Betakova, T., F. Ciampor, and A.J. Hay (2005). Influence
of residue 44 on the activity of the M2 proton channel of influenza A virus.
Journal of General Virology 86(Pt. 1): 181-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The influenza A virus M2 proton channel plays
a role in two stages of virus replication. The proteins of two closely related
strains of the avian H7 subtype of influenza A virus, Rostock and Weybridge,
were found to differ in their pH-modulating activities and activation
characteristics. Of three amino acid differences at residues 27, 38 and 44
within the membrane-spanning domain, substitution at residue 44 was necessary
and sufficient to account for differences in trans-Golgi pH-modulating
activity, whereas changes in all three were required to switch the activation
characteristics of the Weybridge M2 to those of the Rostock M2. These results
not only separate the two phenomena genetically, but also indicate that the
'unique' activation characteristics of the Rostock M2 channel were selected
specifically. In addition, they point to the importance of functional
complementarity between the activation characteristics of the M2 channel and
the pH of membrane fusion by haemagglutinin during virus entry.
Descriptors: influenza A virus, avian metabolism, ion
channels metabolism, viral matrix proteins metabolism, amino acid sequence,
cell line, Golgi apparatus chemistry, Golgi apparatus metabolism,
hemagglutinins, viral metabolism, hydrogen-ion concentration, ion channels
chemistry, molecular sequence data, protein structure, tertiary, protons,
sequence alignment, viral matrix proteins chemistry, virus replication.
Blagoveshchenskaya, O.V. and Y.Z. Ghendon (1978). Comparative
study of virion transcriptase of some influenza virus strains. Acta
Virologica 22(2): 97-103. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The activities, the temperature and pH optima
of in vitro functioning and stability upon heating of virion transcriptase of
10 human influenza virus A strains differing in reactogenicity and isolated in
different epidemiological situations, and of fowl plague virus (FVP) were
compared. As compared with virion transcriptase of human influenza virus
strains studied, that of FPV had a higher pH optimum, was capable of
functioning in vitro at a higher temperature and was more stable on heating.
Freshly isolated and vaccine influenza virus strains on the one hand and
strains isolated at the peak and in the end of an epidemic did not differ in
the virion transcriptase properties. The virion transcriptase of a strain
isolated from a local influenza outbreak was much less active than
transcriptase of a highly epiedmic strain.
Descriptors: influenza A virus avian enzymology, human
enzymology, RNA nucleotidyltransferases metabolism, RNA replicase metabolism,
heat, hydrogen-ion concentration, influenza vaccine, species specificity,
temperature, virion enzymology.
Blinov, V.M., O.I. Kiselev, S.M. Resenchuk, A.I.
Brovkin, A.G. Bukrinskaia, and L.S. Sandakhchiev (1993). Analiz
potentsial'nykh uchastkov rekombinatsii v genakh gemaggliutinina virusov grippa
zhivotnykh v otnoshenii ikh adaptatsii k novomu khoziainu--cheloveku. [An
analysis of the potential areas of recombination in the hemagglutinin genes of
animal influenza viruses in relation to their adaptation to a new host--man].
Voprosy Virusologii 38(6): 263-8.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The authors tried to decode the mechanism of
influenza viruses species adaptation in the process of host changing. The
functionally important replacement in the surface pocket domains were revealed,
particularly in the conservative region 221-241, involving fibronectin-like
part. Close replacements were revealed in the region 141-161. The method of
construction of heteroduplexes between hemagglutinin RNA of duck, pig, and
human viruses was used. The method showed that all heteroduplexes formed
recombinogene structures. An unexpected effect of directional recombination was
elicited for hemagglutinin RNA heteroduplexes in cases of duck-pig and
human-pig viruses. During the directional recombination the following processes
took place: the receptor-binding site of animal type was transmitted to the
duck virus, while the human receptor-binding site was transmitted to the pig
virus. According to the experimental data, a new hypothesis is formulated: the
cascade mechanism of directional recombination for duck, animal and human
viruses makes it possible for the recombinant viruses to overcome interspecies
barriers.
Descriptors: adaptation, physiological genetics, genes
viral genetics, hemagglutinins viral genetics, influenza A virus avian
genetics, porcine genetics, recombination, genetic genetics, amino acid
sequence, ducks microbiology, human genetics, molecular sequence data, nucleic acid heteroduplexes genetics, RNA
viral genetics, swine microbiology, variation genetics genetics.
Blinova, V.K., R.Y. Podchernyaeva, and M.I. Sokolov
(1975). K voprosu rekombinatsii virusov grippa cheloveka i dikikh ptits.
[Recombination of influenza viruses from man and wild birds (terns)]. Sbornik
Trudov Institut Virusologii Imeni D.I. Ivanovskogo, "Ekologiya
Virusov" (3): 31-35.
Descriptors: influenza viruses, wild birds, terns, humans,
virus recombination.
Bogautdinov, Z.F. (1977). Fermentingibiruyushchaya
aktivnost spetsificheskoi syvorotki k neiraminidaze virusa grippa ptitsy.
[Enzyme inhibiting activity of specific serum against the neuraminidase of
avian influenza virus]. Doklady Vsesoyuznoi Akademii
Sel'Skokhozyaistvennykh Nauk (4): 29-30.
Descriptors: avian influenza virus, DEAE cellulose,
neuraminidase, chromatography.
Bogautdinov, Z.F. (1977). Immunoenzymology of the
neuraminidase of avian influenza virus complexed with a substrate and
antibodies. Soviet Agricultural Sciences (10): 39-41. ISSN: 0735-2700.
NAL
Call Number: S1.S68
Descriptors: avian influenza virus, neuraminidase,
immunoenzymology, antibodies.
Bogautdinov, Z.F. and I.G. Lavrova (1976). Izuchenie
svyazi mezhdu antigennoi spetsifichnost'yu i fiziko-khimicheskimi svoistvami
neiraminidaz. [Relationship between antigenic specificity and physico-chemical
properties of neuraminidases of avian influenza viruses]. Doklady
Vsesoyuznoi Akademii Sel'Skokhozyaistvennykh Nauk (1): 37-38.
Descriptors: avian influenza viruses, neuraminidase,
antigens, physio-chemical properties, techniques.
Bonin, J. and C. Scholtissek (1983). Mouse
neurotropic recombinants of influenza A viruses. Archives of Virology
75(4): 255-68. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Recombinants with known gene constellations
between fowl plague virus (FPV) and various prototype influenza virus strains
have been examined for neurovirulence in suckling mice. Strongly neurotropic
recombinants were obtained from crosses between FPV and the strains virus N,
Hong Kong, and PR8, but not between FPV and equi 2 or swine viruses. All highly
neurotropic recombinants had RNA segment 4 (HA) derived from FPV and RNA
segment 2 (Ptra gene) from the other prototype strain. The derivation of two other
RNA segments of the polymerase complex, namely RNA segments 3 (Pol 2) and 5
(NP) and also segment 8 (NS) can modulate these properties. For example, if in
recombinants between FPV and virus N in addition to RNA segment 2 also RNA
segments 3 and/or 8 are derived from virus N, neurovirulence is further
enhanced, while replacement of RNA segment 5 of FPV by the corresponding
segment of virus N decreases or abolishes neurovirulence. The derivation of the
other genes does not seem to be relevant for neurovirulence in the crosses
mentioned above. Of the prototype strains tested, the turkey England (t. Engl.)
strain is the only one which was highly neurotropic for suckling mice.
Recombinants between FPV and t. Engl. which have kept the HA gene of t. Engl. were
still neurotropic, while those with the HA gene of FPV were completely
avirulent. The results obtained demonstrated that 1. the creation of influenza
virus recombinants neurotropic for mice is not a rare event; 2. one of the
parents should multiply well in mouse lungs; 3. the presence of a cleavable
hemagglutinin is necessary, but not sufficient. In the pair FPV/turkey England
the hemagglutinin of turkey England seems to determine neurovirulence.
Descriptors: influenza A virus, genetics, recombination, genetic,
brain microbiology, cultured cells, embryo microbiology, fibroblasts, genes
viral, avian genetics, pathogenicity, kidney, lung microbiology, mice,
virulence.
Borek, A. and C. Sauter (1975). Fowl plague virus
adapted to human leukemia cells: interaction with normal human leukocytes and
plastic surfaces. Pathologia Et Microbiologia 43(1): 62-73. ISSN: 0031-2959.
NAL
Call Number: 448.8 Sch9
Abstract: An avian influenza A virus which grows well
in human leukemic myeloblasts was unable to replicate in normal human
leukocytes. The virus adhered during the first hours of incubation to plastic
surfaces and to leukocytes and was then released into the supernatant; care
should be taken not to confuse this with viral growth.
Descriptors: influenza A virus, avian growth and
development, leukocytes microbiology, adaptation, physiological, adsorption,
adult, cell adhesion, granulocytes microbiology, leukemia, myelocytic, acute,
lymphocytes microbiology, monocytes microbiology, plastics, tissue culture, virus
replication.
Borland, R. and B.W. Mahy (1968). Deoxyribonucleic
acid-dependent ribonucleic acid polymerase activity in cells infected with
influenza virus. Journal of Virology 2(1): 33-9. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Descriptors: DNA, viral metabolism, fibroblasts
enzymology, influenza A virus avian metabolism, RNA biosynthesis, RNA
nucleotidyltransferases biosynthesis, chick embryo, dactinomycin pharmacology,
hemagglutination, viral, RNA viral biosynthesis, tissue culture, virus replication.
Borland, R. and B.W. Mahy (1970). RNA and protein
synthesis in chick embryo lung cell monolayer cultures infected with influenza
virus. Archiv Fur Die Gesamte Virusforschung 30(4): 367-78. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: cytopathogenic effect, viral, lung
metabolism, orthomyxoviridae pathogenicity, proteins biosynthesis, RNA
biosynthesis, tissue culture, carbon isotopes, centrifugation, density
gradient, chick embryo, dactinomycin pharmacology, hemadsorption, hemagglutination,
influenza A virus avian growth and development, avian pathogenicity, lung
pathology, orthomyxoviridae growth and development, species specificity,
sucrose, tritium, uridine metabolism, valine metabolism, virus replication.
Bosch, F.X. (1985). Studies on the development of
the charge heterogeneity of the influenza virus glycoproteins. Archives
of Virology 83(3-4): 311-7. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The heterogeneity in charge of the influenza
virus glycoproteins, hemagglutinin (HA) and neuraminidase (NA) is retained,
when glycosylation is inhibited by tunicamycin (TM) or 2-deoxyglucose (2-dg).
This is in contrast to the charge heterogeneity of the G protein of vesicular
stomatitis virus (VSV), which is mainly due to heterogeneous sulfation of the
carbohydrate side chains and therefore is abolished by the above mentioned
inhibitors of glycosylation. Thus, the charge heterogeneity of influenza virus
glycoproteins might be attributable to some as yet unidentified modifications
of the polypeptide backbone.
Descriptors: hemagglutinins viral, influenza A virus avian
analysis, membrane glycoproteins, neuraminidase, viral envelope proteins, viral
proteins, cultured cells, chick embryo, deoxyglucose pharmacology,
electrophoresis, polyacrylamide gel, hemagglutinin glycoproteins, influenza
virus, avian enzymology, avian metabolism, human analysis, isoelectric
focusing, isoelectric point, translation, genetic, tunicamycin pharmacology,
vesicular stomatitis Indiana virus analysis.
Bosch, F.X., W. Garten, H.D. Klenk, and R. Rott
(1981). Proteolytic cleavage of influenza virus hemagglutinins: primary
structure of the connecting peptide between HA1 and HA2 determines proteolytic
cleavability and pathogenicity of Avian influenza viruses. Virology
113(2): 725-35. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: hemagglutinins viral analysis, influenza A
virus avian immunology, peptide hydrolases metabolism, amino acid sequence,
human immunology, human pathogenicity, isoelectric point.
Bosch, F.X., A. Mayer, and R.T. Huang (1980). Simple
and rapid separation of ortho- and paramyxovirus glycoproteins. Medical
Microbiology and Immunology 168(4): 249-59.
ISSN: 0300-8584.
Abstract: The hemagglutinin (HA) and neuraminidase (NA)
of influenza viruses, as well as the fusion protein (F) and
hemagglutinin-neuraminidase (HN) of paramyxoviruses, have been separated in
native form using a two-step procedure. The glycoproteins are efficiently
extracted from virions using the on-ionic detergent octyl-beta-D-glucoside and
are then applied to a column of agarose beads coupled with tyrosine-sulfanilic
acid. Pure HA and F are obtained in good yield in the flow-through from this
column. NA and HN bind strongly and can be eluted, albeit somewhat contaminated
with HA or F, by raising the pH of the column buffer. The separated
non-denatured fractions can be used for structural, functional, and antigenic
studies.
Descriptors: glycoproteins isolation and purification,
influenza A virus avian analysis, human analysis, Newcastle disease virus
analysis, viral proteins isolation and purification, chromatography, affinity,
detergents, hemagglutinins viral isolation and purification, neuraminidase
isolation and purification.
Bosch, F.X., M. Orlich, G. Legler, R.T. Schwarz, and
R. Rott (1984). Effect of inhibitors of glycosylation on proteolytic
activation of avian influenza virus hemagglutinins: discrimination between
tryptic cleavage and elimination of the connecting peptide. Virology
132(1): 199-204. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The glycosylation inhibitors tunicamycin
(TM), 2-deoxyglucose (2-dg), bromoconduritol (BC; 3,5/4,6-6-bromo
3,4,5-trihydroxycyclohex-1-ene), and N-methyl-deoxynojirimycin (MdN) have been
used to study the role of glycosylation in the two proteolytic reactions
involved in the biological activation of H7 influenza virus hemagglutinins
(HAs): trypsinlike cleavage and subsequent elimination of the connecting
peptide. The results obtained revealed that trypsin-like cleavage of the HAs of
pathogenic strains does not require glycosylation, since these HAs were
efficiently cleaved in the presence of TM and 2-dg. The elimination of the
connecting peptide between HA1 and HA2, however, appears to require the transfer
of oligosaccharides onto the HA polypeptide, since this activity was blocked by
TM and by 2-dg. Elimination was not blocked by BC or MdN, which inhibit glucose
trimming and subsequent conversion of the high-mannose type to the complex type
of carbohydrate.
Descriptors: 1 deoxynojirimycin analogs and derivatives,
carbohydrates metabolism, hemagglutinins viral metabolism, influenza A virus
avian analysis, trypsin metabolism, deoxyglucose pharmacology, glucosamine
analogs and derivatives, glucosamine pharmacology, inositol analogs and
derivatives, inositol pharmacology, tunicamycin pharmacology, virion analysis.
Bosch, F.X., V. Von Hoyningen Huene, C. Scholtissek,
and R. Rott (1982). The overall evolution of the H7 influenza virus
haemagglutinins is different from the evolution of the proteolytic cleavage
site. Journal of General Virology 61(Pt. L): 101-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: It has been shown previously that the
pathogenicity of avian influenza A viruses depends strictly on the proteolytic
cleavability of their haemagglutinins (HAs) in infected cells. In this
communication, pathogenic and non-pathogenic strains of the H7 subtype have
been studied by comparing the genetic relatedness of their HA genes. Some of
the cleavable HAs of pathogenic strains were genetically more closely related
to the uncleaved HAs than to other cleavable HAs. These data clearly
demonstrate that the overall evolution of the H7 haemagglutinins is different
from the evolution of the specific cleavage site.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian immunology, evolution, hemagglutinins viral analysis,
avian genetics, avian pathogenicity, nucleic acid hybridization.
Bossart Whitaker, P., M. Carson, Y.S. Babu, C.D.
Smith, W.G. Laver, and G.M. Air (1993). Three-dimensional structure of
influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy
2,3-dehydro-N-acetyl neuraminic acid. Journal of Molecular Biology
232(4): 1069-83. ISSN: 0022-2836.
NAL
Call Number: 442.8 J8224
Abstract: We present here the three-dimensional
structure of neuraminidase (E.C. 3.2.1.18) from influenza virus
A/Tern/Australia/G70c/75 (N9), determined by the method of multiple isomorphous
replacement, and the structure of the neuraminidase complexed with an
inhibitor, 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid (DANA). Native and
inhibitor complex crystals are isomorphous and belong to space group I432 with
unit cell dimensions of 183.78 A. The native enzyme structure and the inhibitor
complex structure have been refined at 2.5 A and 2.8 A resolution,
respectively, with crystallographic R-factor values of 0.193 for the native
enzyme, and 0.179 for the inhibitor complex. The current enzyme model includes
387 amino acid residues which comprise the asymmetric unit. The
root-mean-square deviation from ideal values is 0.013 A for bond lengths and
1.6 degree for bond angles. The neuraminidase (NA), as proteolytically cleaved
from the virus, retains full enzymatic and antigenic activity, and is a
box-shaped tetramer with edge lengths of 90 A and a maximal depth of 60 A. The
NA tetramers are composed of crystallographically equivalent monomers related
by circular 4-fold symmetry. Each monomer folds into six antiparallel
beta-sheets of four strands. The secondary structure composition is 50%
beta-sheet. The remaining 50% of the residues form 24 strand-connecting loops
or turns. One of the loops contains a small alpha-helix. The structure of the
complex of NA with DANA, a transition state analog, has enabled us to identify
and characterize the site of enzyme catalysis. The center of mass of bound
inhibitor is 32 A from the 4-fold axis of the tetramer, lodged at the end of a
shallow crater of diameter 16 A with a depth of 8 to 10 A. There are 12 amino
acid residues that directly bind DANA, with a further six conserved amino acids
lining the active site pocket. The neuraminidase inhibitor complex provides a
three-dimensional model which will be used to further the understanding of
enzymatic hydrolysis and aid the design of specific, antineuraminidase
antiviral compounds.
Descriptors: influenza A virus avian enzymology,
neuraminidase antagonists and inhibitors, neuraminidase chemistry, sialic acids
chemistry, binding sites, influenza B virus enzymology, mercury chemistry,
models, molecular, molecular conformation, N-acetylneuraminic acid, platinum
chemistry, protein conformation, sialic acids metabolism, x-ray diffraction.
Brecht, H., U. Hammerling, and R. Rott (1971). Undisturbed
release of influenza virus in the presence of univalent antineuraminidase
antibodies. Virology 46(2): 337-43.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: antibodies, influenza A virus avian growth
and development, neuraminidase isolation and purification, neuraminidase
metabolism, orthomyxoviridae growth and development, centrifugation, density
gradient, chick embryo, chromatography, DEAE-cellulose, fibroblasts,
hemagglutination tests, immune sera, immunoglobulin g, immunoglobulins, avian
enzymology, avian immunology, avian pathogenicity, neuraminic acids
biosynthesis, orthomyxoviridae enzymology, orthomyxoviridae immunology,
orthomyxoviridae pathogenicity, rabbits, sucrose, tissue culture, virus
replication.
Breslin, J.J., L.G. Smith, and J.S. Guy (2001). Baculovirus
expression of turkey coronavirus nucleocapsid protein. Avian Diseases
45(1): 136-43. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The nucleocapsid (N) gene of turkey
coronavirus (TCV) was amplified by reverse transcriptase-polymerase chain
reaction, cloned, and expressed in the baculovirus expression system. A
recombinant baculovirus containing the TCV N gene (rBTCV/N) was identified by
polymerase chain reaction and expression of TCV N protein as determined by
western immunoblot analysis. Two TCV-specific proteins, 52 and 43 kDa, were
expressed by rBTCV/N; one of these proteins, p52, was comparable in size to
native TCV N protein. Baculovirus-expressed N proteins were used as antigen in
an indirect enzyme-linked immunosorbent assay (ELISA) for detection of
TCV-specific antibodies. The ELISA detected antibodies specific for TCV and
infectious bronchitis virus, a closely related avian coronavirus, but did not
detect antibodies specific for other avian viruses (avian influenza, avian
reovirus, avian paramyxovirus 3, avian adenovirus 1, or Newcastle disease
virus). These findings indicate that baculovirus-expressed TCV N protein is a
suitable source of antigen for ELISA-based detection of TCV-specific antibodies
in turkeys.
Descriptors: baculoviridae metabolism, nucleocapsid
biosynthesis, nucleocapsid proteins, turkeys virology, enteritis veterinary,
enteritis virology, enzyme linked immunosorbent assay veterinary, North
Carolina, nucleocapsid genetics, poultry diseases virology, reverse
transcriptase polymerase chain reaction veterinary.
Breuning, A. and C. Scholtissek (1986). A
reassortant between influenza A viruses (H7N2) synthesizing an enzymatically
inactive neuraminidase at 40 degrees which is not incorporated into infectious
particles. Virology 150(1): 65-74.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Cells infected with a reassortant (113/Ho,
H7N2) between A/fowl plague/Rostock/34 (FPV, H7N1) and A/Hong Kong/1/68 (H3N2)
carrying RNA segments 1 and 6 of the Hong Kong virus and the residual genes of
FPV, synthesized at 40 degrees a neuraminidase (NA) which is enzymatically not
active and which is not incorporated into infectious particles. At 40 degrees
NA accumulates in the rough endoplasmic reticulum. It contains mainly
carbohydrate side chains of the mannose type, and fucose is only scarcely
incorporated. At 33 degrees NA of the reassortant is overproduced, and at least
some of it is active and is incorporated into viral particles. Under
nonreducing conditions during PAGE its NA migrates to the same position as
after heating with mercaptoethanol, in contrast to the Hong Kong parent virus.
It is speculated that at 40 degrees the tetramerization of the NA in the rough
endoplasmic reticulum does not function, and in this way its migration to the
cytoplasmic membrane and its incorporation into infectious particles does not
occur. Since 113/Ho is as pathogenic for the chicken (body temperature of 41
degrees) as is FPV, the question arises which role the NA plays in virus
replication and spread in the infected organism.
Descriptors: influenza A virus avian genetics, human
genetics, neuraminidase genetics, carbohydrate sequence, cell compartmentation,
chick embryo, glycopeptides analysis, glycoproteins genetics, glycoproteins
metabolism, hemagglutinins viral genetics, avian enzymology, influenza A virus
human enzymology, mutation, neuraminidase metabolism, recombination, genetic,
temperature, viral proteins metabolism, virus replication.
Briedis, D.J., G. Conti, E.A. Munn, and B.W. Mahy
(1981). Migration of influenza virus-specific polypeptides from cytoplasm to
nucleus of infected cells. Virology 111(1): 154-64. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cell nucleus metabolism, cytoplasm
metabolism, influenza A virus avian metabolism, viral proteins metabolism,
capsid metabolism, cell fractionation, cell line, dogs, avian growth and
development, kinetics.
Bromley, P.A. and R.D. Barry (1973). Characterization
of the ribonucleic acid of fowl plague virus. Archiv Fur Die Gesamte
Virusforschung 42(2): 182-96. ISSN:
0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian analysis, RNA viral
analysis, autoradiography, base sequence,
centrifugation, density gradient, chick embryo, chromatography,
DEAE-cellulose, chromatography, gel, densitometry, electrophoresis,
polyacrylamide gel, influenza A virus avian isolation and purification, nucleic
acid denaturation, phosphorus isotopes, RNA viral isolation and purification,
ribonucleases, tissue culture, virus cultivation.
Bromley, P.A. and R.D. Barry (1970). Studies on
the nature of influenza virus ribonucleic acid. Journal of General
Microbiology 63(3): xvi. ISSN:
0022-1287.
NAL
Call Number: 448.3 J823
Descriptors: influenza A virus avian analysis, RNA viral
analysis, base sequence, guanine analysis.
Bron, R., A.P. Kendal, H.D. Klenk, and J. Wilschut
(1993). Role of the M2 protein in influenza virus membrane fusion: effects
of amantadine and monensin on fusion kinetics. Virology 195(2):
808-11. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: We have investigated the effects of the
anti-influenza drug amantadine (AMT) and the proton-ionophore monensin on the
membrane fusion activity of influenza virus in a liposomal model system, using
a kinetic fluorescence lipid mixing assay. Fusion of influenza virus
A/turkey/Oregon/71 (H7N3) with liposomes was slowed down in the presence of 2
microM AMT. The effect of AMT was not observed with an AMT-resistant mutant
virus. Fusion inhibition by AMT was reversed by the proton-ionophore monensin.
In fact, 1 microM monensin stimulated fusion of AMT-sensitive or -resistant
virus, irrespective of the presence of AMT. The effects of AMT and monensin
increased with increasing temperature. They were not observed at 25 degrees,
but were very prominent at 45 degrees. Monensin did not influence the fusion
rates of reconstituted viral envelopes (virosomes), which lack the nucleocapsid
and the M1 protein. These results suggest that intraviral low pH facilitates
influenza virus fusion, possibly by weakening interactions of the C-terminus of
the viral hemagglutinin with the M1 protein and/or the viral nucleocapsid. The
effect of AMT on the fusion capacity of influenza virus may contribute to the
anti-influenza action of the drug in the early stages of cellular infection.
However, the limited extent of the fusion inhibition suggests that the fusion
step is unlikely to be the primary target of AMT.
Descriptors: amantadine pharmacology, influenza A virus
avian metabolism, monensin pharmacology, viral matrix proteins metabolism,
electrophoresis, polyacrylamide gel, immunoblotting, avian drug effects,
kinetics, membrane fusion drug effects.
Brooks, M.J., J.J. Sasadeusz, and G.A. Tannock (
2004). Antiviral chemotherapeutic agents against respiratory viruses: where
are we now and what's in the pipeline? Current Opinion in Pulmonary
Medicine 10(3): 197-203. ISSN:
1070-5287.
Abstract: PURPOSE OF REVIEW: The emergence of severe
acute respiratory syndrome in late 2002 and the recent outbreaks of avian
influenza in Asia are timely reminders of the ever present risks from
respiratory viral diseases. Apart from influenza, there are no vaccines and
very few antiviral chemotherapeutic agents available for the prevention and
treatment of respiratory viral infections-the most common cause of human
illness. If the current H5N1 avian influenza outbreak ever assumes the role of
a pandemic, formidable technical difficulties relating to the properties of the
agent, itself, will ensure that vaccines will only become available after a
significant lead time and then only to a relatively small percentage of the
population. The use of existing antivirals could be critical in limiting the
initial spread of a pandemic, although their use in the control of epidemics
caused by nonpandemic viruses has not been evaluated. It is against this
background that a review of recent developments in respiratory antivirals has been
undertaken. RECENT FINDINGS: The late 1990s were a period of unprecedented
activity in the development of new and much superior antivirals for the
treatment of influenza infections. However, during the past 2 to 3 years and
largely for commercial reasons, there has been a decline in interest in their
further development by major drug companies. This situation may soon change
with the possible advent of new pandemic viruses, and moves are afoot in
several countries to consider the stockpiling of antivirals. The neuraminidase
inhibitors zanamivir and oseltamivir, and the M2 inhibitors amantadine and
rimantadine, remain the only options for controlling respiratory disease caused
by influenza viruses, although the latter two could not be used against very recent
H5N1 strains. There are several other neuraminidase inhibitors in development.
Compounds with activity against other respiratory viruses, notably
rhinoviruses, are also in development, many based on a newer knowledge of viral
protein structure and function (rational drug design). SUMMARY: The following
is an overview of recent papers on the further development of neuraminidase
inhibitors against influenza viruses and on recent development of newer
antivirals against RSV and rhinoviruses. Where possible, comparisons are made
with existing antivirals. For considerations of space, this review has been
structured around stages in the replication cycle of significant respiratory
viruses that have been traditionally used as targets for inhibition.
Descriptors: antiviral agents therapeutic use, respiratory
tract infections drug therapy, respiratory tract infections virology, virus
diseases drug therapy, antiviral agents pharmacology, drugs investigational
pharmacology, drugs investigational therapeutic use, enzyme inhibitors
pharmacology, enzyme inhibitors therapeutic use, ion channels antagonists and
inhibitors.
Brouillette, W.J., S.N. Bajpai, S.M. Ali, S.E. Velu,
V.R. Atigadda, B.S. Lommer, J.B. Finley, M. Luo, and G.M. Air (2003). Pyrrolidinobenzoic
acid inhibitors of influenza virus neuraminidase: Modifications of essential
pyrrolidinone ring substituents. Bioorganic and Medicinal Chemistry
11(13): 2739-2749. ISSN: 0968-0896.
NAL
Call Number: QP550.B55
Abstract: We recently reported the first benzoic acid,
1-(4-carboxy-2-(3-pentylamino)phenyl)-5,5-bis(hydroxymethyl)pyrrolidin-2-one
(8), that is a potent inhibitor of avian influenza A neuraminidase (N9) and,
unlike other reported potent neuraminidase inhibitors, does not contain a basic
aliphatic amine or guanidine nor a simple N-acetyl grouping. However, 8 was a
poor inhibitor of influenza B neuraminidase. In the present study we further
evaluated 8 as an inhibitor of human influenza A NA isolates, and it was
effective against N2 NA but found to be 160-fold less active against N1 NA. We
also synthesized analogues of 8 involving moderate modifications of essential
substituents on the pyrrolidinone ring. Specifically, the aminomethyl (9),
hydroxyethyl (10), and aminoethyl (11) analogues were prepared. Only the most
conservative change (compound 9) resulted in continued effective inhibition of
influenza A, in addition to a noteworthy increase in the activity of 9 for N1
NA. The effectiveness of 9 against influenza B neuraminidase was furthermore
improved 10-fold relative to 8, but this activity remained 50-fold poorer than
for type A NA.
Descriptors: methods and techniques, pharmacology,
influenza, drug therapy, respiratory system disease, viral disease, chemical
synthesis laboratory techniques.
Brown, C.C., H.J. Olander, and D.A. Senne (1992). A
pathogenesis study of highly pathogenic avian influenza virus H5N2 in chickens,
using immunohistochemistry. Journal of Comparative Pathology 107(3):
341-8. ISSN: 0021-9975.
NAL
Call Number: 41.8 J82
Abstract: Eighteen specific pathogen-free chickens
(nine hens older than 1 year and nine 15-week-old males) were inoculated with
highly pathogenic avian influenza virus A/Chicken/Pennsylvania/1370/1983
(H5N2). Birds were serially killed and tissues collected for histological and
immunohistochemical evaluation. In the group of older hens, disease was acute
or peracute. By immunohistochemistry, antigen was abundant in capillary
endothelium in multiple organs, and staining for antigen in parenchymal cells
was marked in brain and heart. In the group of younger male birds, disease was
subacute. Immunohistochemical staining of capillary endothelium was less
pronounced and viral antigen staining was evident in the parenchymal cells of
the heart, brain and kidney.
Descriptors: antigens, viral analysis, brain immunology,
endothelium, vascular immunology, fowl plague pathology, influenza A virus
avian pathogenicity, myocardium immunology, chickens, fowl plague immunology,
immunohistochemistry, avian classification.
Brown, I.H., P.A. Harris, J.W. McCauley, and D.J.
Alexander (1998). Multiple genetic reassortment of avian and human influenza
A viruses in European pigs, resulting in the emergence of an H1N2 virus of
novel genotype. Journal of General Virology 79(Pt. 12):
2947-55. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Novel H1N2 influenza A viruses which were
first detected in pigs in Great Britain in 1994 were examined antigenically and
genetically to determine their origins and establish the potential mechanisms
for genetic reassortment. The haemagglutinin (HA) of all swine H 1 N2 viruses
examined was most closely related to, but clearly distinguishable both
antigenically and genetically from, the HA of human H1N1 viruses which
circulated in the human population during the early 1 980s. Phylogenetic
analysis of the HA gene revealed that the swine H 1 N2 viruses formed a
distinct branch on the human lineage and were probably introduced to pigs
shortly after 1980. Following apparent transfer to pigs the HA gene underwent
genetic variation resulting in the establishment and cocirculation of
genetically and antigenically heterogeneous virus populations. Genetic analyses
of the other RNA segments of all swine H1N2 viruses indicated that the
neuraminidase gene was most closely related to those of early 'human-like'
swine H3N2 viruses, whilst the RNA segments encoding PB2, PB1, PA, NP, M and NS
were related most closely to those of avian viruses, which have been
circulating recently in pigs in Northern Europe. The potential mechanisms and
probable progenitor strains for genetic reassortment are discussed, but we
propose that the swine H1N2 viruses examined originated following multiple
genetic reassortment, initially involving human H1N1 and 'human-like' swine
H3N2 viruses, followed by reassortment with 'avian-like' swine H1N1 virus.
These findings suggest multiple reassortment and replication of influenza
viruses may occur in pigs many years before their detection as clinical
entities.
Descriptors: influenza A virus avian genetics, human
genetics, recombination, genetic, antigens, viral immunology, base sequence,
DNA, viral, Europe, genes viral, genotype, hemagglutination inhibition tests,
hemagglutinin glycoproteins, influenza virus genetics, avian immunology, human
immunology, molecular sequence data, phylogeny, sequence analysis, DNA, swine.
Brownson, J.M. and B.W. Mahy (1979). Productive
influenza virus infection of synchronized chick embryo fibroblast cells. Journal
of General Virology 42(3): 579-88.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The effects of cell metabolic activity on the
outcome of influenza virus infection were studied in partially synchronized
chick embryo fibroblast cultures. There was no evidence to show that the time
in the cell cycle at which cells were infected had any significant effect on
the final virus yield. However, some differences were detected in the length of
the latent period between infections established in synchronized or in
stationary cells. Influenza virus could replicate in synchronized or normal
cell cultures in which DNA synthesis was inhibited with
9-beta-D-arabinofuranosyladenine (ara-A).
Descriptors: influenza A virus avian growth and
development, virus replication drug effects, cell cycle, cell division, chick
embryo, DNA biosynthesis, fibroblasts, avian drug effects, tissue culture,
vidarabine pharmacology.
Brugh, M. and M.L. Perdue (1991). Emergence of
highly pathogenic virus during selective chicken passage of the prototype
mildly pathogenic chicken/Pennsylvania/83 (H5N2) influenza virus. Avian
Diseases 35(4): 824-33. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The prototype mildly pathogenic
A/chicken/Pennsylvania/21525/83 (H5N2) avian influenza virus, which was
isolated more than 5 months before the emergence of highly pathogenic virus in
the major 1983 Pennsylvania outbreak, was examined for the presence of minority
subpopulations of highly pathogenic virus. Selective serial passage of the
parental mildly pathogenic virus in leghorn hens did not lead to recovery of
highly pathogenic virus. However, several highly pathogenic reisolates were
recovered from hens inoculated with either of two mildly pathogenic virus
clones selected for their ability to efficiently produce plaques in trypsin-free
chicken embryo fibroblasts. Unlike the parental virus, these reisolates caused
high mortality in chickens and produced postmortem lesions typical of highly
pathogenic avian influenza. Electrophoretic mobilities of the hemagglutinin
glycoproteins of the highly pathogenic derivatives resembled those of the
prototype highly pathogenic A/chicken/Pennsylvania/1370/83 (H5N2) virus
isolated in October 1983. These results suggest that unrecognized
subpopulations of highly pathogenic virus may have infected Pennsylvania
chickens for several months before emerging as the clinically manifest
component of the virus population.
Descriptors: chickens, fibroblasts microbiology, fowl
plague microbiology, influenza A virus avian pathogenicity, cultured cells,
chick embryo, electrophoresis, polyacrylamide gel, glycoproteins analysis,
hemagglutination inhibition tests, avian chemistry, avian genetics, avian
growth and development, plaque assay, RNA viral analysis, serial passage,
specific pathogen free organisms, viral proteins analysis.
Bruinink, A. and O. Haller (1979). Macrophage
immunity to influenza virus: in vitro and in vivo studies. Experimental Cell Biology 47(3):
190-201. ISSN: 0304-3568.
NAL
Call Number: 448.8 Sch9
Abstract: Using M-TUR, a macrophage-adapted avian
influenza A virus (Hav1, Nav3), antiviral resistance of peritoneal macrophages
obtained from specifically or nonspecifically immunized mice towards in vitro
infection was assessed. M-TUR grew to high titers in macrophages from nonimmune
mice thereby causing a marked cytopathic effect. In contrast, peritoneal
macrophages from mice specifically immunized with TUR virus were not affected
by infection with M-TUR in vitro. This antiviral immunity was specific: mice
immunized with antigenetically unrelated influenza strains such as influenza
A/Hong Kong/1/68 (H3, N2) or influenza B/Lee yielded susceptible macrophages.
Specific macrophage immunity could be abrogated by trypsin treatment in vitro.
Susceptible macrophages from nonimmune hosts became resistant following in
vitro exposure to homologous anti-TUR sera. Peritoneal exudate cells from
BCG-infected animals were less susceptible to in vitro challenge with M-TUR
than control macrophages. In vivo treatment of mice with the unspecific
immunostimulants BCG or Corynebacterium parvum did not protect the animals
against lethal infection with a hepatotropic variant of TUR.
Descriptors: influenza immunology, influenza A virus
immunology, macrophages immunology, antigens, viral, cross reactions, epitopes,
mice, mice inbred c57bl immunology, mice inbred CBA immunology.
Bucher, D.J., I.G. Kharitonenkov, D.K. Lvov, T.V.
Pysina, and H.M. Lee (1980). Comparative study of influenza virus H2 (Asian)
hemagglutinins isolated from human and avian sources. InterVirology
14(2): 69-77. ISSN: 0300-5526.
NAL
Call Number: QR355.I5
Abstract: The hemagglutinin of an influenza virus
isolated from a wild duck (Pintail, Anas acuta) in the USSR in 1976 had
been found to be antigenically indistinguishable from the hemagglutinin of H2N2
viruses of human origin isolated in 1957. The hemagglutinins from viral
preparations of the A/Anas acuta/Primorie/695/76 (H2Nav2) and
A/Singapore/1/57 (H2N2) strains were purified by SDS gel chromatography as the
subunits HA1 and HA2. Comparison of amino acid compositions and peptide maps of
tryptic peptides containing [14C]-carboxymethylcysteine showed a striking
degree of similarity between the H2 hemagglutinins.
Descriptors: hemagglutinins viral analysis, influenza A
virus avian immunology, human immunology, amino acids analysis, ducks
microbiology, peptides analysis.
Buckler White, A.J. and B.R. Murphy (1986). Nucleotide sequence analysis of the
nucleoprotein gene of an avian and a human influenza virus strain identifies
two classes of nucleoproteins. Virology 155(2): 345-55. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The nucleotide sequences of RNA segment 5 of
an avian influenza A virus, A/Mallard/NY/6750/78 (H2N2), and a human influenza
A virus, A/Udorn/307/72 (H3N2), were determined and the deduced amino acid
sequences of the nucleoprotein (NP) of these viruses were compared to two other
avian and two other human influenza A NP sequences. The results indicated that
there are separate classes of avian and human influenza A NP genes that can be
distinguished on the basis of sites containing amino acids specific for avian
and human influenza viruses and also by amino acid composition. The human
influenza A virus NP genes appear to follow a linear pathway of evolution with
the greatest homology (96.9%) between A/NT/60/68 (H3N2) and A/Udorn/72,
isolated only 4 years apart, and the least homology (91.1%) between A/PR/8/34
(H1N1) and A/Udorn/72, isolated 38 years apart. Furthermore, 84% of the
nucleotide substitutions between A/PR/8/34 and A/NT/60/68 are preserved in the
NP gene of the A/Udorn/72 strain. In contrast, a distinct linear pathway is not
present in the avian influenza NP genes since the homology (90.3%) between the
two avian influenza viruses A/Parrot/Ulster/73 (H7N1) and A/Mallard/78 isolated
only 5 years apart is not significantly greater than the homology (90.1%)
between strains A/FPV/Rostock/34 and A/Mallard/78 isolated 44 years apart and
only 49% of the nucleotide substitutions between A/FPV/34 and A/Parrot/73 are found
in A/Mallard/78. A determination of the rate of evolution of the human
influenza A virus NP genes suggested that there were a greater number of
nucleotide substitutions per year during the first several years immediately
following the emergence of a new subtype in 1968.
Descriptors: influenza A virus genetics, nucleoproteins
genetics, viral proteins genetics, amino acid sequence, base sequence,
evolution, genes viral, nucleoproteins classification, RNA viral genetics,
sequence homology, nucleic acid, viral proteins classification.
Buckler White, A.J., C.W. Naeve, and B.R. Murphy
(1986). Characterization of a gene coding for M proteins which is involved
in host range restriction of an avian influenza A virus in monkeys. Journal
of Virology 57(2): 697-700. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: The nucleotide sequence of the region of RNA
segment 7 coding for the M1 and M2 proteins of avian influenza A/Mallard/New
York/6750/78 was determined, and the deduced amino acid sequences were compared
to other avian and human M protein sequences. The M2 proteins of the avian and
human viruses have diverged much more than the M1 proteins, although amino
acids specific for avian and human viruses were found in both M1 and M2
proteins.
Descriptors: genes viral, influenza A virus avian genetics,
RNA viral genetics, viral proteins genetics, amino acid sequence, haplorhini
microbiology, avian growth and development, messenger genetics.
Bukrinskaia, A.G. and T.A. Asadullaev (1968). Sravnitel'noe
deistvie gistonov i 6-azauridina na reproduktsiiu miksovirusov. [Comparative
effect of histones and 6-azauridine on the reproduction of myxoviruses]. Voprosy
Virusologii 13(5): 549-54. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: histones pharmacology, orthomyxoviridae drug
effects, triazines pharmacology, virus replication drug effects, influenza A
virus avian drug effects, Newcastle disease virus drug effects, RNA viral
antagonists and inhibitors.
Bukrinskaia, A.G., G.V. Kornilaeva, N.K. Vorkunova,
N.G. Timofeeva, and G.I. Shaposhnikova (1982). Gangliozidy--spetsificheskie
retseptory dlia virusa grippa. [Gangliosides--specific receptors for the
influenza virus]. Voprosy Virusologii 27(6): 661-6. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The capacity of two gangliosides, GD1a and
GT1b isolated from bovine brain to function as specific receptors of influenza
virus was determined. A primary chick fibroblast culture was treated with
neuraminidase to destroy natural receptors, the cells were loaded with
gangliosides GD1a and GT1b, inoculated with 3H-uridine-labeled virus, and virus
adsorption and penetration into the cell nucleus were determined. Both
gangliosides were shown to restore virus adsorption to the cell surface and
penetration of viral structures into the cell, GT1b facilitating more effective
transportation of viral structures into the nuclei than GD1a and inducing
penetration into the nuclei nearly 1.5-fold as much amount of viral structures
as in native cells. The same ganglioside partially restored virus-induced
hemolysis upon loading it on erythrocytes pre-treated with neuraminidase. It is
concluded that ganglioside GT1b is a specific receptor for influenza virus.
3.9% of this ganglioside was found in chick fibroblast lipids.
Descriptors: gangliosides metabolism, orthomyxoviridae
metabolism, receptors, virus metabolism, adsorption, cell nucleus metabolism,
chick embryo, erythrocytes metabolism, fibroblasts metabolism, hemolysis,
influenza A virus avian metabolism.
Bukrinskaia, A.G., N.V. Prokazova, G.I.
Shaposhnikova, S.L. Kocharov, and S.L. Shevchenko (1982). Rol' gangliozidov
v retseptsii i proniknovenii v kletku virusa grippa. [Role of gangliosides in
influenza virus reception and penetration into the cell]. Doklady Akademii
Nauk SSSR 263(6): 1481-4. ISSN:
0002-3264.
NAL
Call Number: 511 P444A
Descriptors: cell transformation, viral drug effects,
gangliosides pharmacology, influenza A virus avian pathogenicity, receptors,
virus drug effects, adsorption, carcinoma, Ehrlich tumor microbiology, avian
drug effects, neuraminidase pharmacology.
Bukrinskaya, A.G., A.K. Gitelman, and V.B. Martynenko
(1978). Abortive infection of influenza virus in Ehrlich ascites tumor
cells. Unusual fragility of virus particles. Archives of Virology
56(4): 279-90. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Noninfectious virus particles were produced
in Ehrlich ascites tumor cells infected intraperitoneally with fowl plague
virus. The PFU yield of virus per cell was less than 0.1 and the ratio PFU/HA
units in the progeny virus was less than 10(3). The virus particles had the
same morphology and size as egg-grown virus but were more fragile. They were
disrupted by centrifugation through sucrose and caesium chloride gradients, but
this disruption was avoided by fixing the particles with formaldehyde before
centrifugation. Analysis of polypeptides by SDS-PAGE showed that ascites-grown
virus particles contained reduced amounts of matrix protein compared with
egg-grown virus.
Descriptors: carcinoma, Ehrlich tumor microbiology,
influenza A virus avian growth and development, centrifugation, density
gradient, avian enzymology, avian ultrastructure, mice, neoplasm
transplantation, neuraminidase metabolism, peptides analysis, viral proteins
analysis, virus replication.
Bukrinskaya, A.G., A.K. Gitelman, V.B. Martynenko,
and T.A. Assadulaev (1979). Properties of influenza virus nucleocapsids in
nonpermissive cells. Acta Virologica 23(5): 353-9. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The properties of fowl plague virus
(influenza virus A) nucleocapsids isolated from the cytoplasm of infected
Ehrlich ascites carcinoma cells and chick embryo cells were compared. Nucleocapsids
isolated from both systems possessed similar polypeptides (P and NP) but
differed in their biophysical characteristics. Nucleocapsids from ascites cells
sedimented in velocity sucrose gradients slower (from 25 to 50 S) and the
majority of them banded at higher density in CsCl gradients (rho 1.38 as
compared to 1.34 g/ml) than nucleocapsids from chick embryo cells. In the
electron microscope they appeared as thin threads 3--4 nm in diameter.
Descriptors: capsid analysis, influenza A virus avian analysis,
viral proteins analysis, capsid biosynthesis, carcinoma, Ehrlich tumor,
cultured cells, centrifugation, density gradient, chick embryo, cytoplasm
analysis, avian growth and development, avian metabolism, mice, microscopy,
electron.
Bullough, P.A. and P.A. Tulloch (1991). Spot-scan
imaging of microcrystals of an influenza neuraminidase-antibody fragment
complex. Ultramicroscopy 35(2): 131-43.
ISSN: 0304-3991.
NAL
Call Number: QH201.U4
Abstract: Electron micrographs of two-dimensional
microcrystals of a complex of an avian influenza virus neuraminidase and an
antibody Fab fragment, termed 32/3, have been recorded using the spot-scan
method of imaging. The crystals have a large unit cell (159.5 A x 159.5 A x
130.5 A) and a high solvent content (approximately 71% by volume) and are a
challenging specimen for testing the spot-scan methodology. Crystalline order
was preserved to beyond 4 A resolution as demonstrated by electron diffraction,
using an embedding medium of a mixture of glucose and neutral potassium
phosphotungstate. Using a Philips C400 computer control system interfaced to an
EM420 electron microscope, and with the inclusion of additional software in the
system, we have been able to record micrographs at low temperature with a
relatively narrow (1500 A diameter) moving beam. There is evidence that the use
of such a spot-scan beam reduces the effects of beam-induced specimen motion on
the quality of micrographs. Conventional low-dose "flood-beam" images
showed good isotropic optical diffraction in only 15% of cases whereas 30% of
spot-scan images showed good diffraction. The best flood-beam images gave
phases to only 15 A resolution after computer processing, whereas the best
spot-scan images gave phases to 7 A resolution. Electron diffraction patterns
were also recorded at low temperature, and the resulting diffraction amplitudes
combined with phases from spot-scan images to yield a projection map of the
structure. A 7 A resolution projection map of the complex is presented, and is
compared with the projection map of the same avian influenza neuraminidase
complexed with a different monoclonal Fab fragment, NC41, which has been solved
to high resolution by X-ray diffraction.
Descriptors: antibodies, viral chemistry, image
processing, computer assisted, immunoglobulins, Fab ultrastructure, influenza A
virus avian ultrastructure, neuraminidase ultrastructure, binding sites,
crystallization, crystallography, immunoglobulins, Fab chemistry, avian
enzymology, avian immunology, microscopy, electron, neuraminidase chemistry,
x-ray diffraction.
Burger, H., H. Steuler, and C. Scholtissek (1985). A
mutant of fowl plague virus (influenza A) with an enhanced electrophoretic
mobility of RNA segment 8. Journal of General Virology 66(Pt. 8):
1679-86. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: A temperature-sensitive mutant (ts 1/9)
obtained by undiluted passage of fowl plague virus (FPV) at 33 degrees C
carried a strong ts defect in RNA segment 6 [neuraminidase (NA) gene] and a
weak ts defect in RNA segment 8 [non-structural (NS) protein Although the viral
proteins have normal migration rates, the NS gene migrated during
polyacrylamide gel electrophoresis (PAGE) significantly faster than the NS gene
of wild-type FPV, even after denaturation by glyoxal. Despite this observation,
the NS gene of ts 1/9 did not carry a deletion as shown by sequence
determination. There were only five base replacements which resulted in three
changes in amino acids. Three of the base replacements led to a more compact
secondary structure of RNA segment 8, which seems to be responsible for the
faster migration rate during PAGE and which seems to resist, at least
partially, the treatment with glyoxal.
Descriptors: influenza A virus avian genetics, mutation,
RNA viral isolation and purification, amino acid sequence, base sequence,
cultured cells, chick embryo, cloning, molecular, genes, structural, genes
viral, hemagglutinins genetics, neuraminidase genetics, plasmids, viral
genetics, RNA directed DNA polymerase metabolism.
Bush, R.M. (2004). Influenza as a model system for
studying the cross-species transfer and evolution of the SARS coronavirus. Philosophical
Transactions of the Royal Society of London. Series B Biological Sciences
359(1447): 1067-73. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Abstract: Severe acute respiratory syndrome coronavirus
(SARS-CoV) moved into humans from a reservoir species and subsequently caused
an epidemic in its new host. We know little about the processes that allowed
the cross-species transfer of this previously unknown virus. I discuss what we
have learned about the movement of viruses into humans from studies of
influenza A, both how it crossed from birds to humans and how it subsequently
evolved within the human population. Starting with a brief review of severe
acute respiratory syndrome to highlight the kinds of problems we face in
learning about this viral disease, I then turn to influenza A, focusing on
three topics. First, I present a reanalysis of data used to test the hypothesis
that swine served as a "mixing vessel" or intermediate host in the
transmission of avian influenza to humans during the 1918 "Spanish
flu" pandemic. Second, I review studies of archived viruses from the three
recent influenza pandemics. Third, I discuss current limitations in using
molecular data to study the evolution of infectious disease. Although influenza
A and SARS-CoV differ in many ways, our knowledge of influenza A may provide
important clues about what limits or favours cross-species transfers and
subsequent epidemics of newly emerging pathogens.
Descriptors: evolution, molecular, influenza transmission,
influenza A virus physiology, models, biological, phylogeny, SARS virus
physiology, zoonoses virology, influenza genetics, influenza A virus genetics,
swine virology.
Cabezas, J.A. (1991). Etudes sur la sialidase et
l'esterase des virus de la grippe. [Studies on sialidase and esterase in
influenza viruses]. Annales Pharmaceutiques Francaises 49(2):
57-66. ISSN: 0003-4509.
NAL
Call Number: 396.8 AN7
Abstract: The main contributions of the author and
collaborators about sialidase (EC 3.2.1.18) of influenza virus types A and B
and O-acetylesterase (EC 3.1.1.53) of type C are summarized. After a short
introduction on the topic, the negative results obtained by the author on
inhibitors are commented. Then, the peculiarities of the three procedures
assayed, based on the NADH determination as a measurement for the sialidase
activity, are discussed. The spectrofluorimetric measurement of NADH concentration
is a more sensitive and convenient procedure than that by spectrophotometry,
although it is less sensitive than that based on bioluminiscence. Sialidase
activity is generally higher in influenza virus type A than in type B; however,
some differences have been found between the three sub-types A analysed.
Furthermore, thermal stability and stability against changes in the pH values
are higher for influenza virus from ducks, followed by those from humans and,
finally, by those from pigs. O-acetylesterase of influenza virus type C shows a
broad specificity; it acts on O-acetyl-containing compounds which may not be
sialic acids. It seems that this enzyme might contribute to facilitate the
action of sialidase of influenza virus types A and B. The peculiarities of
influenza virus type C suggest to include this type as a new genus in the
future classification of viruses.
Descriptors: carboxylic ester hydrolases analysis,
neuraminidase analysis, orthomyxoviridae enzymology, ducks, fowl plague
enzymology, influenza enzymology, influenza A virus avian enzymology, human
enzymology, porcine enzymology, influenza B virus enzymology, influenza virus C
enzymology, orthomyxoviridae infections enzymology, swine.
Cameron, K.R., V. Gregory, J. Banks, I.H. Brown, D.J.
Alexander, A.J. Hay, and Y.P. Lin (2000). H9N2 subtype influenza A viruses
in poultry in Pakistan are closely related to the H9N2 viruses responsible for
human infection in Hong Kong. Virology 278(1): 36-41. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: disease outbreaks veterinary, influenza
veterinary, influenza A virus avian classification, human classification,
poultry diseases virology, antigens, viral genetics, antigens, viral immunology,
cloning, molecular, genome, viral, hemagglutination inhibition tests,
hemagglutinins viral genetics, Hong Kong epidemiology, influenza epidemiology,
avian genetics, avian immunology, human genetics, human immunology, molecular
sequence data, Pakistan epidemiology, phylogeny, poultry diseases epidemiology,
sequence analysis, protein, viral proteins genetics, viral proteins immunology.
Capua, I., F. Mutinelli, and M.H. Hablovarid (2002). Avian
embryo susceptibility to Italian H7N1 avian influenza viruses belonging to
different genetic lineages. Archives of Virology 147(8): 1611-21. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: In the present paper we report of the results
of an immunohistochemical investigation to assess tissue tropism and viral
replication in developing chicken, turkey, Muscovy duck and mallard duck
embryos, of Italian H7N1 isolates belonging to different genetic lineages. LPAI
isolates were chosen on the basis of the location in the phylogenetic tree: a
progenitor strain, A/ty/Italy/977/V99, (exhibiting no additional glycosylation
site, nAGS), strain A/ty/Italy/2379/V99 (AGS in position 123) and strain
A/ty/Italy/3675/V99 (AGS in position 149) were selected. The latter two strains
belonged to distinct lineages originating from the pool of progenitor strains.
HPAI isolate A/ty/Italy/4580/V99 was also included in the study. All the
embryos tested supported the growth of HPAI. The LPAI isolates replicated
readily in the allantoic layer of the CAM of all the species tested, and did
not grow in the developing chicken, turkey and Muscovy duck embryos. In
contrast, they replicated to different extents in the respiratory tract of the
developing mallard embryo, which also presented lower mortality rates than the
other species. We conclude from these findings that the pathogenesis of LPAI
infections in mallard embryos is different to that observed in other species,
and should be investigated further.
Descriptors: allantois virology, chick embryo virology,
chorion virology, influenza A virus avian pathogenicity, disease
susceptibility, ducks, embryo loss etiology, glycosylation, immunohistochemistry, avian genetics,
turkeys.
Capua, I., C. Terregino, G. Cattoli, and A. Toffan
(2004). Increased resistance of vaccinated turkeys to experimental infection
with an H7N3 low-pathogenicity avian influenza virus. Avian Pathology
33(2): 158-163. ISSN: 0307-9457.
NAL
Call Number: SF995.A1A9
Descriptors: avian influenza virus, disease control,
disease prevention, disease resistance, experimental infection, immune
response, vaccination, turkeys.
Caric Lazar, M., C. Scholtissek, and R. Rott (1975). Effect
of tetraethyl thiuram disulfide (disulfiram) on the multiplication of enveloped
viruses. Archives of Virology 48(4): 297-306. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Disulfiram at concentrations between 0.1 and
0.3 mM inhibits the multiplication of Semliki Forest virus (SFV), fowl plague
virus (FPV), Newcastle disease virus (NDV), vesicular stomatitis virus (VSV),
and pseudorabies virus (PRV), when administered 1 hour before and during
adsorption. There is, however, no inhibition of virus multiplication, when the
drug is added after adsorption onto chick embryo cells. Disulfiram interferes
neither with the receptors of the virus nor of erythrocytes, and it does not
prevent virus adsorption. Possibly an early step in virus multiplication is
affected by disculfiram. Infected cells once treated with the drug recover
after some time of incubation in an ingibitor-free medium. The inhibitory state
can be maintained, however, if relatively low doses of disulfiram are present
in the culture medium also after adsorption. Disulfiram has no effect on
macromolecular synthesis of the host cells. It has, however, a marked affect on
membrane function. While virus multiplication is readily inhibited by
disulfiram when chick embryo or BHK cells were investigated, virus
multiplication in HeLa cells is almost resestant against the action of
disulfiram.
Descriptors: disulfiram pharmacology, herpesviridae growth
and development, herpesvirus 1, suid growth and development, influenza A virus
avian growth and development, Newcastle disease virus growth and development,
Semliki Forest virus growth and development, vesicular stomatitis Indiana virus
growth and development, virus replication drug effects, adsorption, ditiocarb
pharmacology, erythrocytes drug effects, ethanol pharmacology, influenza A
virus avian drug effects, Newcastle disease virus drug effects, pseudorabies
drug therapy, Semliki Forest virus drug effects, tissue culture, vesicular
stomatitis Indiana virus drug effects.
Carroll, S.M. and J.C. Paulson (1985). Differential
infection of receptor-modified host cells by receptor-specific influenza
viruses. Virus Research 3(2): 165-79. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Influenza viruses of contrasting receptor
specificity have been examined for their ability to infect receptor-modified
MDCK cells containing sialyloligosaccharide receptor determinants of defined
sequence. Cells were treated with sialidase to remove sialic acid and render
them resistant to infection and were then incubated with sialyltransferase and
CMP-sialic acid to restore sialic acid in the SA alpha 2,6Gal or SA alpha
2,3Gal linkages. The viruses A/RI/5 + /57 and A/duck/Ukraine/1/63, previously
shown to exhibit preferential binding of SA alpha 2,6Gal and SA alpha 2,3Gal
linkages, respectively, were found to exhibit differential infection of the
receptor-modified cells in accord with their receptor specificity. Coinfection
of SA alpha 2,3Gal derivatized cells with a mixture of the two viruses resulted
in selective propagation of the SA alpha 2,3Gal-specific A/duck/Ukraine/1/63
virus. The results demonstrate the potential for cell surface receptors to
mediate selection of receptor-specific variants of influenza virus.
Descriptors: influenza A virus avian metabolism, human
metabolism, oligosaccharides metabolism, receptors, virus metabolism,
adsorption, antibodies, viral analysis, binding sites, cell line, dogs,
erythrocytes microbiology, hemagglutinins viral, avian immunology, human
immunology, kidney, neuraminidase metabolism, receptors, virus genetics,
receptors, virus immunology, sialic acids metabolism, sialyltransferases
metabolism, species specificity, viral proteins analysis.
Carter, M.J. and B.W. Mahy (1982). Incomplete
avian influenza A virus displays anomalous interference. Archives of
Virology 74(1): 71-6. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian physiology, viral
interference, cultured cells, chick embryo, defective viruses physiology,
fibroblasts, kinetics, probability.
Carter, M.J. and B.W. Mahy (1982). Synthesis of
RNA segments 1-3 during generation of incomplete influenza A (fowl plague)
virus. Archives of Virology 73(2): 109-19. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Incomplete influenza A virus (fowl plague
Dobson strain) was prepared by undiluted passage in primary chick embryo
fibroblast cells. Analysis of released virus RNA revealed a deficiency in RNA
segments 1-3, characteristic of incomplete virus formation. The virus yield
from a high multiplicity infection with standard virus always showed this
deficiency, even when analysed as early as 6 hours post-infection, whereas infection
at low multiplicity gave rise to virus indistinguishable in RNA composition
from the parent virus. The relative amounts of intracellular,
non-polyadenylated, complementary RNA (template RNA) were found to reflect
accurately the eventual RNA composition of released virus, and were altered in
phase with PFU:HAU ratio, throughout a von Magnus cycle.
Descriptors: defective viruses growth and development,
influenza A virus avian growth and development, RNA viral biosynthesis,
cultured cells, chick embryo, defective viruses metabolism, avian metabolism,
kinetics, plaque assay, templates, genetic.
Caton, A.J. and J.S. Robertson (1980). Structure
of the host-derived sequences present at the 5' ends of influenza virus mRNA.
Nucleic Acids Research 8(12): 2591-603.
ISSN: 0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: Nucleotide sequence analysis of the terminal
virus-coded regions of a clone of the matrix gene of influenza virus indicated
that the region corresponding to the 5' end of the mRNA contains an additional
13 non-virus coded nucleotides. Using the dideoxy-chain termination sequencing
method with a restriction fragment derived from this clone, we have determined
that the 5' ends of matrix gene mRNAs contain a heterogenous sequence of 9-15
nucleotides. In addition, the data indicate that the 3' terminal nucleotide of
matrix gene virion RNA is not transcribed into mRNA, transcription of influenza
virus-specific sequences commencing with the penultimate nucleotide at the 3'
end of viron RNA.
Descriptors: influenza A virus avian analysis, RNA,
messenger, viral, base sequence, cloning, molecular, DNA restriction enzymes,
DNA, recombinant.
Cattoli, G., V. Brasola, and I. Capua (2003). Plaque
morphology of Italian H7N1 LPAI isolates in MDCK cells and in primary cells of
different avian species. Avian Diseases 47(Special Issue):
1161-1163. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The morphology of plaques induced by Italian,
H7N1, low-pathogenic avian influenza (LPAI) viruses belonging to different
lineages was investigated in primary chicken, turkey, Muscovy duck, and mallard
duck kidney cells and in MDCK cells in the absence of trypsin. LPAI isolates
were selected on the basis of the location in the phylogenetic tree: 977/V99
(located at the root, no additional glycosylation site (nAGS)), 2379/V99 (AGS
in position 123), and 3675/V99 (AGS in position 149). Different isolates did
not induce plaques with a statistically significant different size in MDCK
cells. However, in primary cells of different avian origin, the presence or
absence of AGS significantly influenced plaque size. Generally speaking,
977/V99 was the least efficient at plaquing in all cells, while 2379/V99 (AGS
in position 123) plaqued more efficiently in turkey cells and 3675/V99 (AGS in
position 149) in chicken cells. The presence of either AGS induced
statistically significant larger plaques in cells of waterfowl origin.
Descriptors: cell biology, infection, avian influenza,
infectious disease, respiratory system disease, viral disease, cell culture
culturing techniques, laboratory techniques, glycosylation sites plaque
morphology.
Chambers, T.M. and R.G. Webster (1987). Defective
interfering virus associated with A/Chicken/Pennsylvania/83 influenza virus.
Journal of Virology 61(5): 1517-23.
ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The A/Chicken/Pennsylvania/1/83 influenza
virus, isolated from a respiratory infection of chickens, is an avirulent H5N2
virus containing subgenomic RNAs (W.J. Bean, Y. Kawaoka, J.M. Wood, J.E.
Pearson, and R.G. Webster, J. Virol. 54:151-160, 1985). We show here that
defective interfering particles are present in this virus population. The virus
had a low ratio of plaque-forming to hemagglutinating units and produced
interference with standard virus multiplication in infectious center reduction
assays. Subgenomic RNAs were identified as internally deleted polymerase RNAs.
We have confirmed that this virus protects chickens from lethal H5N2 influenza
virus infection. This protective effect appeared to be due to the inhibition of
virulent virus multiplication. Additionally, subgenomic RNAs derived from
polymerase RNAs were detected in 5 of 18 RNA preparations from animal influenza
virus isolates. Therefore, defective interfering particles are sometimes
produced in natural influenza virus infections, not just under laboratory
conditions. These particles may be capable of suppressing the pathogenic effect
of virulent virus infections in nature.
Descriptors: defective viruses genetics, influenza A virus
avian genetics, DNA directed RNA polymerases genetics, defective viruses growth
and development, genes viral, avian growth and development, viral genetics,
viral interference, virus replication.
Chambers, T.M., S. Yamnikova, Y. Kawaoka, D.K. Lvov,
and R.G. Webster (1989). Antigenic and molecular characterization of subtype
H13 hemagglutinin of influenza virus. Virology 172(1): 180-8. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Influenza A viruses with subtype H13
hemagglutinin display an unusual host range. Although common in shorebirds,
they are very rare or absent in wild ducks; additionally, H13 viruses have been
isolated from a whale. To study the molecular basis for this host range, we
have determined the complete nucleotide sequences of the hemagglutinin genes of
three H13 influenza viruses from different species or geographical areas:
A/gull/Maryland/77, A/gull/Astrachan (USSR)/84, and A/pilot whale/Maine/84.
Based on the deduced amino acid sequences, H13 hemagglutinin shares the basic
structure of other type A hemagglutinin subtypes such as H3, but has clearly
diverged from other completely sequenced subtypes. Unique features of H13
hemagglutinin include the occurrence, near the receptor binding pocket, of
residues Arg/Lys-227 and Trp-229 (H3 numbering); the significance of these are
unknown. The sequence of the HA1-HA2 cleavage site resembles those of avirulent
avian influenza viruses. The whale H13 hemagglutinin is similar to those from
gulls, supporting the hypothesis that influenza viruses from avian sources can
enter marine mammal populations but are probably not permanently maintained
there. Antigenic analysis using a panel of monoclonal antibodies suggests that,
like other subtypes, H13 viruses are heterogeneous, with different antigenic
variants predominating in the eastern versus the western hemispheres.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, amino acid sequence, base sequence, genes viral,
hemagglutinins viral classification, hemagglutinins viral genetics, avian
classification, influenza A virus avian genetics, molecular sequence data, RNA
viral genetics.
Chen Hualan, Yu Kangzhen, and Tian Guobin (1997). Amplification
and cloning of haemagglutinin genes of avian influenza virus of H5 and H7
subtypes by RT-PCR. Chinese Journal of Animal and Poultry Infectious
Diseases (2): 16-18. ISSN:
1001-6961.
Descriptors: poultry, avian influenza virus, DNA, nucleotide
sequence, molecular cloning, acids, domestic animals, genetic engineering,
genomes, influenza virus, livestock, nucleic acids, nucleic compounds, organic
acids, orthomyxoviridae, useful animals, viruses.
Chepulis, G.K., A.F. Bocharov, and V.M. Zhdanov (1967).
Ionoobmennaia khromatografiia virusa klassicheskoi chumy ptits na
tselliuloznykh obmennikakh. [Ion-exchange chromatography of classical fowl
plague virus on cellulose exchangers]. Voprosy Virusologii 12(4):
439-45. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian isolation and
purification, cellulose, chromatography, ion exchange.
Chepulis, G.K. and V.M. Zhdanov (1970). Cellular
antigens in myxo- and paramyxoviruses as revealed by immunodiffusion methods.
Experientia 26(10): 1141-3. ISSN: 0014-4754.
NAL
Call Number: 475 Ex7
Descriptors: abo blood group system analysis, antigens
analysis, erythrocytes immunology, fetal membranes immunology, haptens
analysis, immunodiffusion, immunoelectrophoresis, influenza A virus avian
immunology, kidney immunology, Newcastle disease virus immunology,
parainfluenza virus 1, human immunology, guinea pigs, immunity, cellular,
methods, rabbits, rats.
Chepulis, G.S., I.U.S. Derkach, and V.M. Zhdanov
(1972). Belkovye komponenty virusa klassicheskoi chumy ptits i virusa
bolezni N'iukasla. [Protein components of classical fowl plague virus and
Newcastle disease virus]. Voprosy Virusologii 17(1): 48-52. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian analysis, Newcastle
disease virus analysis, viral proteins analysis, antigens, viral analysis,
centrifugation, density gradient, electrophoresis, disc, immunodiffusion.
Chepulis, G.S., V.M. Zhdanov, I. Nas, I. Cherba, and
K. Rozha (1971). Vyiavlenie kletochnykh antigenov u miksovirusov i
paramiksovirusov metodami immunodiffuzii. [Detection of cellular antigens in
myxoviruses and paramyxoviruses by the immunodiffusion method]. Voprosy
Virusologii 16(1): 62-70. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antigens analysis, influenza A virus avian
immunology, Newcastle disease virus immunology, orthomyxoviridae immunology,
parainfluenza virus 1, human immunology, antigens, viral analysis, guinea pigs,
immunodiffusion, immunoelectrophoresis, rabbits, rats, species specificity.
Cherednichenko, O.G., Z.M. Biiasheva, and N.B.
Akhmatullina (2001). Geneticheskii analiz retsessivnykh letal'nykh mutatsii,
indutsirovannykh virusom grippa v X-khromosome Drosophila melanogaster.
[Genetic analysis of recessive lethal mutations induced by the influenza virus
in the X chromosome of Drosophila melanogaster]. Genetika 37(7): 908-14.
ISSN: 0016-6758.
NAL
Call Number: QH431.A1G4
Abstract: Mutagenic potential of the influenza virus
was evaluated. Based on its capacity of inducing recessive lethal mutations in
the X chromosome of Drosophila
melanogaster, the influenza virus can be classified as a moderate-activity
mutagen. Its mutagenicity does not depend on ability to reproduce in the cell system.
This virus was shown to disrupt formation of the wing, particularly wing vein
M1 + 2. Cytogenetic examination of polytene X chromosomes bearing recessive
lethal mutations in Drosophila salivary glands did not reveal chromosome
rearrangements. These lethals are assumed to be small deletions or point
mutations. The determination of the lethal activity stage of these mutations
showed that they disrupt the expression of genes functioning at various
developmental stage of Drosophila. Two of them were conditionally lethal
(temperature-sensitive). Two of 15 mutations analyzed were mapped to region
2B9-10-3C10-11.
Descriptors: Drosophila melanogaster genetics, Drosophila
melanogaster virology, influenza A virus avian genetics, mutagenesis, X
chromosome genetics, genes, lethal, genes, recessive, point mutation.
Chiu, S.Y., H.K. Shieh, J.H. Shien, S.Y. Tai, and
L.H. Lee (1994). Preparation of monoclonal antibody against avian influenza
virus H5N9 strain. Journal of the Chinese Society of Veterinary Science
20(1): 40-50. ISSN: 0253-9179.
NAL
Call Number: SF604.C54
Abstract: The spleen of BALB/c mice, which had been
immunized five times with purified avian influenza virus, H5N9 strain, and had
good antibody response, was harvested; the spleen cells were fused with NS-1
myeloma cells. After a screening for specific antibody production with the
ELISA test, 18 of 460 wells showed strong positive reactions. Three further
subclonings established nine strains of hybridoma with stable activities of
secreting monoclonal antibodies. The isotypes of the nine monoclonal antibodies
were all IgG1, and all their light chains also belong to the kappa chain. The
antibodies were applied on CEF cultures infected with AIV H5N9 by means of
indirect fluorescent antibody staining. Fluorescence was observed among the
cell cytoplasm only. All monoclonal antibodies had HI and neutralization
abilities, but formed no precipitation line in a immunodiffusion test. One
antibody reacted with viral polypeptide, which was HA2 antigen with molar mass
28 kD, according to the western blotting test. In order to detect the
specificity, we reacted the monoclonal antibody with AIV subtypes H1 through
H12, respectively, according to the HI test. Besides H5N9, the antibody reacted
with strain H8N4, but not H8N6. Viral protein analysis by means of SDS-PAGE
revealed that both H5N9 and H8N4 had common peptide bands 69, 57, 48, 37 and 28
kD, especially the peptide of HA2, 28 kD.
Descriptors: immune system, infection, microbiology, pathology,
pharmacology, veterinary medicine, vaccination viral protein analysis.
Chizhov, N.P. (1974). Protivovirusnoe deistvie
nukleaz i gistonov [Antiviral action of nucleases and histones]. Voprosy
Virusologii (6): 647-52. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antiviral agents pharmacology,
deoxyribonucleases pharmacology, histones pharmacology, ribonucleases
pharmacology, adenoviridae drug effects, adenoviridae infections drug therapy,
antiviral agents therapeutic use, aphthovirus drug effects, conjunctivitis drug
therapy, DNA, viral biosynthesis, deoxyribonucleases therapeutic use,
encephalitis virus, Venezuelan equine drug effects, encephalitis viruses, tick
borne drug effects, herpesviridae infections drug therapy, histones therapeutic
use, influenza A virus avian drug effects, keratitis, dendritic drug therapy,
meningitis, viral drug therapy, Newcastle disease virus drug effects,
orthomyxoviridae drug effects, polioviruses drug effects, RNA viral
biosynthesis, ribonucleases therapeutic use, simplexvirus drug effects,
vaccinia virus drug effects, vesicular stomatitis Indiana virus drug effects,
virus replication drug effects.
Choi, Y.K., S.M. Goyal, M.W. Farnham, and H.S. Joo
(2002). Phylogenetic analysis of H1N2 isolates of influenza A virus from
pigs in the United States. Virus Research 87(2): 173-9. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Twenty-four H1N2 influenza A viruses were
newly isolated from pigs in the United States. These isolates originated from
19 farms in 9 different swine producing states between 1999 and 2001. All farms
had clinical histories of respiratory problem and/or abortion. The viral
isolates were characterized genetically to determine the origin of all eight
gene segments. The results showed that all H1N2 isolates were reassortants of
classical swine H1N1 and triple reassortant H3N2 viruses. The neuraminidase
(NA) and PB1 genes of the H1N2 isolates were of human origin, while the
hemagglutinin (HA), nucleoprotein (NP), matrix (M), non-structural (NS), PA and
PB2 polymerase genes were of avian or swine origin. Fifteen of the 24 H1N2
isolates were shown to have a close phylogenic relationship and high amino acid
homology with the first US isolate of H1N2 (A/SW/IN/9K035/99). The remaining nine
isolates had a close phylogenic relationship with classical swine influenza
H1N1 in the HA gene. All other genes including NA, M, NP, NS, PA, PB1 and PB2
showed a close phylogenic relationship with the H1N2 (A/SW/IN/9K035/99) strain
and triple reassortant H3N2 viruses. However, PB1 genes of two isolates
(A/SW/KS/13481-S/00, A/SW/KS/13481-T/00) were originated from avian influenza A
virus lineage. These results suggest that although there are some variations in
the HA genes, the H1N2 viruses prevalent in the US swine population are of a
similar genetic lineage.
Descriptors: influenza A virus, porcine genetics,
antigens, viral, hemagglutinin glycoproteins, influenza virus genetics, porcine
classification, porcine enzymology, porcine isolation and purification,
molecular sequence data, neuraminidase
genetics, phylogeny, swine, United States, variation genetics.
Chucholowius, H.W. and R. Rott (1972). A new
method for purification of myxoviruses by zonal centrifugation with two
different sucrose density gradients. Proceedings of the Society for
Experimental Biology and Medicine, New York, NY 140(1): 245-7. ISSN: 0037-9727.
NAL
Call Number: 442.9 So1
Descriptors: orthomyxoviridae isolation and purification,
centrifugation, density gradient, centrifugation, zonal, influenza A virus
avian isolation and purification, methods, Newcastle disease virus isolation
and purification, sucrose.
Ciampor, F., P.M. Bayley, M.V. Nermut, E.M. Hirst,
R.J. Sugrue, and A.J. Hay (1992). Evidence that the amantadine-induced, M2-mediated
conversion of influenza A virus hemagglutinin to the low pH conformation occurs
in an acidic trans Golgi compartment. Virology 188(1): 14-24. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Amantadine treatment of cells infected with H7
strains of influenza A viruses causes an M2 protein-mediated conversion of
hemagglutinin (HA) from its native to its low pH conformation.
Immunofluorescence and electron microscopic observations showed that the
structural alteration and hence drug action occur shortly after HA exits from
the Golgi complex during its passage through the strans Golgi region. Using the
DAMP/anti-DNP pH probe it is evident that virus infection causes increased
acidity of the trans Golgi region and that vesicles containing low pH HA in
amantadine-treated virus-infected cells are particularly acidic. These results
indicate therefore that the alteration in HA is the direct consequence of
exposure to an adverse low pH and provide further support for the conclusion
that the M2 protein, the target of amantadine action, is involved in regulating
vesicular pH, a function important for the correct maturation of the HA
glycoprotein.
Descriptors: amantadine pharmacology, Golgi apparatus
metabolism, hemagglutinins viral chemistry, influenza A virus avian drug
effects, cell compartmentation, cultured cells, fluorescent antibody technique,
hemagglutinin glycoproteins, influenza virus, hemagglutinins viral drug
effects, hemagglutinins viral metabolism, hydrogen-ion concentration, avian ultrastructure,
microscopy, immunoelectron, monensin pharmacology, protein conformation drug
effects, temperature.
Ciampor, F., C.A. Thompson, S. Grambas, and A.J. Hay
(1992). Regulation of pH by the M2 protein of influenza A viruses. Virus
Research 22(3): 247-58. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: Inhibition of the function of the M2 protein
by amantadine can cause a conformational change in the haemagglutinin (HA) of
H7 influenza A viruses and the consequent expression of the low pH form of the
glycoprotein on the surface of virus-infected cells. Immunofluorescence studies
showed that this conversion occurs shortly after HA exists from the Golgi
complex apparently during its transport through the trans Golgi network and
using the pH probe, DAMP/anti-DNP, that it is the direct result of reduced
vesicular pH. The lowest pHs encountered were estimated using mutant HAs
differing in pH stability to be approximately 5.2 and 5.6 in virus-infected CEF
or MDCK cells, respectively, in the absence of functional M2. Depending on the
particular M2, this protein was responsible for increases in vesicular pH of up
to 0.8 units. The influence of mutations in both HA and M2 on the maturation of
native HA illustrates the important relationship between the structural and
functional properties of these two proteins. Using the fluorescent probe
SNARF-1 the M2 protein was also shown to be largely responsible for the 0.3-0.4
unit reduction in intracellular pH of virus-infected cells. The data thus provide
further evidence for the pH regulatory function of M2 and its importance for
the maturation of the HA glycoprotein.
Descriptors: influenza A virus avian physiology, viral
matrix proteins physiology, amantadine pharmacology, cell line, fluorescent antibody
technique, hemagglutination, viral, hydrogen-ion concentration.
Ciampor, F. and P. Turcan (1972). Electron
microscopy of tissue culture cells infected with myxoviruses. II.
Nucleo-cytoplasmic changes in fowl plague virus-infected cells. Acta
Virologica 16(3): 177-82. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: cell nucleus microbiology, cultured cells
microbiology, cytoplasm microbiology, influenza A virus avian growth and
development, orthomyxoviridae growth and development, cell membrane
microbiology, cell nucleolus, cultured cells cytology, chick embryo,
cytopathogenic effect, viral, hamsters, inclusion bodies, viral, kidney
cytology, microscopy, electron, time factors, virus replication.
Clements, M.L., S.D. Sears, K. Christina, B.R.
Murphy, and M.H. Snyder (1989). Comparison of the virologic and immunologic
responses of volunteers to live avian-human influenza A H3N2 reassortant virus
vaccines derived from two different avian influenza virus donors. Journal
of Clinical Microbiology 27(1): 219-22.
ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: We compared the abilities of the six internal
RNA segments of two avian influenza viruses, A/Mallard/Alberta/88/76 (H3N8) and
A/Mallard/NY/6750/78 (H2N2), to confer attenuation on wild-type human influenza
A/Bethesda/1/85 (H3N2) virus in seronegative adult volunteers. Live avian-human
influenza A reassortant virus vaccines derived from either avian virus parent
were comparable in the following properties: safety, infectivity, immunogenicity,
and genetic stability. Since the avian influenza A/Mallard/Alberta/76 virus
offered no clear advantage as a donor virus, we will conduct our future
evaluations on live influenza A virus reassortants derived from the more
extensively characterized avian influenza A/Mallard/NY/78 virus.
Descriptors: antibodies, viral biosynthesis, influenza
prevention and control, influenza A virus avian immunology, human immunology,
influenza vaccine immunology, dose response relationship, immunologic,
electrophoresis, polyacrylamide gel, enzyme linked immunosorbent assay, genes
viral, hemagglutination inhibition tests, avian genetics, avian physiology,
human genetics, human physiology, influenza vaccine adverse effects, vaccines,
attenuated adverse effects, vaccines, attenuated immunology, vaccines,
synthetic adverse effects, vaccines, synthetic immunology, virus replication.
Clements, M.L., M.H. Snyder, A.J. Buckler White, E.L.
Tierney, W.T. London, and B.R. Murphy (1986). Evaluation of avian-human
reassortant influenza A/Washington/897/80 x A/Pintail/119/79 virus in monkeys
and adult volunteers. Journal of Clinical Microbiology 24(1):
47-51. ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: A reassortant influenza A virus was produced
by mating an avian influenza A/Pintail/Alberta/119/79 (H4N6) virus with
wild-type human influenza A/Washington/897/80 (H3N2) virus. The avian-human
influenza A reassortant virus contained the genes coding for the hemagglutinin
and neuraminidase surface antigens of the human influenza wild-type virus and
the six other RNA segments (internal genes) of the avian influenza A virus
donor. In the lower respiratory tract of squirrel monkeys, this avian-human
influenza reassortant virus, like its avian influenza A parent virus, was restricted
approximately 100-fold in replication compared with the wild-type human
influenza A virus. Despite this restriction of replication, infection of
monkeys with the avian-human influenza A reassortant virus induced resistance
to wild-type human influenza A virus challenge. In comparison with the
wild-type human influenza A virus, the avian-human influenza A reassortant was
also fully attenuated when 10(5.5) to 10(7.5) 50% tissue culture infective
doses were administered to susceptible adult volunteers. Attenuation was
indicated by a more than 300-fold reduction in virus shedding and lack of
reactogenicity. The reassortant virus did not spread to susceptible contacts
and could not be isolated from the blood or stools of infected adults. The 50%
human infectious dose was 10(6.2) 50% tissue culture infective dose, indicating
that this reassortant virus is only slightly less infectious for adults than a
similarly derived avian-human influenza A/Washington/80 X A/Mallard/78
reassortant virus. These findings suggest that the avian influenza A/Pintail/79
virus may be a satisfactory donor of attenuating genes for production of live,
attenuated avian-human influenza A reassortant virus vaccines.
Descriptors: influenza A virus human immunology,
immunology, influenza vaccine immunology, adolescent, adult, genes viral,
influenza immunology, influenza prevention and control, human genetics,
genetics, influenza vaccine adverse effects, saimiri, vaccines, attenuated
adverse effects, vaccines, attenuated immunology, virus replication.
Clements, M.L., E.K. Subbarao, L.F. Fries, R.A.
Karron, W.T. London, and B.R. Murphy (1992). Use of single-gene reassortant
viruses to study the role of avian influenza A virus genes in attenuation of
wild-type human influenza A virus for squirrel monkeys and adult human
volunteers. Journal of Clinical Microbiology 30(3): 655-62. ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: The transfer of six internal RNA segments
from the avian influenza A/Mallard/New York/6750/78 (H2N2) virus reproducibly
attenuates human influenza A viruses for squirrel monkeys and adult humans. To
identify the avian influenza A virus genes that specify the attenuation and
host range restriction of avian-human (ah) influenza A reassortant viruses (referred
to as ah reassortants), we isolated six single-gene reassortant viruses (SGRs),
each having a single internal RNA segment of the influenza A/Mallard/New
York/6750/78 virus and seven RNA segments from the human influenza A/Los
Angeles/2/87 (H3N2) wild-type virus. To assess the level of attenuation, we
compared each SGR with the A/Los Angeles/2/87 wild-type virus and a 6-2 gene ah
reassortant (having six internal RNA segments from the avian influenza A virus
parent and two genes encoding the hemagglutinin and neuraminidase glycoproteins
from the wild-type human influenza A virus) for the ability to replicate in
seronegative squirrel monkeys and adult human volunteers. In monkeys and
humans, replication of the 6-2 gene ah reassortant was highly restricted. In
humans, the NS, M, PB2, and PB1 SGRs each replicated significantly less
efficiently (P less than 0.05) than the wild-type human influenza A virus
parent, suggesting that each of these genes contributes to the attenuation
phenotype. In monkeys, only the NP, PB2, and possibly the M genes contributed
to the attenuation phenotype. These discordant observations, particularly with
regard to the NP SGR, indicate that not all genetic determinants of attenuation
of influenza A viruses for humans can be identified during studies of SGRs
conducted with monkeys. The PB2 and M SGRs that were attenuated in humans each
exhibited a new phenotype that was not observed for either parental virus.
Thus, it was not possible to determine whether avian influenza virus PB2 or M gene
itself or a specific constellation of avian and human influenza A virus
specified restriction of virus replication in humans.
Descriptors: influenza A virus avian genetics, human
genetics, adult, base sequence, genes viral, human pathogenicity, human
physiology, influenza vaccine isolation and purification, molecular sequence
data, RNA viral genetics, saimiri, transfection, vaccines, attenuated isolation
and purification, virulence genetics, virus replication genetics.
Cmarkova, J., D. Cmarko, E. Zavodska, A. Ellinger, M.
Pavelka, and F. Ciampor (1995). Ultrastructural lectinocytochemistry of fowl
plague virus-infected and uninfected MDCK cells. Acta Virologica
39(2): 85-93. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Using horseradish peroxidase (HRP)-conjugated
lectins for pre-embedding labelling we have shown differences in
ultrastructural localization of saccharides in cell compartments of fowl plague
(FP) virus-infected and uninfected MDCK cells. Lectinochemical staining of the cell
compartments in the case of FP virus-infected MDCK cells was less intensive as
compared with uninfected cells. Also certain differences in the staining of
subcompartments of cell organells were seen. Staining of uninfected cells with
Pisum sativum agglutinin (PSA)-HRP revealed an extensive visualization of Golgi
complex, mainly its cis-part, TGN vesicles and lysosomes. Staining of FP
virus-infected cells with the same lectin marked very lightly rough endoplasmic
reticulum and not at all the Golgi complex. Staining with Erythrina
cristagalli agglutinin (ECA)-HRP revealed a picture very similar to PSA-HRP
staining of uninfected and FP virus-infected cells. The differences in the
lectinochemical staining of cell organelles of FP virus-infected and uninfected
cells may be connected with the inhibition of cell protein synthesis during FP
virus morphogenesis.
Descriptors: influenza A virus avian chemistry, plant
lectins, antibodies, monoclonal immunology, cell line, dogs, hemagglutinin
glycoproteins, influenza virus, hemagglutinins viral metabolism, hemagglutinins
viral ultrastructure, immunoenzyme techniques, avian ultrastructure, lectins
metabolism.
Condobery, P.K. and R.D. Slemons (1992). Biological
properties of waterfowl-origin type A influenza viruses in chickens. Avian
Diseases 36(1): 17-23. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The replicative abilities and tissue tropism
properties of 13 non-pathogenic or low-pathogenic waterfowl-origin type A
influenza isolates recovered in 1986 were examined in chickens. Following
intravenous challenge, reisolation of challenge virus was attempted from swabs
of the luminal surfaces of the cloaca, jejunum, ileum, bursa, trachea, and air
sacs and from swabs of bone marrow and liver tissues. Virus-isolation attempts
were also accomplished on brain, thymus, spleen, pancreas, gonad, kidney,
blood, and lung tissues. The overall frequency of influenza virus recovery for
each experiment ranged from 3.1% to 49.3%. For all experiments combined, 58.3%
of the kidney tissues and 62.9% of the cloacal swab samples collected on days 1
to 10 postinoculation were positive for challenge virus recovery. Virus titers
up to 10(8.7) mean embryo infective dose per gram of kidney tissue were
demonstrated in clinically normal chickens. Distinct biological variations and
nephrotropism appear to exist among the corporate properties of virus
populations making up each of the 13 waterfowl-origin type A influenza
isolates.
Descriptors: chickens, fowl plague microbiology, influenza
A virus avian physiology, virus replication, antibodies, viral blood, chick
embryo, cloaca microbiology, avian immunology, avian isolation and
purification, kidney microbiology, serial passage, specific pathogen free
organisms.
Connor, R.J., Y. Kawaoka, R.G. Webster, and J.C.
Paulson (1994). Receptor specificity in human, avian, and equine H2 and H3
influenza virus isolates. Virology 205(1): 17-23. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The receptor specificity of 56 H2 and H3
influenza virus isolates from various animal species has been determined to
test the relevance of receptor specificity to the ecology of influenza virus.
The results show that the receptor specificity of both H2 and H3 isolates
evaluated for sialic acid linkage specificity and inhibition of
hemagglutination by horse serum correlates with the species of origin, as
postulated earlier for H3 strains based on a limited survey of five human,
three avian, and one equine strain. Elucidation of the amino acid sequence of several
human H2 receptor variants and analysis of known sequences of H2 and H3
isolates revealed that receptor specificity varies in association with an amino
acid change at residues 228 in addition to the change at residue 226 previously
documented to affect receptor specificity of H3 but not H1 isolates. Residues
226 and 228 are leucine and serine in human isolates, which preferentially bind
sialic acid alpha 2,6-galactose beta 1,4-N-acetyl glucosamine (SA alpha
2,6Gal), and glutamine and glycine in avian and equine isolates, which exhibit
specificity for sialic acid alpha-2,3-galactose beta-1,3-N-acetyl galactosamine
(SA alpha 2,3Gal). The results demonstrate that the correlation of receptor
specificity and species of origin is maintained across both H2 and H3 influenza
virus serotypes and provide compelling evidence that influenza virus hosts
exert selective pressure to maintain the receptor specificity characteristics
of strains isolated from that species.
Descriptors: influenza A virus avian metabolism, human
metabolism, metabolism, receptors, virus metabolism, amino acid sequence, amino
acids genetics, carbohydrate sequence, chick embryo, hemagglutinin
glycoproteins, influenza virus, hemagglutinins viral genetics, molecular
sequence data, species specificity, viral envelope proteins genetics.
Content, J. (1976). Cell-free translation of
influenza virus mRNA. Journal of Virology 18(2): 604-18. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Cytoplasmic poly (A)-rich RNA extracted from
fowl plague virus-infected cells was found to program efficiently the
translation of two major peptides in the wheat germ cell-free system. These
peptides have the same electrophoretic mobility, on polyacrylamide gels, as the
two major virion proteins M and NP. [35S] methionine tryptic peptide analysis
by one-dimensionalthin-layer ionophoresis and finger printing by
two-dimensional thin-layer ionophoresis and chromatography show a high degree
of similarity between the two in vitro products and the authentic viral proteins
M and NP. Although virion RNA is devoid of any poly (A) sequence, it is
confirmed here that the viral complementary cytoplasmic RNA contains poly (A)
stretches of varying lengths. Intact purified virion was found to promote the
synthesis of very low amounts of the same NP and M proteins in this cell-free system. Quantitative aspects
of data would indicate that this is due to minute amounts of complementary
viral RNA associated with the virion or with the virion RNA itself. In
conclusion, it is shown diectly by cell-free translation of authentic viral
products that the influenza virion is "negative stranded" (Baltimore,
1971), at least for its two major structural proteins.
Descriptors: influenza A virus avian metabolism, RNA,
messenger metabolism, RNA viral metabolism, translation, genetic, cell free
system, glycoproteins biosynthesis, avian analysis, peptide synthesis, plant
extracts, poly A analysis, RNA, messenger analysis, viral analysis, tissue
culture, triticum, viral proteins biosynthesis.
Content, J. (1969). Virus growth inhibition by
ethidium chloride and other dyes. Archiv Fur Die Gesamte Virusforschung
26(1): 74-85. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: dactinomycin pharmacology, dyes pharmacology,
virus replication drug effects, acridines pharmacology, carbon isotopes, chick
embryo, encephalitis viruses drug effects, encephalomyocarditis virus drug
effects, fibroblasts, herpesviridae drug effects, influenza A virus avian drug
effects, light, Newcastle disease virus drug effects, orotic acid metabolism,
polioviruses drug effects, tissue culture, uridine metabolism, vaccinia virus
drug effects.
Content, J., L.D. Wit, and M. Horisberger (1977). Cell-free
coupling of influenza virus RNA transcription and translation. Journal
of Virology 22(2): 247-55. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: A cell-free coupled system for the
transcription and translation of fowl plague virus RNA is described. The system
utilizes a new nuclease-preincubated rabbit reticulocyte lysate that has a high
sensitivity to exogenous mRNA and a very low level of nuclease activity.
Translation of the viral proteins in the coupled system is strictly dependent
upon the viral transcriptase activity. In the coupled system the optimal concentration
of magnesium is intermediate between the optimum for transcription and that for
translation. Translation of the viral proteins seems faithful. The products
represent the major viral peptides M and NP and two peptides with the same
electrophoretic mobility as HA and P2. Viron NA is not resolved in the kind of
polyacrylamide gels described. Proteins M and NP were immunoprecipitable with
monospecific antisera. It is concluded that the virion-associated RNA
polymerase transcribes the negative-stranded segments of the viral genome
coding for these major structural proteins into fully functional mRNA's.
Descriptors: influenza A virus avian metabolism, RNA viral
metabolism, transcription, genetic, translation, genetic, cell free system,
avian enzymology, magnesium metabolism, oligonucleotides pharmacology, peptide
synthesis, RNA replicase metabolism, messenger metabolism, viral biosynthesis,
rabbits, reticulocytes, viral proteins biosynthesis.
Conti, G. and P. Portincasa (2002). Chromomycin A3
inhibits influenza a virus multiplication in chick embryo fibroblast cells.
New Microbiologica Official Journal of the Italian Society for Medical,
Odontoiatric, and Clinical Microbiology SIMMOC 25(4): 385-98. ISSN: 1121-7138.
NAL
Call Number: QR1.M57
Abstract: The multiplication of Ulster 73 virus, an
avian strain of type A influenza virus, was blocked in chick embryo fibroblast
cells, CEF, by treatment with 0.5 microg/ml of chromomycin A3 whereas in
LLC-MK2 cells no inhibition of replication was observed. Virus-induced
polypeptide synthesis in chick embryo fibroblast cells was confined to the
synthesis of PB2, PB1 and PA subunits of the RNA dependent-RNA polymerase, the
nucleoprotein NP, the non-structural protein NS1, the haemagglutinin HA, the
non-structural protein NS2; only the membrane M1 polypeptide synthesis was
greatly inhibited. Viral unpolyadenylated cRNAs synthesis was studied at a late
time of the infection, 8 hours p.i.: chromomycin A3 was able to inhibit the
"novo" synthesis of complementary RNA poly(A)- and segment 7 of
virion RNA. The mode of action of the drug in chick embryo fibroblast cells is
discussed.
Descriptors: chromomycin A3 pharmacology, fibroblasts drug
effects, influenza A virus avian drug effects, nucleic acid synthesis
inhibitors pharmacology, virus replication drug effects, cell line, chick
embryo, electrophoresis, polyacrylamide gel, fibroblasts virology, avian
physiology, RNA viral biosynthesis, RNA viral genetics, virus cultivation.
Conti, G., P. Portincasa, and C. Chezzi (1995). Cerulenin
inhibits production of mature virion particles in chick embryo fibroblasts
infected by influenza A viruses. Research in Virology 146(2):
141-9. ISSN: 0923-2516.
NAL
Call Number: QR355.A44
Abstract: We investigated acylation of haemagglutinin
(HA) of type A influenza viruses during infection of permissive chick embryo
fibroblasts (CEF) treated with cerulenin. Fatty acid binding was monitored
using a maintenance medium containing 3H-palmitic acid. Our results suggest
that fatty acid acylation of viral haemagglutinin may be essential for
production of mature viral particles. Indeed, palmitoylation was found in
infected CEF cells, but was lacking during the infectious cycle when cells were
treated with a dose of 30 micrograms/ml of cerulenin. We discuss the
possibility that acylation of virus-induced HA is a posttranslational
modification regulating correct insertion of virus haemagglutinin into the
cellular membrane and, as a consequence, controlling the maturation of budding
influenza virus.
Descriptors: antiviral agents pharmacology, cerulenin
pharmacology, influenza A virus avian drug effects, virion drug effects,
acylation, cells,cultured, chick embryo, dose response relationship, drug,
fatty acids metabolism, fibroblasts cytology, hemagglutinin glycoproteins
influenza virus, hemagglutinins viral metabolism, avian metabolism, avian
physiology, virus replication drug effects.
Conti, G., P. Portincasa, C. Chezzi, and A. Sanna
(1988). Inhibition of late influenza virus genome expression by
diamidinophenylindole. Annales De L'Institut Pasteur. Virology
139(1): 69-78. ISSN: 0769-2617.
NAL
Call Number: QR355.A44
Abstract: The growth cycle of influenza virus strain
FPV, Ulster 73, was altered by treatment of LLC-MK2 cells with
diamidinophenylindole. Viral protein synthesis was restricted to the early
pattern of virus multiplication, and post-treatment experiments showed the
ability of the drug to block virus replication until the 4th hour p.i. Drug
addition (followed by removal) revealed the inhibition of synthesis of late
viral products, and especially of membrane protein. Kinetic studies on the
production of viral RNA indicated a decrease in the synthesis of late
virus-induced RNA species, suggesting that the target of DAPI is probably the
late transcription of the virus genome. The nonpermissive condition mediated by
the drug could represent a suitable model to study cellular intervention during
viral growth.
Descriptors: indoles pharmacology, influenza A virus avian
growth and development, virus replication drug effects, capsid genetics, gene
expression regulation drug effects, avian genetics, RNA viral biosynthesis, RNA
viral genetics, time factors, viral core proteins genetics, viral nonstructural
proteins.
Conti, G., P. Portincasa, A. Pesce, and C. Chezzi
(1985). Biological characterization of FPV, Ulster 73, replicative cycle.
Microbiologica 8(2): 151-64. ISSN: 0391-5352.
NAL
Call Number: QR1.M57
Abstract: The replication of an avian influenza A, Fowl
plague virus (FPV), Ulster 73 strain, was studied in chick embryo fibroblasts,
assumed to be the natural host, and in cells of different origin such as
LLC-MK2, Hep-2, Vero, KB and Mc Coy. In the natural host, FPV shows a characteristic
pattern of polypeptide synthesis suggesting a transcriptional and/or
translational mediated control mechanism, specific for this strain of influenza
A. FPV was able to give a productive infection in all the above mentioned cells
releasing mature viral particles. This behaviour is very interesting if one
compares FPV, Ulster strain to FPV, Rostock strain. These viruses, belonging to
the same antigenic subtype (H7 N1 group) recognize the same cellular
determinants but Rostock strain undergoes an abortive replication whereas
Ulster strain gives productive infection in all cellular lines tested. These
observations lead to postulate a viral genetic mechanism controlling host range
both at early and late steps in infection. This genetic mechanism controls the
interaction between viral and cell molecules affecting synthesis of virus
specific polypeptides.
Descriptors: influenza A virus avian physiology, virus
replication, chick embryo, dactinomycin pharmacology, avian genetics, RNA
viral analysis, viral proteins analysis, viral proteins biosynthesis, viral
structural proteins.
Conti, G., P. Valcavi, A. Natali, and G.C. Schito
(1980). Different patterns of replication in influenza virus-infected KB
cells. Archives of Virology 66(4): 309-20. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: When KB cells were infected either with the
fowl plague (FPV) Rostock strain (Hav1N1) or the WSN (H0N1) strain of influenza
A virus the yield of cell-associated haemagglutinin and neuraminidase
polypeptides was essentially comparable, but virus particles were not produced
in the FPV-KB system. WSN virus-infected KB cells synthesized normal amounts of
mature virus particles and had all the characteristics of a permissive
replication cycle. Biosynthesis and transport of RNP antigen from nucleus to
cytoplasm of infected cells were traced by immunofluorescent staining at 4 and
8 hours after the beginning of infection. While the fluorescent-stained
material was totally confined to the nuclei in FPV-infected KB cells, RNP antigen
migrated out of the nucleus during the replicative cycle of WSN virus in the
same host cell. Patterns of virus-specific protein synthesis were studied by
pulse-labelling with 35S-methionine. The most significant feature concerned the
amplification of synthesis of virus-induced matrix (M) protein which did not
occur in FPV-infected cells but occurred normally during WSN infection. The
different patterns of replication in the same host cell when infected by
different influenza A viruses is discussed.
Descriptors: influenza A virus avian growth and
development, human growth and development, cell line, cytopathogenic effect,
viral, hemagglutinins viral analysis, avian metabolism, human metabolism,
neuraminidase metabolism, ribonucleoproteins metabolism, viral proteins
biosynthesis, virus replication.
Cook, R.F., R.J. Avery, and N.J. Dimmock (1980). Complementation
with an avian influenza virus is required for synthesis of M protein of a human
strain in chicken erythocytes. Archives of Virology 65(3-4): 319-24. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The M protein of avian, but not human,
strains of influenza A viruses is synthesized in infected chicken erythrocytes.
In dual infections an avian strain complemented the human virus and both the
human and avian M proteins were expressed.
Descriptors: erythrocytes microbiology, influenza A virus
avian metabolism, human metabolism, viral proteins biosynthesis, chick embryo,
dactinomycin pharmacology, avian growth and development, human growth and
development.
Cook, R.F., R.J. Avery, and N.J. Dimmock (1979). Infection
of chicken erythrocytes with influenza and other viruses. Infection and
Immunity 25(1): 396-402. ISSN:
0019-9567.
NAL
Call Number: QR1.I57
Abstract: Chicken erythrocytes can be infected by the
fowl plague (Rostock) strain (FP/R) of influenza type A, Newcastle disease
virus (NDV), and Semliki Forest virus (SFV). Only NDV and SFV produced
infectious progeny, albeit at low levels. Infection by FP/R was monitored by de
novo synthesis of viral proteins, and the proteins synthesized could be
identified by comparison with infected chicken fibroblast cells. FP/R
synthesized far greater amounts of viral protein than did NDV or SFV.
Descriptors: erythrocytes microbiology, chick embryo,
hemagglutinins viral analysis, influenza A virus avian growth and development,
avian metabolism, leukocytes microbiology, neuraminidase metabolism, Newcastle
disease virus growth and development, Newcastle disease virus metabolism,
Semliki Forest virus growth and development, Semliki Forest virus metabolism,
viral proteins biosynthesis.
Cooper, L.A. and K. Subbarao (2000). A simple
restriction fragment length polymorphism-based strategy that can distinguish
the internal genes of human H1N1, H3N2, and H5N1 influenza A viruses. Journal
of Clinical Microbiology 38(7): 2579-83.
ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: A simple molecular technique for rapid
genotyping was developed to monitor the internal gene composition of currently
circulating influenza A viruses. Sequence information from recent H1N1, H3N2,
and H5N1 human virus isolates was used to identify conserved regions within
each internal gene, and gene-specific PCR primers capable of amplifying all
three virus subtypes were designed. Subtyping was based on subtype-specific
restriction fragment length polymorphism (RFLP) patterns within the amplified
regions. The strategy was tested in a blinded fashion using 10 control viruses
of each subtype (total, 30) and was found to be very effective. Once
standardized, the genotyping method was used to identify the origin of the
internal genes of 51 influenza A viruses isolated from humans in Hong Kong
during and immediately following the 1997-1998 H5N1 outbreak. No avian-human or
H1-H3 reassortants were detected. Less than 2% (6 of 486) of the RFLP analyses
were inconclusive; all were due to point mutations within a restriction site.
The technique was also used to characterize the internal genes of two avian
H9N2 viruses isolated from children in Hong Kong during 1999.
Descriptors: genes viral, influenza virology, influenza A
virus human classification, human genetics, polymorphism, restriction fragment
length, disease outbreaks, Hong Kong, avian classification, avian genetics,
avian isolation and purification, human isolation and purification, reverse
transcriptase polymerase chain reaction.
Corfield, A.P., H. Higa, J.C. Paulson, and R. Schauer
(1983). The specificity of viral and bacterial sialidases for alpha(2-3)-
and alpha(2-6)-linked sialic acids in glycoproteins. Biochimica Et
Biophysica Acta 744(2): 121-6. ISSN:
0006-3002.
NAL
Call Number: 381 B522
Abstract: The anomeric specificity of six sialidases (Vibrio
cholerae, Arthrobacter ureafaciens, Clostridium perfringens, Newcastle
disease virus, fowl plague virus and influenza A2 virus sialidases) was
assessed with sialylated antifreeze glycoprotein, ovine submandibular gland
glycoprotein and alpha 1-acid glycoprotein, resialylated specifically in
alpha(2-3) or alpha(2-6) linkage with N-acetylneuraminic acid or
N-glycolylneuraminic acid using highly purified sialyltransferases. The rate of
release of sialic acid from these substrates was found to correlate well with
the specificity observed earlier with the same sialidases using small oligosaccharide
substrates, i.e., alpha(2-3) glycosidic linkages are hydrolyzed faster than
alpha(2-6) linkages, with the exception of the enzyme from A. ureafaciens.
Sialidase activity was higher with N-acetylneuraminic acid when compared with
N-glycolylneuraminic acid. The studies also showed that the core
oligosaccharide and protein structure in glycoproteins may influence the rate
of release for different glycosidic linkages.
Descriptors: glycoproteins metabolism, neuraminidase
metabolism, sialic acids metabolism, arthrobacter enzymology, Clostridium
perfringens enzymology, influenza A virus avian enzymology, enzymology,
Newcastle disease virus enzymology, structure activity relationship, substrate
specificity, vibrio cholerae enzymology.
Corfield, A.P., M. Wember, R. Schauer, and R. Rott
(1982). The specificity of viral sialidases. The use of oligosaccharide
substrates to probe enzymic characteristics and strain-specific differences.
European Journal of Biochemistry FEBS 124(3): 521-5. ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: 1. The action of sialidases from Newcastle
disease virus (NDV), influenza A2 virus (IA2V) and fowl plague virus (FPV) on
sialyloligosaccharide substrates containing alpha 2-3, alpha 2-6 or alpha 2-8
linkages was studied. 2. In all cases 2-3-linked sialic acids were
preferentially released. Compared with II6Neu5AcLac, all 2-6-linked substrates,
including sialyl-N-acetyllactosamine and its asparaginyl derivative, a urinary
hexasaccharide and Neu5Ac(2-6)GalNAc were cleaved at improved rates by NDV and
less by FPV sialidases. In the case of IA2V sialidase the asparaginyl
oligosaccharide was very poorly cleaved, illustrating a variation in viral
strain specificity. 3. A decrease in relative rates was observed in the order NDV
greater than IA2V greater than FPV for substrates with 2-3 linkages relative to
II6Neu5AcLac. The greatest relative rate was 470-fold higher. The 2-3-linked
sialyl-N-acetyllactosaminylasparagine and IV3Neu5AcLcOse4 were poor substrates
for the IA2V sialidase, but the rates were greater than with the 2-6 linked
substrates. 4. The ganglioside substrate II3Neu5AcLacCer showed lower activity
than its oligosaccharide analogue, but neither II3Neu5AcGgOse4Cer nor its
oligosaccharide were substrates. 5. The Km values for 2-6-linked substrates
were generally of the order 10 mM while those for the 2-3-linked substrates
were approximately 1 mM. The V values were consistently higher for the
2-3-linked substrates. IV3Neu5AcLcOse4 showed high Km and very high V values, while
the 2-8-linked disialyllactose showed this trend only with NDV enzyme, the IA2V
and FPV sialidases exhibiting high Km and low V values. 6. The results are
discussed in the light of the current knowledge of viral sialidase specificity
and relative to the binding of virus particles to cell surfaces.
Descriptors: neuraminidase metabolism, oligosaccharides
metabolism, viruses enzymology, colorimetry, glycoproteins metabolism,
influenza A virus avian enzymology, enzymology, kinetics, Newcastle disease virus
enzymology, species specificity, substrate specificity.
Cox, N.J. and R.D. Barry (1976). Hybridization
studies of the relationship between influenza virus RNA and cellular DNA. Virology
69(1): 304-13. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: DNA analysis, influenza A virus avian
analysis, nucleic acid hybridization, RNA, ribosomal analysis, viral analysis,
bromelains pharmacology, genes, avian drug effects, avian isolation and
purification, kinetics, temperature, transcription, genetic.
Crawford, J.M., M. Garcia, H. Stone, D. Swayne, R.
Slemons, and M.L. Perdue (1998). Molecular characterization of the
hemagglutinin gene and oral immunization with a waterfowl-origin avian
influenza virus. Avian Diseases 42(3): 486-496. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Vaccination against highly pathogenic (HP)
subtypes of avian influenza (AI) virus in poultry has been prohibited in the
United States. Recently, policy has been changed to potentially allow use of
inactivated vaccines in emergency programs to control HP H5 and H7 AI.
Vaccination with inactivated virus against non-highly pathogenic AI viruses has
been allowed in the U.S. turkey industry since 1979 (1) but requires expensive
handling of individual birds for parenteral inoculation. Oral immunization
would provide a less expensive method to protect commercial poultry from AI.
Prime candidates for oral vaccines are waterfowl-origin (WFO) isolates, which
have a tropism for the alimentary tract. One WFO isolate, A/mallard/Ohio/556/1987
(H5N9) (MOh87), was characterized by determining the complete nucleotide
sequence of its hemagglutinin (HA) gene. The HA protein of this isolate
possessed a deduced amino acid sequence nearly identical to the consensus amino
acid sequence for all published H5 genes, indicating that it has potential as a
broadly effective vaccine. Experimental results demonstrated measurable serum
antibody responses to orally delivered live and inactivated preparations of
MOh87. Oral vaccination also protected chickens from diverse, lethal H5 AI
virus challenge strains and blocked cloacal shedding of challenge virus.
Descriptors: avian influenza virus, chickens,
hemagglutinins, immunization, oral administration, genes, oral vaccination,
virulence, live vaccines, inactivated vaccines, experimental infections, strain
differences, nucleotide sequences, amino acid sequences, immune response,
molecular sequence data, GENBANK u67783.
Crescenzo Chaigne, B., S. van der Werf, and N.
Naffakh (2002). Differential effect of nucleotide substitutions in the 3'
arm of the influenza A virus vRNA promoter on transcription/replication by
avian and human polymerase complexes is related to the nature of PB2 amino acid
627. Virology 303(2):
240-52. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Using a genetic system that allows the in
vivo reconstitution of active ribonucleoproteins, the ability to ensure
transcription/replication of a viral-like reporter RNA harboring the G(3)
--> A(3), U(5) --> C(5), and C(8) --> U(8) mutations (triple 3-5-8
mutations) in the 3' arm of the promoter was examined with core proteins from
human or avian strains of influenza A viruses. The efficiency of
transcription/replication of the viral-like RNA with the triple 3-5-8 mutations
in COS-1 cells was found to be slightly decreased as compared to the wild-type
RNA when the polymerase was derived from a human virus. In contrast, it was
found to be considerably increased when the polymerase was derived from an
avian virus, in agreement with published observations using the avian
A/FPV/Bratislava virus (G. Neumann and G. Hobom, 1995, J. Gen. Virol. 76,
1709-1717). This increase could be attributed to the compensation of the defect
in transcription/replication activity in the COS-1 mammalian cell line due to
the presence of a glutamic acid at PB2 residue 627, characteristic of avian
strains of influenza viruses. Our results thus suggest that PB2 and/or cellular
proteins interacting with PB2 could be involved in RNA conformational changes
during the process of transcription/replication.
Descriptors: DNA directed RNA polymerases physiology,
influenza A virus avian enzymology, human enzymology, promoter regions
genetics, viral chemistry, transcription, genetic, viral proteins chemistry,
virus replication, amino acid sequence, base sequence, cos cells, molecular
sequence data, mutation, nucleic acid conformation, viral biosynthesis.
Crumpton, W.M., N.J. Dimmock, P.D. Minor, and R.J.
Avery (1978). The RNAs of defective-interfering influenza virus. Virology
90(2): 370-3. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: defective viruses analysis, influenza A virus
avian, RNA viral analysis, defective viruses growth and development, defective
viruses metabolism, viral proteins biosynthesis.
Dammgen, J.W. and C. Scholtissek (1975). Cellular
RNA and influenza-virion RNA are synthesized from different
pyrimidine-nucleoside-triphosphate pools in chick-embryo cells. European
Journal of Biochemistry FEBS 59(1): 51-4.
ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: Chick embryo cells infected with an influenza
A (fowl plague) virus have been labelled with (3H)-uridine for different
lengths of time. Virion RNA and cellular RNA have been separated by specific
hybridization with a surplus of unlabelled viral complementary RNA and RNase
digestion. The ratio of the specific radioacticity in the UMP and CMP moieties
of both types of RNA has been determined. Since the rate of approach to
equilibrium of CMP to UMP labelling of both types of RNA is completely
different it is concluded that cellular and virion RNA are synthesized using
different pyrimidine nucleoside triphosphate pools.
Descriptors: influenza A virus avian metabolism,
pyrimidine nucleotides metabolism, RNA biosynthesis, RNA viral biosynthesis,
cells cultured, chick embryo, nucleic acid hybridization, transcription,
genetic, uridine metabolism.
Daniels, R.S., J.J. Skehel, and D.C. Wiley (1985). Amino
acid sequences of haemagglutinins of influenza viruses of the H3 subtype
isolated from horses. Journal of General Virology 66(Pt. 3):
457-64. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The amino acid sequence of the haemagglutinin
of A/equine/Miami/63 (H3N8), the prototype influenza virus of the H3 subtype
from horses, is deduced from the nucleotide sequence of virus RNA and compared
with the sequences of haemagglutinins of viruses of this subtype isolated from
humans [X-31 (H3N2)] and from birds [A/duck/Ukraine/63 (H3N8)] and with the
sequence of the haemagglutinin of A/equine/Fontainebleau/79 (H3N8) a virus
isolated from a recent outbreak of equine influenza. The amino acid sequence
differences detected are discussed with reference to the structure of the
molecules, their antigenicity and antigenic drift in influenza viruses viruses
isolated from horses.
Descriptors: hemagglutinins viral, influenza A virus
genetics, amino acid sequence, avian genetics, immunology, RNA viral genetics,
species specificity, horses.
Darveau, A., N.G. Seidah, M. Chretien, and J. Lecomte
(1982). Peptide mapping of 125I-labelled membrane protein of influenza
viruses by reverse-phase high-performance liquid chromatography. Journal
of Virological Methods 4(2): 77-85.
ISSN: 0166-0934.
NAL
Call Number: QR355.J6
Abstract: The resolution potential of reverse-phase
high-performance liquid chromatography (HPLC) for peptide analysis of
hydrophobic viral membranes has been investigated, using as model the membrane
(M) protein of influenza virus. Proteolytic digests of 125I-labelled M protein
and CNBr fragments, extracted from radioiodinated whole virus, have been
separated on a uBondapak C18 column with an isopropanol or acetonitrile solvent
system. Peptide mapping of trypsin digests of M protein from A/PR/8/34 (H1N1)
and A/chicken/Germany/N/49 (H10N7) viruses was identical, whereas Staphylococcus
aureus V8 protease digests showed minor differences in at least two
peptides. The results also show that HPLC is a powerful tool for the separation
of proteolytic digests of viral proteins, since the peptide maps are highly
reproducible and recovery was greater than 85%.
Descriptors: chromatography, high pressure liquid methods,
influenza A virus avian analysis, membrane proteins analysis, peptides
analysis, viral proteins analysis, electrophoresis, polyacrylamide gel, iodine
radioisotopes.
Datema, R., P.A. Romero, R. Rott, and R.T. Schwarz
(1984). On the role of oligosaccharide trimming in the maturation of Sindbis
and influenza virus. Archives of Virology 81(1-2): 25-39. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The alpha-glucosidase inhibitor
bromoconduritol inhibits the formation of the N-linked, complex-type
oligosaccharides of the glycoproteins from influenza viruses (fowl plague
virus, influenza virus PR-8) and from sindbis virus. Viral glycoproteins
produced in bromoconduritol-treated chicken-embryo and baby-hamster kidney
cells are fully glycosylated, but accumulate N-linked, high-mannose
oligosaccharides of the composition Glc1Manx (GlcNAc)2 (x = 7, 8, and 9). Other
alpha-glucosidase inhibitors (nojirimycin, deoxynojirimycin, acarbose) were not
specific inhibitors of oligosaccharide processing under the conditions used in
the present investigation. In bromoconduritol-treated, sindbis virus-infected
chicken-embryo and baby-hamster kidney cells, the sindbis glycoproteins are
metabolically stable. Specific proteolytic cleavage of the polyprotein
precursors to form E2 and E1 occurs in bromoconduritol-treated chicken-embryo
cells, but cleavage of PE2 to E2 is prevented in the infected baby-hamster
kidney cells. Yet, release of infectious sindbis virus particles is inhibited
in both cell types indicating that the formation of complex oligosaccharides is
required for a late step in virus formation. The release of virus particles
from influenza virus PR-8-infected bromoconduritol-treated chicken-embryo cells
is not inhibited, and virus with only high-mannose oligosaccharides is formed.
In contrast, when chicken-embryo cells were infected with the influenza virus
fowl plague virus, release of infectious particles was inhibited. The fowl
plague virus hemagglutinin is cleaved in chicken-embryo cells, in contrast to
the hemagglutinin of the PR-8 virus. However, the cleavage products HA1 and HA2
do not reach the cell surface. In addition, or as a consequence, HA1 and HA2
are proteolytically broken down, whereas uncleaved hemagglutinin of PR-8
appeared metabolically stable. These results may explain the decrease in
formation of fowl plague virus particles and the lack of effect on PR-8 virus
in bromoconduritol-treated cells. This work thus shows different biological
roles for oligosaccharide processing.
Descriptors: glycoproteins biosynthesis, influenza A virus
avian growth and development, oligosaccharides metabolism, sindbis virus growth
and development, viral proteins biosynthesis, cell line, chick embryo,
glycoproteins isolation and purification, glycoside hydrolases antagonists and
inhibitors, hamsters, avian drug effects, inositol analogs and derivatives,
inositol pharmacology, kidney, oligosaccharides isolation and purification,
sindbis virus drug effects, viral proteins isolation and purification.
Davenport, F.M., A.V. Hennessy, and E. Minuse (1968).
The age distribution in humans of hemagglutinating-inhibiting antibodies
reacting with avian strains of influenza A virus. Journal of Immunology
100(3): 581-5. ISSN: 0022-1767.
NAL
Call Number: 448.8 J8232
Descriptors: antibodies analysis, influenza immunology,
influenza A virus avian immunology, adolescent, adult, aged, aging, child,
child preschool, hemagglutination inhibition tests, infant, middle aged,
statistics.
Davey, J., S.M. Hurtley, and G. Warren (1985). Reconstitution
of an endocytic fusion event in a cell-free system. Cell 43(3 Pt.
2): 643-52. ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Abstract: Using a cell-free system we have obtained
fusion of vesicles from the endocytic pathway. The fusion is rapid, efficient,
and requires ATP. Only vesicles derived from certain positions along the
endocytic pathway are capable of fusing. Lysosomes and vesicles derived from
the plasma membrane do not fuse.
Descriptors: endocytosis, membrane fusion, adenosine
triphosphate physiology, cell line, cell membrane physiology, cell free system,
hamsters, influenza A virus avian, kidney, lysosomes physiology, mesocricetus,
Semliki Forest virus, sialic acids analysis.
Davies, P. and R.D. Barry (1966). Nucleic acid of
influenza virus. Nature 211(47): 384-7. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: orthomyxoviridae analysis, RNA viral
analysis, aphthovirus analysis, centrifugation, density gradient, encephalitis
viruses analysis, influenza A virus avian analysis, molecular weight, Newcastle
disease virus analysis, phosphorus isotopes, rauscher virus analysis, sarcoma
viruses, avian analysis, spectrum analysis.
Deibel, R., D.E. Emord, W. Dukelow, V.S. Hinshaw, and
J.M. Wood (1985). Influenza viruses and paramyxoviruses in ducks in the
Atlantic flyway, 1977-1983, including an H5N2 isolate related to the virulent
chicken virus. Avian Diseases 29(4): 970-85. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: From 1977 to 1983, waterfowl migrating along
the Atlantic flyway were annually monitored for orthomyxoviruses and
paramyxoviruses in an area in central New York State. A total of 168 influenza
isolates were obtained from 1,430 waterfowl. Twenty-four combinations of
hemagglutinin and neuraminidase subtypes were detected, with as many as 12
found in a single year. One combination, an H5N2 isolate in 1982, was closely
related to the virulent chicken virus that appeared in Pennsylvania in 1983.
The prevalence of influenza varied greatly among the common waterfowl species:
mallards 42%, black ducks 30%, blue-winged teal 11%, wood ducks 2%, and Canada
geese 0%. A total of 89 paramyxoviruses were also from these waterfowl. In
contrast to findings with influenza virus, the prevalence of paramyxoviruses
did not differ significantly among the duck species. Serotype 1 (Newcastle
disease virus) was predominant; three other serotypes were also identified.
These findings indicated that ducks in the Atlantic flyway continually harbor
influenza viruses and paramyxoviruses. The viruses may be a source of infection
for other species.
Descriptors: ducks microbiology, influenza A virus avian
isolation and purification, orthomyxoviridae isolation and purification,
paramyxoviridae isolation and purification, antigens, viral analysis,
demography, New York, species specificity.
Dem'ianenko, I.V., Z.I. Rovnova, E.I. Isaeva, and
Z.K. Chuvakova (1989 ). Antigennaia struktura gemaggliutininov virusov
grippa H1N1 (Hsw1N1), vydelennykh ot liudei i utok. [Antigenic structure of
hemagglutinins of influenza H1N1 (Hsw1N1) virus isolated from humans and ducks].
Voprosy Virusologii 34(6): 661-5.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The method of specific adsorption followed by
the use of antisera in HI test and competitive enzyme immunoassay was used to
study the antigenic composition of hemagglutinins (HA) Hsw1 in influenza
viruses isolated in 1982 from humans in Bulgaria and in 1976 in Canada from
ducks as well as their antigenic relationships with HA of Hsw1 variant isolated
from swine and man. Hemagglutinins of Hsw1 strains isolated from man in
Bulgaria and Alma-Ata were found to be similar to HA of A/New Jersey/8/76 virus
in two determinants and with hemagglutinin of the classic virus of swine in
three determinants. The HA of A/duck/Alberta/35/76 virus was similar in three
determinants to HA of A/New Jersey/8/76 virus and in two determinants with
other Hsw1 variants. The similarities and differences in antigenic determinants
of HA in Hsw1 viruses isolated from man and animals attest to their common
origin and different modes of variability.
Descriptors: epitopes analysis, hemagglutinins viral
immunology, influenza A virus avian immunology, human immunology, ducks, enzyme
linked immunosorbent assay, immunosorbent techniques.
Dem'ianenko, I.V., A.A. Shilov, Z.K. Chuvakova, O.V.
Chaika, and E.I. Isaeva (1988). Sravnitel'naia kharakteristika
gemaggliutinov virusov grippa A s antigennoi strukturoi Hsw1N1, vydelennykh ot
cheloveka i zhivotnykh. [Comparative characteristics of hemagglutinins of
influenza A viruses with antigenic structure Hsw1N1 isolated from man and
animals]. Voprosy Virusologii 33(2): 157-62. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Competitive radioimmunoassay was used to
study the antigenic composition of hemagglutinin of Hsw1N1 viruses isolated
from man in comparison with hemagglutinin Hsw1 of influenza virus of swine and
ducks. The data of oligonucleotide analysis of the 4th RNA segment coding for
hemagglutinin in these viruses are presented. It has been shown that in
Alma-Ata, 1984-1985, influenza viruses Hsw1N1 were isolated with the antigenic
structure of hemagglutinin and with the hemagglutinin gene identical with those
of the classical influenza virus of swine A/Swine/Iowa/15/30 but differing from
virus A/New Jersey/8/76.
Descriptors: antigens, viral analysis, hemagglutinins
viral analysis, influenza A virus avian immunology, human immunology,
influenza A virus porcine immunology, immunology, adsorption, antigens, viral
genetics, binding, competitive, ducks, genes viral, hemagglutinins viral
genetics, avian genetics, avian isolation and purification, human genetics,
human isolation and purification, porcine genetics, porcine isolation and
purification, Kazakhstan, oligonucleotides analysis, oligonucleotides genetics
, RNA viral analysis, viral genetics,
radioimmunoassay methods, swine.
Desheva, J.A., L.G. Rudenko, G.I. Alexandrova, X. Lu,
A.R. Rekstin, J.M. Katz, N.J. Cox, and A.I. Klimov (2004). Reassortment
between avian apathogenic and human attenuated cold-adapted viruses as an
approach for preparing influenza pandemic vaccines. International
Congress Series 1263: 724-727.
Abstract: To prepare candidate influenza pandemic vaccines,
we are developing an approach based on reassortment of antigenically
appropriate nonpathogenic avian viruses of different subtypes (H5, H9, H7) with
the cold-adapted master strain (MS) A/Leningrad/134/17/57 (Len/17) that is
currently used in Russia for preparing licensed live attenuated vaccines for
adults and children. In the present study, reassortants between
A/Duck/Potsdam/1402-6/86(H5N2) (H5N2-wt) and Len/17 were obtained. One of the
clones, A/17/Duck/Potsdam/86-92(H5N2) (Len17/H5), was chosen for further
detailed genetic and antigenic analysis. Len17/H5 inherited the HA gene from
the H5N2-wt and all other genes from Len/17 (7:1 genome composition). The HA
gene sequence of Len17/H5 was identical to that of the parent H5N2-wt virus.
The antigenic profile of the reassortant virus was similar to that of the
H5N2-wt parent strain in the hemagglutination-inhibition (HI) test with a panel
of antisera to different avian and human H5 viruses. The reassortant
demonstrated high growth ability (9.3+0.3 lg EID50/ml) in embryonated hens'
eggs (CE) at optimal (34 [deg]C) temperature, comparable with that of the
parent Len/17 MS. Also, Len17/H5 demonstrated cold-adapted (ca) and
temperature-sensitive (ts) phenotypes similar to those of Len/17 and was
attenuated for mice.
Descriptors: avian influenza, live attenuated reassortant
vaccine.
Deshpande, K.L., V.A. Fried, M. Ando, and R.G.
Webster (1987). Glycosylation affects cleavage of an H5N2 influenza virus
hemagglutinin and regulates virulence. Proceedings of the National
Academy of Sciences of the United States of America 84(1): 36-40. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Based on nucleotide sequence analysis of the
hemagglutinin (HA) gene from the virulent and avirulent A/chicken/Pennsylvania/83
influenza viruses, it was previously postulated that acquisition of virulence
was associated with a point mutation that resulted in loss of a glycosylation
site. Since there are two potential glycosylation sites in this region of the
HA molecule and since all Asn-Xaa-Thr/Ser sequences in the HAs of different
strains are not necessarily glycosylated, the question remained open as to
whether either one of these sites was glycosylated. We now provide direct
evidence that a site-specific glycosylation affects cleavage of the influenza
virus HA and thus virulence. We have identified the glycosylation sites on the
HA1 subunit from the virulent and avirulent strains by direct structural
analysis of the isolated proteins. Our results show that the only difference in
glycosylation between the HA1s of the virulent and avirulent strains is the
lack of an asparagine-linked carbohydrate on the virulent HA1 polypeptide at
residue 11. Further, we show that the HA1s of both the avirulent and virulent
viruses are not glycosylated at one potential site, while all other sites
contain carbohydrate. Amino acid sequence analysis of the HA1 of an avirulent
revertant of the virulent strain confirmed these findings.
Descriptors: genes, structural, genes viral, glycoproteins
genetics, hemagglutinins viral genetics, influenza A virus avian pathogenicity,
amino acid sequence, chick embryo, chromatography, high pressure liquid,
glycopeptides analysis, hemagglutinins viral isolation and purification, avian
genetics, oligosaccharides analysis, peptide fragments analysis, trypsin,
virulence.
Deshpande, K.L., C.W. Naeve, and R.G. Webster (1985).
The neuraminidases of the virulent and avirulent A/Chicken/Pennsylvania/83
(H5N2) influenza A viruses: sequence and antigenic analyses. Virology
147(1): 49-60. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: To define the sequence changes that occurred
in an avian influenza virus neuraminidase (NA) during the evolution of
virulence, we have studied the NA of the virulent and avirulent A/Chick/Penn/83
(H5N2) influenza viruses. A comparison of the deduced amino acid sequence from
these viruses shows that the virulent strain, which evolved from the avirulent
by the accumulation of point mutations (Bean et al., 1985), acquired four amino
acid changes in the NA: one in the transmembrane segment, one in the stalk, and
two in the head. A comparison of the deduced amino acid sequences with those of
the human N2 NAs indicates a 20-amino acid deletion in the stalk of the
Chick/Penn/83 NA. Antigenic analysis of the NAs from the avirulent and virulent
Chick/Penn/83 virus shows they are antigenically very closely related, but can
be distinguished with two monoclonal antibodies at a site which probably
involves at least one of the amino acid changes in the NA head. Antigenic
analysis also shows the Chick/Penn/83 NAs are closely related to the NAs of
other N2 avian influenza viruses isolated between 1965 and 1984, supporting
previous studies which indicate a relative antigenic stability of the NA among
avian N2 influenza viruses. The Chick/Penn/83 NAs are the first N2 NA genes of
an avian virus to be sequenced. These NAs are antigenically closely related to
the 1957 human N2 NAs, and show a high degree of amino acid sequence homology
with the prototype 1957 human N2 NA. These data give further support to the
view that the 1957 human H2N2 viruses were at least partially derived from an
avian source.
Descriptors: influenza A virus avian enzymology,
neuraminidase isolation and purification, amino acid sequence, antibodies
monoclonal diagnostic use, base sequence, chick embryo, chickens, epitopes
analysis, genes structural, genes viral, avian genetics, avian pathogenicity,
models molecular, neuraminidase immunology, protein conformation, species
specificity, virulence.
Desselberger, U., K. Nakajima, P. Alfino, F.S.
Pedersen, W.A. Haseltine, C. Hannoun, and P. Palese (1978). Biochemical
evidence that "new" influenza virus strains in nature may arise by
recombination (reassortment). Proceedings of the National Academy of
Sciences of the United States of America 75(7): 3341-5. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Oligonucleotide analysis of two avian
influenza A viruses (Hav6N2 and Hav6Nav4) isolated in nature showed identical
or almost identical patterns for the corresponding M and HA genes; 24 of 25 and
13 of 13 large oligonucleotides were indistinguishable by two-dimensional gel
analysis. On the other hand, remarkable differences in the oligonucleotide
patterns of the remaining genes were observed. Only 2 of 11 oligonucleotide
spots of the NS gene, 10 of 27 spots of the NA/NP genes, and 22 of 49 spots of
the P genes were indistinguishable between the two strains. On the basis of
this observation that at least two genes of these viruses are virtually
identical whereas others show easily detectable differences, we conclude that
the two avian strains are related to each other by a recombinational event. In
addition, it was found that animals in nature can be doubly infected with
influenza viruses. Both lines of evidence strongly suggest that recombination
is at least one mechanism by which "new" influenza virus strains
emerge in nature.
Descriptors: genes viral, influenza A virus avian
genetics, recombination, genetic, hemagglutinins viral analysis, avian
immunology, oligoribonucleotides analysis, RNA viral analysis.
Desselberger, U. and P. Palese (1978). Molecular
weights of RNA segments of influenza A and B viruses. Virology
88(2): 394-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus analysis, orthomyxoviridae
analysis, RNA viral analysis, genes viral, hemagglutinins viral genetics, avian
analysis, human analysis, genetics, molecular weight, neuraminidase genetics,
nucleic acid denaturation, oligonucleotides analysis, orthomyxoviridae
genetics.
Diringer, H., W.R. Willems, and R. Rott (1978). Metabolism
of myoinositol in avian and mammalian cells infected with naked and enveloped
DNA and RNA viruses. Journal of General Virology 40(2): 471-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The uptake of 3H-inositol into the pool of
free inositol and its incorporation into the lipid phosphatidylinositol have
been studied in various avian and mammalian cells infected by different
viruses. In all the virus-cell systems investigated, virus infection results in
a drastically reduced amount of free 3H-inositol about 3 to 5 h post-infection,
demonstrable in the infected cells as compared to the mock-infected controls.
In contrast, the incorporation of 3H-inositol into lipid can be enhanced,
reduced, or not influenced at all, depending on the virus-cell system under
observation.
Descriptors: DNA viruses growth and development, inositol
metabolism, RNA viruses growth and development, adenoviruses, human growth and
development, birds, cell line, herpesvirus 1, suid growth and development,
influenza A virus avian growth and development, mammals, Newcastle disease
virus growth and development, phosphatidylinositols biosynthesis, polioviruses
growth and development, tissue culture.
Donatelli, I., L. Campitelli, M.R. Castrucci, A.
Ruggieri, L. Sidoli, and J.S. Oxford (1991). Detection of two antigenic
subpopulations of A(H1N1) influenza viruses from pigs: antigenic drift or
interspecies transmission? Journal of Medical Virology 34(4):
248-57. ISSN: 0146-6615.
Abstract: Serological analysis of a group of 63
influenza H1N1 viruses isolated from pigs in Italy in the period 1976-1988
revealed the presence of two distinct antigenic subpopulations: some viruses
possessed a haemagglutinin indistinguishable from that of viruses typically
associated with pigs, i.e., A/New Jersey/8/76 (H1N1), whereas others showed a
close antigenic relatedness with the haemagglutinin of avian-like H1 viruses.
These findings represent further evidence that influenza A viruses from avian
species may be transmitted to mammals. The surface and internal proteins of
some of these viruses were also analyzed biochemically to evaluate the
molecular relatedness among viruses circulating in non-human hosts.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, porcine immunology, orthomyxoviridae infections
veterinary, swine microbiology, swine diseases microbiology, antibodies,
monoclonal immunology, antigenic variation, electrophoresis, polyacrylamide
gel, avian isolation and purification, porcine isolation and purification,
Italy, orthomyxoviridae infections microbiology, orthomyxoviridae infections
transmission, peptide mapping, species specificity.
Donis, R.O., W.J. Bean, Y. Kawaoka, and R.G. Webster
(1989). Distinct lineages of influenza virus H4 hemagglutinin genes in
different regions of the world. Virology 169(2): 408-17. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: To understand the determinants of influenza
virus evolution, phylogenetic relationships were determined for nine
hemagglutinin (HA) genes of the H4 subtype. These genes belong to a set of
viruses isolated from several avian and mammalian species from various
geographic locations around the world between 1956 and 1985. We found that the
HA gene of the H4 subtype is 1738 nucleotides in length and is predicted to
encode a polypeptide of 564 amino acids. The connecting peptide, which is
removed from the precursor polypeptide by peptidases to yield the mature HA1
and HA2 polypeptides, contains only one basic amino acid. This type of
connecting peptide is a feature of all avian avirulent HAs. On the basis of
pairwise nucleotide sequence homology comparisons the genes can be segregated
into two groups: influenza virus genes isolated in North America and those
isolated from other parts of the world. A high degree of homology exists
between pairs of genes from viruses of similar geographic origin. The
nucleotide sequences within a group differ by 1.5 to 10.6%; in contrast,
between groups the differences range from 15.8 to 19.4%. An evolutionary tree
for the nine sequences suggests that North American isolates have diverged
extensively from those circulating in other parts of the world. Geographic barriers
which determine flyway outlay may prevent the gene pools from extensive mixing.
The lack of correlation between date of isolation and evolutionary distance
suggests that different H4 HA genes cocirculate in a fashion similar to avian
H3 HA genes (H. Kida et al., 1987, Virology 159, 109-119) and influenza C genes
(D. Buonagurio et al., 1985, Virology 146, 221-232) implying the absence of
selective pressure by antibody that would give a significant advantage to
antigenic variants. In contrast to avian influenza virus genes, human influenza
virus genes evolve rapidly under the selective pressure of antibody.
Descriptors: hemagglutinins viral genetics, influenza A
virus genetics, amino acid sequence, base sequence, cloning, molecular,
geography, molecular sequence data, sequence homology, nucleic acid.
Dotti, C.G., J. Kartenbeck, and K. Simons (1993). Polarized
distribution of the viral glycoproteins of vesicular stomatitis, fowl plague
and Semliki Forest viruses in hippocampal neurons in culture: a light and
electron microscopy study. Brain Research 610(1): 141-7. ISSN: 0006-8993.
Abstract: We have shown previously using
immunofluorescence microscopy that upon infection of polarized hippocampal
cells in culture with vesicular stomatitis virus (VSV) and fowl plague virus
(FPV) the VSV glycoprotein is delivered to the plasma membrane of the dendrites
and of the cell body whereas the FPV hemagglutinin is transported to the axonal
surface (Cell, 62 (1990) 63-72). In this work electron microscopy of infected rat
hippocampal neurons showed that VSV progeny budded from the plasma membrane of
the dendrites and the cell body. The location of the budding virions
corresponded to the distribution of the VSV glycoprotein which was detected
over the somatodendritic plasma membrane by immunoelectron microscopy. In
contrast, no FPV formation was seen in the infected neurons although the FPV
hemagglutinin was localized to the axonal surface by immunoelectron microscopy.
In Semliki Forest virus (SFV) infected hippocampal cells we observed that the
viral glycoproteins were exclusively present in the dendrites and cell body but
not in axons.
Descriptors: cell polarity physiology, hippocampus
microbiology, membrane glycoproteins analysis, neurons microbiology, viral
envelope proteins analysis, cultured cells, hippocampus cytology, influenza A
virus avian isolation and purification, microscopy, microscopy, electron,
microscopy, immunoelectron, rats, rats, Sprague Dawley, Semliki Forest virus
isolation and purification, vesicular stomatitis Indiana virus isolation and
purification.
Dotti, C.G. and K. Simons (1990). Polarized
sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons
in culture. Cell 62(1): 63-72.
ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Abstract: Cultured hippocampal neurons were infected
with a temperature-sensitive mutant of vesicular stomatitis virus (VSV) and a
wild-type strain of the avian influenza fowl plague virus (FPV). The
intracellular distribution of viral glycoproteins was monitored by
immunofluorescence microscopy. In mature, fully polarized neurons the VSV
glycoprotein (a basolateral protein in epithelial MDCK cells) moved from the
Golgi complex to the dendritic domain, whereas the hemagglutinin protein of FPV
(an apically sorted protein in MDCK cells) was targeted preferentially, but not
exclusively, to the axon. The VSV glycoprotein appeared in clusters on the
dendritic surface, while the hemagglutinin was distributed uniformly along the
axonal membrane. Based on the finding that the same viral glycoproteins are
sorted in a polarized fashion in both neuronal and epithelial cells, we propose
that the molecular mechanisms of surface protein sorting share common features
in the two cell types.
Descriptors: axons microbiology, dendrites microbiology,
glycoproteins analysis, hippocampus microbiology, influenza A virus avian
genetics, neurons microbiology, vesicular stomatitis Indiana virus genetics,
viral proteins analysis, cultured cells, embryo, fluorescent antibody
technique, glycoproteins genetics, rats, viral proteins genetics.
Dragun, M., B. Rada, L. Novotny, and J. Beranek
(1990). Antiviral activities of pyrimidine nucleoside analogues: some
structure--activity relationships. Acta Virologica 34(4): 321-9
. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Seventeen nucleoside derivatives (derived
from arabinosylcytosine, resp. cytidine, 5-fluorouracil and uracil) were tested
by agar-diffusion plaque-inhibition test for their antiviral activity with
herpes simplex, vaccinia, fowl plague, Newcastle disease and western equine
encephalomyelitis viruses. The highest antiviral activity against DNA viruses
exhibited arabinosylcytosine, N4-acylarabinosylcytosines, arabinosylthiouracil,
cyclocytidine and its 5'-chloroderivative. RNA viruses were inhibited by
5-fluorouridine only, whereas other tested compounds were ineffective or
showing marginal activity only. By search for relationship between chemical
structure and antiviral activity a tendency was found of higher antiviral
activity at lower lipophilicity. This is probably due to better transport of
the studied compounds into cell. The chemical structure, however, is the main
reason of antiviral activity.
Descriptors: antiviral agents chemistry, pyrimidine
nucleosides pharmacology, encephalitis virus, western equine drug effects,
encephalitis virus, western equine growth and development, influenza A virus
avian drug effects, avian growth and development, Newcastle disease virus drug
effects, Newcastle disease virus growth and development, plaque assay,
pyrimidine nucleosides chemistry, simplexvirus drug effects, simplexvirus
growth and development, structure activity relationship, vaccinia virus drug
effects, vaccinia virus growth and development.
Drzeniek, R. and A. Gauhe (1970). Differences in
substrate specificity of myxovirus neuraminidases. Biochemical and
Biophysical Research Communications 38(4): 651-6. ISSN: 0006-291X.
NAL
Call Number: 442.8 B5236
Descriptors: influenza A virus avian enzymology,
neuraminidase, Newcastle disease virus enzymology, binding sites, chromosomes,
genetic code, glycosides, kinetics, lactose, neuraminic acids, species
specificity, time factors.
Duc Dodon, M., R. Cecchelli, R. Cacan, L. Gazzolo,
and A. Verbert (1984). Viral neuraminidase and cellular
ectosialyltransferase in human lymphoblastoid cells infected with influenza
virus. Biochimie 66(6):
493-6. ISSN: 0300-9084.
NAL
Call Number: 383 SO1
Abstract: In human lymphoblastoid cells, infected with
an influenza virus, Fowl Plague Virus (FPV), glycoproteins (such as secreted
IgM) are hyposialylated, through the action of viral neuraminidase. In this
study, the modulation of the cellular ectosialyltransferase activity during
viral infection was investigated. This activity was detectable in FPV-infected
cells, was shown to be 2.5-fold higher than that of uninfected cells, and to be
able to restore, at least partially, the level of sialylation of the cell
surface acceptors.
Descriptors: cell transformation, viral, influenza A virus
avian enzymology, neuraminidase metabolism, sialyltransferases metabolism,
transferases metabolism, cell line, cell membrane metabolism, clostridium
enzymology, glycoproteins metabolism, kinetics, lymphocytes, membrane proteins
metabolism.
Duc Dodon, M., L. Gazzolo, G.A. Quash, and T.F. Wild
(1982). Secretion of immunoglobulins by human lymphocytes after infection
with influenza virus. Journal of General Virology 63(2):
441-50. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The biosynthesis of IgM by the Epstein-Barr
virus-negative RAMOS lymphoblastoid cell line infected with an influenza A
virus, fowl plague virus Dobson strain (FPV-B), was investigated. The results
show that FPV infection of RAMOS cells slightly inhibited overall cellular
protein synthesis only at 24 h after infection, despite the synthesis of
FPV-specific proteins. However, even at this time, the synthesis and secretion
of IgM were not affected by virus infection. Secreted IgM contained a reduced
amount of sialic acid. The quantity of the asialylated IgM increased
proportionally to the amount of enzymically active neuraminidase, suggesting
that the asialylation of IgM is due to the action of virus neuraminidase. No
such asialylated IgM was observed in RAMOS cells infected with measles virus,
which does not possess neuraminidase. These results, together with a previous
observation of ours that asialylated immunoglobulins acquire an altered
antigenicity, suggest that the modulation of enzyme activities in B lymphocytes
in response to an exogenous aggression may lead to disturbances in the
structure and in the antigenic properties of immunoglobulins.
Descriptors: immunoglobulin m metabolism, influenza A
virus avian physiology, lymphocytes microbiology, cell line, immunoglobulin m
analysis, lymphocytes immunology, lymphoma, neuraminidase metabolism, proteins
analysis, sialic acids analysis, virus replication.
Duhaut, S.D. and J.W. McCauley (1996). Defective
RNAs inhibit the assembly of influenza virus genome segments in a
segment-specific manner. Virology 216(2): 326-337. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Four avian influenza viruses have been
generated, each containing a single extra defective RNA segment in addition to
the eight standard segments. Three of the extra RNAs were derived from segment
1 and the fourth from segment 2. Chick embryo fibroblast cells were infected
with each virus, and a wild-type virus. Virus RNA was quantified in extracts of
virus-infected cells and in virus released by 10 hr postinfection using reverse
transcription and by Northern blot analysis. In the case of two of the viruses
the presence of the defective RNA did not markedly affect the accumulation of
virus RNA within the infected cell, but significantly and selectively reduced
the amount of the "parent" segment in released virus. This effect was
reduced in a third virus. In a fourth virus, defective RNA was found to be
present at a low-input multiplicity and results were varied. Mixed infections of
one of the viruses with a closely related wild-type virus resulted in reduction
of the corresponding vRNA segment of the nondefective virus. We conclude that
assembly of influenza virus segments is not a purely random process.
Descriptors: chicks, avian influenza virus, RNA,
infection, pathogenesis, quantitative analysis, fibroblasts, acids, analytical
methods, birds, cells, chickens, disease transmission, domestic animals,
domesticated birds, Galliformes, influenza virus, livestock, nucleic acids, nucleic
compounds, organic acids, orthomyxoviridae, pathogenesis, poultry, useful
animals, viruses, young animals, reverse transcription, virus assembly,
transcription, mixed infections.
Durand, D.P. and R. Borland (1969). Effect of
input multiplicity on infection of cells with myxoviruses as studies by
hemadsorption. Proceedings of the Society for Experimental Biology and
Medicine, New York, NY 130(1): 44-7.
ISSN: 0037-9727.
NAL
Call Number: 442.9 So1
Descriptors: orthomyxoviridae pathogenicity, serologic
tests, hemadsorption inhibition tests, immune sera pharmacology, influenza A
virus avian pathogenicity, methods, Newcastle disease virus pathogenicity,
tissue culture.
Easterday, B., W.G. Laver, H.G. Pereira, and G.C.
Schild (1969). Antigenic composition of recombinant virus strains produced
from human and avian influenza A viruses. Journal of General Virology
5(1): 83-91. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: antigens analysis, neuraminidase analysis,
orthomyxoviridae analysis, orthomyxoviridae immunology, recombination, genetic,
electrophoresis, hemagglutination inhibition tests, hemagglutinins viral
analysis, hybridization, genetic, immunodiffusion, influenza A virus avian.
Eggert, H.J., B. Brux, G. Righter, and H. Sinnecker
(1984). Charakterisierung der RNS-polymerase-aktivitat hochgereinigter
praparationen des influenzavirus a/duck/alberta/48/76. [Characterization of RNA
polymerase activity of highly purified preparations of influenza virus
A/duck/Alberta/48/76]. Zentralblatt Fur Bakteriologie, Mikrobiologie,
Und Hygiene. Series A, Medical Microbiology, Infectious Diseases, Virology,
Parasitology 256(4): 534-40. ISSN:
0176-6724.
NAL
Call Number: 448.3 C33 (1)
Abstract: The influenza virus A/duck/Alberta/48/76 with
the antigen formula H7N3 (16) and Hav1 Nav2 (WHO nomenclature from 1971) (15),
respectively, as well as a nonpathogenic virus of the subtype Hav1 were
purified to a high degree by ultracentrifugation in continuous sucrose
gradients (15-40% w/w and 20-60% w/w, respectively). The activity of the RNA
polymerase of this virus preparation was determined by incorporating 3H-UMP in
acid insoluble material following preincubation of the virus with the nonionic
detergens Nonidet P-40 for 15 min at 32 degrees C. The influence of different
concentrations was investigated of dinucleotid, NaCl, MgCl2, Nonidet P-40 and
different incubation temperatures. Optimal incorporation rates were found at
following conditions: 0.2 mM dinucleotid ApG, 150 mM sodium chloride and 8 mM
magnesium chloride by concentration of ions, 0.25-0.5% detergens Nonidet P-40
as well as a temperature of incubation of 32 degrees C. The data for optimal
polymerase activity for the avian influenza virus A/duck/Alberta/48/76 are
generally not different from the conditions described for the Fowl-Plague-Virus
and for human strains.
Descriptors: DNA directed RNA polymerases metabolism,
influenza A virus avian enzymology, bacteriological techniques, chick embryo,
enzyme activation, temperature.
Ehrhardt, C., C. Kardinal, W.J. Wurzer, T. Wolff, C.
von Eichel Streiber, S. Pleschka, O. Planz, and S. Ludwig (2004). Rac1 and
PAK1 are upstream of IKK-epsilon and TBK-1 in the viral activation of
interferon regulatory factor-3. FEBS Letters 567(2-3): 230-8. ISSN: 0014-5793.
NAL
Call Number: QD415.F4
Abstract: The anti-viral type I interferon (IFN)
response is initiated by the immediate induction of IFN beta, which is mainly
controlled by the IFN-regulatory factor-3 (IRF-3). The signaling pathways
mediating viral IRF-3 activation are only poorly defined. We show that the Rho
GTPase Rac1 is activated upon virus infection and controls IRF-3
phosphorylation and activity. Inhibition of Rac1 leads to reduced IFN beta
promoter activity and to enhanced virus production. As a downstream mediator of
Rac signaling towards IRF-3, we have identified the kinase p21-activated kinase
(PAK1). Furthermore, both Rac1 and PAK1 regulate the recently described IRF-3
activators, I kappa B kinase- and TANK-binding kinase-1, establishing a first canonical
virus-induced IRF-3 activating pathway.
Descriptors: DNA binding proteins metabolism, protein
serine threonine kinases metabolism, transcription factors metabolism, RACL GTP
binding protein metabolism, cell line, DNA binding proteins chemistry, DNA
binding proteins genetics, dimerization, dogs, enzyme activation, influenza A
virus, avian pathogenicity, human pathogenicity, interferon beta genetics,
nuclear proteins metabolism, phosphorylation, promoter regions genetics,
protein serine threonine kinases antagonists and inhibitors, protein serine
threonine kinases genetics, RNA, double stranded immunology, double stranded
metabolism, signal transduction, trans activators metabolism, transcription
factors chemistry, transcription factors genetics, transcription, genetic,
virus replication.
Ellis, M.N., C.S. Eidson, J. Brown, and S.H. Kleven
(1983). Studies on interferon induction and interferon sensitivity of avian
reoviruses. Avian Diseases 27(4): 927-36. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Four strains of avian reovirus were
ineffective inducers of interferon (IFN) in chicken kidney (CK) cell cultures.
All strains were similar in single-cycle replication curves. At multiplicities
of infection between 0.20 and 10 plaque-forming units per cell, IFN was not
induced in CK cells. Reovirus did not produce an IFN blocker in CK cells.
Attenuated reovirus did induce IFN in aged chicken embryo fibroblast (CEF) cell
cultures. By priming cells with a low dose of IFN before infection with reovirus,
IFN formation by CEF could be enhanced. Ultraviolet-inactivated avian reovirus
was an effective inducer of IFN in both CK and CEK cell cultures. The
sensitivity of avian reoviruses (Fahey-Crawley, Reo-25, S-1133, Reo-V) to
chicken interferon (Ch-IFN) was studied by the plaque-reduction method. Avian
reoviruses were less sensitive to Ch-IFN than was vesicular stomatitis virus or
Semliki Forest virus and appeared to be as resistant to IFN as was Newcastle
disease virus.
Descriptors: interferons biosynthesis, reoviridae growth
and development, virus replication, cultured cells, chickens, cytopathogenic
effect, viral, drug resistance, microbial, influenza A virus avian growth and
development, interferons pharmacology, kidney, Newcastle disease virus growth
and development, Semliki Forest virus growth and development, ultraviolet rays,
vesicular stomatitis Indiana virus growth and development.
Emtage, J.S., G.H. Catlin, and N.H. Carey (1979). Polyadenylation
and reverse transcription of influenza viral RNA. Nucleic Acids Research
6(4): 1221-39. ISSN: 0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: The polyadenylation of Fowl Plague Viral RNA
and of Influenza A/Victoria Viral RNA using E. coli poly (A) polymerase and the
subsequent reverse transcription of the polyadenylated species is reported. We
have shown that all 8 genome fragments are adenylated and that an average of
25--30 adenylic acid residues per molecule is sufficient for maximal
transcription with reverse transcriptase. The cDNA product is 95% sensitive to
Sl-nuclease and hybridisation analysis against viral RNA reveals it to be a
faithful copy of the RNA. Amongst the transcription products are long, discrete
copies of genes 1--8, the lengths of which are comparable with those of the
vRNA determined by electrophoresis on formamide acrylamide gels. These
single-stranded cDNAs have been further transcribed to form double-stranded
products with hair-pin structures at one end. Analysis of this material on
native acrylamide gels revealed some DNA bands corresponding to the predicted
sizes for genes 4--8.
Descriptors: Escherichia coli enzymology,
nucleotidyltransferases metabolism, poly A biosynthesis, polynucleotide
adenylyltransferase metabolism, RNA viral metabolism, RNA directed DNA
polymerase metabolism, DNA, viral biosynthesis, influenza A virus avian,
kinetics, molecular weight, nucleic acid hybridization, orthomyxoviridae.
Emtage, J.S., W.C. Tacon, G.H. Catlin, B. Jenkins,
A.G. Porter, and N.H. Carey (1980). Influenza antigenic determinants are
expressed from haemagglutinin genes cloned in Escherichia coli. Nature
283(5743): 171-4. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Abstract: A gene sequence for the fowl plague virus
(FPV) haemagglutinin molecule has been inserted into a bacterial plasmid such
that its transcription is under the control of a promoter derived from the
tryptophan operon. Such plasmids direct the synthesis of a protein that reacts
specifically with antisera to FPV haemagglutinin. Evidence is also presented
that in some cases DNA inserted at the HindIII site of pBR322 is expressed.
Descriptors: antigens, viral genetics, DNA, recombinant, Escherichia
coli genetics, hemagglutinins viral genetics, influenza A virus avian
genetics, epitopes, genes, structural, influenza A virus avian immunology,
operon, plasmids, transcription, genetic, tryptophan genetics.
Emtage, J.S., W.C. Tacon, G.H. Catlin, B. Jenkins,
A.G. Porter, and N.H. Carey (1992). Influenza antigenic determinants are
expressed from haemagglutinin genes cloned in Escherichia coli. 1980.
Biotechnology 24: 491-4. ISSN:
0740-7378.
NAL
Call Number: QD320.B56
Descriptors: antigens, viral biosynthesis, hemagglutinins
viral biosynthesis, influenza A virus avian genetics, amino acid sequence,
antigens, viral genetics, antigens, viral immunology, base sequence, Escherichia
coli genetics, hemagglutinin glycoproteins, influenza virus, hemagglutinins
viral genetics, hemagglutinins viral immunology, history of medicine, 20th
century, influenza A virus avian immunology, molecular sequence data,
recombinant proteins biosynthesis, recombinant proteins genetics, recombinant
proteins immunology.
Erokhina, L.M., N.I. Arkhipov, N.A. Lagutkin, M.M.
Zubairov, N.I. Mitin, and VP Shishkov (ed.). (1980). Morfologicheskaya
otsenka xhimioterapevticheskogo deistviya Midantana i preparata C-4.
[Morphological assessment of the chemotherapeutic activity of the antiviral
agents Midantan and C-4 (amantadine-1-boradamantine) in avian influenza].
In: Patomorfologiya, patogenez i diagnostika boleznei s. kh. zhivotnykh, Nauchnye
Trudy VASKNIL, p. 168-169.
NAL
Call Number:
SF769.P36
Descriptors: avian influenza virus,
chemotherapy, antiviral agents.
Ershov, F.I. and A.S. Agabalian (1970). Prostoi
bystryi metod titrovaniia interferona po podavleniiu sinteza gemaggliutininov.
[Simple and rapid method of interferon titration by suppression of
hemagglutinin synthesis]. Laboratornoe Delo 4: 228-31. ISSN: 0023-6748.
Descriptors: antibody formation, interferons analysis,
arboviruses, chick embryo, encephalitis viruses, encephalomyelitis, equine,
hemagglutination inhibition tests, hemagglutinins viral biosynthesis, hemolytic
plaque technique, influenza A virus avian, tissue culture.
Esievo, K.A. (1983). Trypanosoma vivax, stock
V953: inhibitory effect of type A influenza virus anti-HAV8 serum on in vitro
neuraminidase (sialidase) activity. Journal of Parasitology 69(3):
491-5. ISSN: 0022-3395.
NAL
Call Number: 448.8 J824
Abstract: Trypanosoma vivax stock V953 lysates
were observed to produce neuraminidase (sialidase EC 3.2.1.18) in vitro, which
cleaved neuraminic (sialic) acid from the substrate fetuin. The neuraminidase
activity was proportional to the number of trypanosomes in the lysates, with 0.44,
0.88, and 1.75 X 10(6) trypanosomes producing 1.4 +/- 0.06, 3.1 +/- 0.1, and
6.7 +/- 0.1 micrograms of sialic acid liberated, respectively. Equal numbers of
unlysed and lysed trypanosomes produced approximately the same amount of the
enzyme. Trypanosome eluates stored at room temperature appeared to have lost
neuraminidase activities within 4 days. An inhibition test for identifying the
neuraminidase antigen on influenza viruses was performed in vitro on the T.
vivax lysates. The inhibition test, using Type A influenza virus anti-HAV8
serum, showed a highly significant (P less than 0.0001) reduction in
neuraminidase activities. The effect of equal amounts of influenza antiserum on
serially diluted trypanosome lysates showed that 1 ml of influenza anti-HAV8
serum would inhibit a mean of 6.74 +/- 0.18 micrograms of T. vivax stock V953
neuraminidase activity.
Descriptors: antibodies, viral immunology, influenza A
virus avian immunology, neuraminidase antagonists and inhibitors, Trypanosoma
enzymology, immune sera, neuraminidase immunology, temperature.
Ewasyshyn, M.E. and L.R. Sabina (1983). Effects of
influenza virus replication on neutral proteolytic activities in embryonated
egg fluids. Acta Virologica 27(3): 193-9. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The levels of neutral protease activity
associated with allantoic and amniotic fluids of embryonated eggs during the
replication of influenza strains A/PR/8/34 (H1N1) and A/turkey/Ontario/7732/66
(H5N9) were investigated. A sensitive fluorometric technique proved useful for
characterization and monitoring changes of protease activities in egg fluids.
The predominant type of protease in allantoic and amniotic fluids had
trypsin-like specificities. Variation in protease levels of both fluids
occurred throughout the course of virus replication irrespective of the virus
strain or the route of inoculation used. Concomitant with the production of
high levels of infectious virus there was a marked decrease in neutral protease
activity in the fluid from the cavity initially infected. Translocation of
virus also occurred especially with amniotically infected eggs, as evidenced by
high infectious virus titers and decreased protease activities in allantoic
fluids.
Descriptors: allantois enzymology, amniotic fluid
enzymology, fetal membranes enzymology, influenza A virus physiology, peptide
hydrolases metabolism, virus replication, allantois microbiology, amniotic
fluid microbiology, chick embryo, influenza A virus avian physiology, protease
inhibitors pharmacology, turkeys.
Fang, R., W. Min Jou, D. Huylebroeck, R. Devos, and
W. Fiers (1981). Complete structure of A/duck/Ukraine/63 influenza
hemagglutinin gene: animal virus as progenitor of human H3 Hong Kong 1968
influenza hemagglutinin. Cell 25(2): 315-23. ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian genetics, influenza A virus human genetics, amino acid
sequence, base sequence, cloning, molecular, ducks microbiology, epitopes,
hemagglutinins viral immunology, influenza A virus avian immunology, influenza
A virus human immunology, mutation.
Fatunmbi, O.O., J.A. Newman, D.A. Halvorson, and V.
Sivanandan (1993). Effect of temperature on the stability of avian influenza
virus antigens under different storage conditions. Avian Diseases
37(3): 639-646. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The combined effect of time and temperature
on the stability of two avian influenza virus (AIV) isolates concentrated with
polyethylene glycol (PEG), stored at different temperatures, and used in the
preparation of avian influenza vaccine was evaluated in turkeys at 24 hr and at
12, 24, 30, 36, and 42 months of storage. The differences detected between
antibodies raised in turkeys by vaccines made from isolates under different
storage conditions, times, and temperatures were not significant (P > 0.05),
especially with vaccines prepared from one isolate. Virus recovery rates
following challenge studies of vaccinated birds were similar. However, birds
that were vaccinated twice had lower rates of virus recovery from the trachea,
lungs, pancreas, and fecal samples following challenge infection. The results
suggest that if stable isolates of AIV can be identified, such isolates can be
rapidly concentrated with PEG and stored at -20 C or -196 C for at least 42
months without any loss of potency in the vaccine prepared from these isolates.
This would reduce the costs associated with vaccine storage and subsequent
expiration dates.
Descriptors: turkeys, avian influenza virus, antigens,
vaccines, freezing, storage, temperature, time, alcohols, polyethylene,
vaccination, birds, disease control, Galliformes, immunization, immunological
factors, immunology, immunostimulation, immunotherapy, influenza virus,
polymers, processing, therapy, viruses, viral antigens, potency, polyethylene
glycol.
Fedorova, G.I., R.I.A. Podcherniaeva, A.M.
Amchenkova, N.I. Nikitina, and V.K. Blinova (1974). Izuchenie
vzaimodeistviia virusov pozvonochnykh i virusov iadernogo poliedroza nasekomykh
s peresevaemymi diploidnymi embrional'nymi kletkami drozofily [Interaction of
vertebrate viruses and insect nuclear polyhedrosis viruses with transplantable
diploid embryonal Drosophila cells]. TSitologiia i Genetika
8(5): 396-9. ISSN: 0564-3783.
NAL
Call Number: QH573.T75
Abstract: When the Drosophila cells were
infected with the mixo- and arboviruses, in case of influenza A/WSN virus a
rise in the titre and slight cytopathogenic effect with the subsequent decrease
in the titre was observed. Since the decrease in the virus titer was not
observed when actinomycin D was added, it was supposed that interferonlike
inhibitor may be produced by the infected cells. Vacuolization and increase in
the size of the infected cells were caused by all the nuclear polyhedrosis
viruses tested. The number of the infected cells depended on the virus type and
multiplicity of the infection.
Descriptors: insect viruses, viruses, arboviruses,
cultured cells, cytopathogenic effect, viral, encephalitis virus, western
equine, influenza A virus avian, Newcastle disease virus, orthomyxoviridae.
Feldmann, A., M.K. Schafer, W. Garten, and H.D. Klenk
(2000). Targeted infection of endothelial cells by avian influenza virus
A/FPV/Rostock/34 (H7N1) in chicken embryos. Journal of Virology
74(17): 8018-27. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The tissue tropism and spread of infection of
the highly pathogenic avian influenza virus A/FPV/Rostock/34 (H7N1) (FPV) were
analyzed in 11-day-old chicken embryos. As shown by in situ hybridization, the
virus caused generalized infection that was strictly confined to endothelial
cells in all organs. Studies with reassortants of FPV and the apathogenic avian
strain A/chick/Germany/N/49 (H10N7) revealed that endotheliotropism was linked
to FPV hemagglutinin (HA). To further analyze the factors determining
endotheliotropism, the HA-activating protease furin was cloned from chicken
tissue. Ubiquitous expression of furin and other proprotein convertases in the
chick embryo indicated that proteolytic activation of HA was not responsible
for restriction of infection to the endothelium. To determine the expression of
virus receptors in embryonic tissues, histochemical analysis of alpha2,3- and
alpha2,6-linked neuraminic acid was carried out by lectin-binding assays. These
receptors were found on endothelial cells and on several epithelial cells, but
not on tissues surrounding endothelia. Finally, we analyzed the polarity of
virus maturation in endothelial cells. Studies on cultured human endothelial
cells employing confocal laser scanning microscopy revealed that HA is
specifically targeted to the apical surface of these cells, and electron
microscopy of embryonic tissues showed that virus maturation occurs also at the
luminar side. Taken together, these observations indicate that
endotheliotropism of FPV in the chicken embryo is determined, on one hand, by
the high cleavability of HA, which mediates virus entry into the vascular system,
and, on the other hand, by restricted receptor expression and polar budding,
which prevent spread of infection into tissues surrounding endothelia.
Descriptors: endothelium virology, influenza A virus avian
pathogenicity, chick embryo, endothelium metabolism, endothelium pathology,
Furin, hemagglutinin glycoproteins, influenza virus metabolism, in situ
hybridization, influenza A virus avian ultrastructure, microscopy, confocal,
neuraminic acids analysis, neuraminidase metabolism, organ specificity, proprotein
convertase 5, receptors, virus analysis, serine endopeptidases metabolism,
subtilisins metabolism.
Feldmann, H., E. Kretzschmar, B. Klingeborn, R. Rott,
H.D. Klenk, and W. Garten (1988). The structure of serotype H10
hemagglutinin of influenza A virus: comparison of an apathogenic avian and a
mammalian strain pathogenic for mink. Virology 165(2): 428-37. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The primary structure of the hemagglutinin of
the apathogenic avian influenza virus A/chick/Germany/N/49 (H10N7) and of the
serologically related strain A/mink/Sweden/84 (H10N4) pathogenic for mink has
been elucidated by nucleotide sequence analysis, and the carbohydrates attached
to the polypeptide have been determined. The H10 hemagglutinin has 65, 52, 46,
45, and 44% amino acid sequence homology with serotypes H7, H3, H1, H2, and H5,
respectively. H10 and H7 hemagglutinins are also most closely related in their
glycosylation patterns. There is a high sequence homology between both H10 strains
supporting the concept that the mink virus has obtained its hemagglutinin from
an avian strain. The sequence homology includes the cleavage site which
consists of a single arginine as is the case with most other hemagglutinins
exhibiting low susceptibility to proteolytic activation. The similarity in
hemagglutinin structure between both H10 strains is discussed in light of the
distinct differences in the pathogenicity of both viruses.
Descriptors: hemagglutinins viral genetics, influenza A
virus genetics, amino acid sequence, base sequence, carbohydrates analysis,
chickens microbiology, glycosylation, hemagglutinins viral analysis, influenza
A virus immunology, mink microbiology, molecular sequence data, sequence
homology, nucleic acid.
Finskaia, N.N., I.U.A. Smirnov, I.A. Rudneva, and
N.V. Kaverin (1988). Svoistva reassortantov virusov grippa cheloveka i
ptits. Reproduktsiia v kletkakh MDCK pri suboptimal'noi temperature.
[Properties of reassortants of human and avian influenza viruses. Reproduction
in MDCK cells at suboptimum temperatures]. Molekuliarnaia Genetika,
Mikrobiologiia i Virusologiia (4): 26-9.
ISSN: 0208-0613.
NAL
Call Number: QH506.M65F2
Abstract: A series of reassortants has been constructed
by crossing of UV-inactivated avian influenza virus of H3N8 subtype and live
human influenza virus of H1N1 subtype, adapted to growth in continuous canine
kidney cell line (MDCK). The analysis of RNA duplexes has shown that the
reassortants contain HA gene of avian influenza virus whereas the other genes
belong to human parent virus. The reassortants were efficiently reproduced in
MDCK cells at low temperature (limiting for the avian parent virus). The data
suggest that the avian virus HA gene does not hamper the reproduction of reassortant
viruses in mammalian cells under the conditions unfavorable for the
multiplication of avian influenza subtype H3N8 viruses.
Descriptors: genes viral, influenza A virus avian
genetics, human genetics, virus replication, cultured cells, dogs, hemagglutinins
viral genetics, hemagglutinins viral immunology, avian immunology, avian
physiology, human immunology, human physiology, kidney, nucleic acid
hybridization, phenotype, RNA viral genetics, temperature.
Fischer, A.A., K. Muller, and C. Scholtissek (1990). Specific
inhibition of the synthesis of influenza virus late proteins and stimulation of
early, M2, and NS2 protein synthesis by 3-deazaadenosine. Virology
177(2): 523-31. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: 3-Deazaaristeromycin and 3-deazaadenosine
(3DA-Ado) both interfere with the methylation of RNA, but only 3DA-Ado is
metabolized to the corresponding homocysteine derivative. In contrast to
3-deazaaristeromycin, 3DA-Ado inhibits the synthesis of late influenza A virus
proteins in chicken embryo cells (CEC), while it causes an overproduction of
early proteins and of the nonstructural proteins NS2 and M2. Only the former
effect of 3DA-Ado can be reversed by concomitant addition of adenosine, but not
by guanosine. 3DA-Ado acts only early in the infectious cycle and, after
removal of the drug, its effect on the yield of infectious virus is reversible.
It can be significantly enhanced by homocysteine thiolactone. Except for the M
gene, synthesis of viral mRNA is not significantly affected by 3DA-Ado. We
conclude that 3DA-Ado acts via its homocysteine derivative by interfering with
a specific post-transcriptional modification of viral mRNA and on splicing of
specifically the M mRNA. In L-cells influenza viral protein synthesis is comparable
to that in CEC in the presence of 3DA-Ado in that there is only little HA and
M1 synthesized, and a severe overproduction of NS2 is observed. Under the
experimental conditions 3DA-Ado has no inhibiting effect on the replication of
other RNA viruses like Newcastle disease virus, Semliki Forest virus, or West
Nile virus whose RNA is not methylated, since they do not have a nuclear phase
during replication.
Descriptors: anti bacterial agents pharmacology, influenza
A virus genetics, tubercidin pharmacology, viral proteins biosynthesis,
adenosine analogs and derivatives, adenosine pharmacology, aminoglycosides,
capsid biosynthesis, cell line, cultured cells, chick embryo, enzyme inhibitors
pharmacology, influenza A virus avian drug effects, avian physiology, influenza
A virus drug effects, influenza A virus metabolism, isomerism, kinetics, mice,
RNA, messenger biosynthesis, RNA viral biosynthesis, viral core proteins
biosynthesis, viral nonstructural proteins, viral proteins isolation and
purification, virus replication.
Fiszon, B. and C. Hannoun (1990). Comparison of
neuraminidases of the same subtype but from different species using a new
method of titration. Journal of Virological Methods 27(1):
79-90. ISSN: 0166-0934.
NAL
Call Number: QR355.J6
Abstract: Neuraminidase is one of the two surface
glycoproteins of influenza virions. In order to compare neuraminidases of the
same subtype but isolated from different species (man, birds, pig), a new and
simple method was adapted and optimized using peanut hemagglutinin. Results
were very similar to those obtained with the classical method recommended by
the WHO, using fetuin as a substrate. The technique was used to examine the
relationship between animal and human neuraminidases belonging to serotypes N1
and N2. The results confirm the possible role of ducks as a reservoir for
influenza viruses and the eventuality of interspecific exchanges.
Descriptors: neuraminidase analysis, orthomyxoviridae
enzymology, antigenic variation immunology, ducks, influenza A virus avian
classification, avian enzymology, human classification, human enzymology,
porcine classification, porcine enzymology, lectins, neuraminidase immunology,
orthomyxoviridae classification, peanut agglutinin, species specificity, swine.
Fiszon, B., C. Hannoun, A. Garcia Sastre, E. Villar,
and J.A. Cabezas (1989). Comparison of biological and physical properties of
human and animal A(H1N1) influenza viruses. Research in Virology
140(5): 395-404. ISSN: 0923-2516.
NAL
Call Number: QR355.A44
Abstract: The study of biological properties of
influenza virus strains belonging to the same subtype A(H1N1) and closely
antigenically related, but isolated from different animal species (man, pig and
duck), demonstrated that avian strains were more resistant than those isolated
from mammals to high temperature and low pH, as shown by titration of residual
infectivity in cell cultures (MDCK) and by sialidase assay. The difference in
behaviour could be correlated to biological adaptation of the virus to its host.
Avian body temperature is 40 degrees C and influenza virus, in ducks, is
enterotropic and therefore capable of passing through the low pH values in the
upper digestive tract of the animal. These results do not contradict the
hypothesis of a possible filiation between avian and mammalian
orthomyxoviruses.
Descriptors: influenza A virus physiology, body
temperature, cell line, ducks, hemagglutination tests, hydrogen-ion
concentration, influenza A virus avian enzymology, avian growth and
development, avian physiology, human enzymology, human growth and development,
human physiology, porcine enzymology, porcine growth and development, porcine
physiology, influenza A virus enzymology, influenza A virus growth and
development, neuraminidase analysis, plaque assay, swine, temperature, virus
replication.
Flehmig, B., A. Vallbracht, and H.J. Gerth (1976). Influenza
virus: association of mouse-lung virulence with plaque formation in mouse
kidney cells. InterVirology 7(4-5): 201-10. ISSN: 0300-5526.
NAL
Call Number: QR355.I5
Abstract: In genetic recombination experiments with the
mouse-lung-adapted human influenza A/Engl/1/61 (H2N2) and an avian influenza
strain A/Rostock/34 (FPV) (Hav1N1) which is avirulent for the mouse lung,
recombinants in which hemagglutinin and neuraminidase were either segregated
(Hav1N2; H2N1) or not segregated (Hav1N1) were selected. The recombinants were
studied for mouse-lung virulence and their ability to propagate in mouse kidney
cells, mouse embryo fibroblasts, chick embryo kidney cells and chick embryo
fibroblasts. An association between plaque formation in mouse kidney cells and
mouse-lung virulence was found.
Descriptors: influenza A virus human pathogenicity,
antigens, viral analysis, hemagglutinins viral analysis, human growth and
development, human immunology, lung microbiology, mice, neuraminidase
immunology, plaque assay, recombination, genetic, tissue culture, virulence,
virus replication.
Follett, E.A., C.R. Pringle, W.H. Wunner, and J.J.
Skehel (1974). Virus replication in enucleate cells: vesicular stomatitis
virus and influenza virus. Journal of Virology 13(2): 394-9. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Descriptors: cultured cells microbiology, orthomyxoviridae
growth and development, vesicular stomatitis Indiana virus growth and
development, virus replication, autoradiography, carbon radioisotopes, cell
line, cell nucleus microbiology, cytochalasin B pharmacology, electrophoresis,
polyacrylamide gel, haplorhini, influenza A virus avian growth and development,
avian metabolism, kidney, orthomyxoviridae metabolism, peptide synthesis,
plaque assay, RNA viral biosynthesis, sulfur radioisotopes, tritium, vesicular
stomatitis Indiana virus metabolism, viral proteins biosynthesis.
Fontaine, M. and M. Aymard Henry (1975). Contribution
a l'etude antigenique des virus influenza des animaux. I. Neuraminidase des
virus influenza equins. [Contribution to the antigenic study of influenza
viruses in animals. I. Neuraminidase of the equine influenza viruses (author's
transl)]. Annales De Recherches Veterinaires Annals of Veterinary
Research 6(4): 397-410. ISSN: 0003-4193.
NAL
Call Number: SF602.A5
Abstract: From the Revised Nomenclature of WHO, the
fowl influenza virus A/Duck/Ukraine/63 (Hav7 Neq2) has the same neuraminidase
as the equine virus A/equi 2/Miami/63 (Heq2 Neq2); the A/Chicken Germany
"N"/49 virus has the same neuraminidase as the equine virus A/equi 1/Prague/56.
A comparative study of the antigenic specificities confirms that the Neq2
neuraminidases are closely connected, whatever their animal origin, and that
the fowl strain Hav7 Neq2 can be used for the titration of anti Neq2 antibodies
in the serums of animals immunized with the equine virus Heq2 Neq2. The Neqi
neuraminidases of various animal origins are connected, but the neuraminidase
of the fowl strain Hav2 Neqi is slightly inhibited by the anti Neq1 antibodies
of animals immunized with the Heq1 Neq1 virus: to titrate the anti Neq1
antibodies of equine origin, the H72 Neq1 recombinant should therefore be used.
The antigenic characterization of the different equine influenza strains
isolated since 1967 by the study of their neuraminidase has been completed: The
various neuraminidases, like the hemagglutinins of the various strains
belonging to the sub-type A equi2 are closely connected; a minor antigenic
variation, concerning the two surface antigens, seems to exist between the
strain A equi 1/Prague/56 and the strain of the same subtype isolated in 1973.
Descriptors: antigens, viral, neuraminidase immunology,
orthomyxoviridae immunology, cross reactions, epitopes, hemagglutination
inhibition tests, horse diseases immunology, horses, influenza immunology,
influenza veterinary, influenza A virus avian immunology.
Freidlin, P.J., R. Bock, A. Inbar, and Y. Samberg
(1985). Immunoelectrophoresis of avian viral proteins in a
phosphate-buffered system. Avian Diseases 29(3): 613-6. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Avian influenza and hemorrhagic enteritis
viral preparations were immunoelectrophoresed in a phosphate-buffered system.
Excellent separation and resolution of viral proteins were achieved. Reasons
are given why this method might be preferred over the conventional method
employing a veronal (barbital)-buffered system.
Descriptors: antigens, viral analysis, coronaviridae
analysis, coronavirus, turkey analysis, influenza A virus avian analysis, viral
proteins analysis, coronavirus, turkey immunology, immunoelectrophoresis
methods, viral proteins immunology.
Friebolin, H., W. Baumann, G. Keilich, D. Ziegler, R.
Brossmer, and H. von Nicolai (1981). 1H-NMR-Spektroskopie--Eine
aussagekraftige Methode zur Bestimmung der Substratspezifitat von Sialidasen.
[1H-NMR spectroscopy--a potent method for the determination of substrate
specificity of sialidases (author's transl)]. Hoppe Seyler's Zeitschrift
Fur Physiologische Chemie 362(11): 1455-63.
ISSN: 0018-4888.
NAL
Call Number: 384 Z38
Abstract: We describe here the application of 1H-NMR
spectroscopy to determine the substrate specificity of sialidases using a 1:1
mixture of NeuAc alpha 2-3Gal beta 1-4Glc and NeuAc alpha 2-6Gal beta 1-4Glc,
one viral and five bacterial sialidases. This method utilizes the separate
signals in NMR spectra, characteristic for the different alpha ketosidically
linked NeuAc residues and also for bound and free NeuAc. The signals generally
most suitable for these purposes are those of H3a, H3e and NCOCH3. By
observation and integration of these signals we can follow--qualitatively and
quantitatively--which and how many NeuAc residues of the substrates are
hydrolized. In contrast to the generally used colorimetric tests it is now
possible to investigate with this method substrates containing two or more
NeuAc residues and to determine the corresponding rate constants for hydrolysis
of the differently bound NeuAc molecules. The six sialidases used show large
differences in their specificity as compared with our "model
substrate": The sialidase from fowl plague virus hydrolizes NeuAc alpha
2-3Gal beta 1-4Glc nearly 18 times and the enzyme from Clostridium
perfringens four times, from Vibrio cholerae two times faster than
NeuAc alpha 2-6Gal beta 1-4Glc. On the contrary, the sialidase from Arthrobacter
ureafaciens hydrolizes the alpha 2-6 linkage six times faster than the
alpha 2-3 linkage. The sialidases from Bifidobacterium show no obvious
differences in their specificities relative to the linkage.
Descriptors: neuraminidase metabolism, actinomycetaceae
enzymology, arthrobacter enzymology, Clostridium perfringens enzymology,
influenza A virus avian enzymology, kinetics, magnetic resonance spectroscopy
methods, substrate specificity, Vibrio cholerae enzymology.
Frischholz, K.W. and C. Scholtissek (1984). Influence of infection with an influenza A
virus (fowl plague) on Ca++-uptake and lipid metabolism of chick embryo cells
in culture. Archives of Virology 80(2-3): 163-70. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: After infection of primary chick embryo cells
with an influenza A virus (FPV) the synthesis of polar lipids was specifically
inhibited, while mono-, di- and triacylglycerols and fatty acids accumulated.
Influx of Ca++ accelerated and Ca++ accumulated in the infected cells. Since
enzymes like choline phosphotransferase are sensitive to high concentrations of
Ca++, specific inhibition of the synthesis of polar lipids is presumably due to
an increased influx of Ca++ by the infection.
Descriptors: calcium metabolism, fowl plague metabolism,
lipids metabolism, biological transport, cultured cells, chick embryo,
influenza A virus avian.
Fukushi, H., R. Yanagawa, and H. Kida (1982). Host
species-related antigenic groups of avian influenza viruses possessing H4
hemagglutinin revealed by monoclonal antibodies. Archives of Virology
72(3): 217-21. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, antibodies, monoclonal immunology, antibodies, viral
immunology, birds microbiology, cross reactions, ducks microbiology, epitopes,
hemagglutination inhibition tests, hemagglutinins viral classification,
influenza A virus avian classification.
Fuller, S.D., C.H. von Bonsdorff, and K. Simons
(1985). Cell surface influenza haemagglutinin can mediate infection by other
animal viruses. EMBO Journal 4(10): 2475-85. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: We have used filter-grown Madin-Darby canine
kidney (MDCK) cells to explore the mechanism by which influenza virus
facilitates secondary virus infection. Vesicular stomatitis virus (VSV) and
Semliki Forest virus (SFV) infect only through the basolateral surface of these
polarized epithelial cells and not through the apical surface. Prior infection
with influenza virus rendered the cell susceptible to infection by VSV or SFV
through either surface. The presence of both a permissive and a restrictive
surface for virus entry in the same cell allowed us to determine how the
influenza infection enhanced the subsequent infection of a second virus.
Biochemical and morphological evidence showed that influenza haemagglutinin on
the apical surface serves as a receptor for the superinfecting virus by binding
to its sialic acid-bearing envelope proteins. Influenza virus also facilitates
secondary virus infection in non-epithelial cells; baby hamster kidney cells
(BHK-21), which are normally resistant to infection by the coronavirus (mouse
hepatitis virus MHV-A59), could be infected via the haemagglutinin-sialic acid
interaction. Facilitation of secondary virus infection requires only the sialic
acid-binding properties of the haemagglutinin since the uncleaved
haemagglutinin could also mediate virus entry.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian metabolism, receptors, virus metabolism, vesicular stomatitis
Indiana virus metabolism, cell compartmentation, cultured cells, dogs,
endocytosis, hamsters, kidney microbiology, murine hepatitis virus metabolism,
Semliki Forest virus metabolism, sialic acids physiology, viral proteins
biosynthesis, virus replication.
Fynan, E.F., R.G. Webster, D.H. Fuller, J.R. Haynes,
J.C. Santoro, and H.L. Robinson (1993). DNA vaccines: protective
immunizations by parenteral, mucosal, and gene-gun inoculations. Proceedings
of the National Academy of Sciences of the United States of America 90(24):
11478-82. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Plasmid DNAs expressing influenza virus
hemagglutinin glycoproteins have been tested for their ability to raise
protective immunity against lethal influenza challenges of the same subtype. In
trials using two inoculations of from 50 to 300 micrograms of purified DNA in
saline, 67-95% of test mice and 25-63% of test chickens have been protected
against a lethal influenza challenge. Parenteral routes of inoculation that
achieved good protection included intramuscular and intravenous injections.
Successful mucosal routes of vaccination included DNA drops administered to the
nares or trachea. By far the most efficient DNA immunizations were achieved by
using a gene gun to deliver DNA-coated gold beads to the epidermis. In mice,
95% protection was achieved by two immunizations with beads loaded with as
little as 0.4 micrograms of DNA. The breadth of routes supporting successful
DNA immunizations, coupled with the very small amounts of DNA required for
gene-gun immunizations, highlight the potential of this remarkably simple
technique for the development of subunit vaccines.
Descriptors: DNA, viral administration and dosage, fowl
plague prevention and control, hemagglutinins viral genetics, influenza
prevention and control, influenza A virus avian immunology, human immunology,
cell line, chickens, DNA, viral immunology, fowl plague immunology, genes viral, hemagglutinin glycoproteins,
influenza virus, hemagglutinins viral biosynthesis, influenza immunology, avian
genetics, human genetics, injections, injections, intramuscular, injections,
intravenous, mice, mice inbred BALB c, mucous membrane, restriction mapping,
transfection, viral envelope proteins biosynthesis, viral envelope proteins
genetics.
Galegov, G.A. and A.A. Iatsyna (1980). Ingibiruiushchee
deistvie solianokislogo rimantadina (alpha-metil-1-adamantanmetilamina) na
sintez belkov virusa grippa. [Inhibitory effect of rimantidine hydrochloride
(alpha-methyl-1-adamantan methylamine) on the synthesis of influenza virus
proteins]. Doklady Akademii Nauk SSSR 251(2): 481-82. ISSN: 0002-3264.
NAL
Call Number: 511 P444A
Descriptors: adamantane analogs and derivatives, influenza
A virus avian drug effects, rimantadine pharmacology, viral proteins
biosynthesis, chick embryo, fibroblasts microbiology, avian metabolism, RNA,
messenger metabolism.
Galegov, G.A., A.A. Iatsyna, G.L. Linitskaia, and
N.L. Pushkarskaia (1976). Ingibiruiushchee deistvie solianokislogo
al'fa-metil-1-adamantanmetilamina (rimantadina) na induktsiiu RNK-zavisimoi RNK-polimerazy
v kul'ture kletok, infitsirovannykh virusom grilla [Inhibitory effect of
alpha-methyl-1-adamantane methylamine hydrochloride (rimantadine) on
RNA-dependent RNA polymerase induction in culture of cells, infected with
influenza virus]. Biokhimiia Moscow, Russia 41(12): 2237-9. ISSN: 0320-9725.
NAL
Call Number: 385 B523
Abstract: An anti-influenza preparation, rimantadine
(alpha-methyl-1-adamantane methylamine hydrochloride) at concentrations of
10--25 mkg/ml depresses the RNA-dependent RNA polymerase induction in a culture
of cells infected with influenza virus (fowl plague virus). The inhibitory
effect is also observed 2 hours following cell infection. In vitro studies have
demonstrated that rimantadine has no effect on the activity of virus-induced
RNA-dependent RNA polymerase, as well as on that of RNA-dependent RNA
polymerase associated with virus particles.
Descriptors: adamantane analogs and derivatives, antiviral
agents pharmacology, bridged compounds analogs and derivatives, influenza A
virus avian, RNA nucleotidyltransferases biosynthesis, RNA replicase
biosynthesis, adamantane pharmacology, cultured cells, enzyme induction drug
effects, virus cultivation.
Galegov, G.A., N.A. Pushkarskaia, K.M. Ermolaev, and
I.A. Red'kin (1970). Ingibiruiushchee deistvie
2-N-atsetilaminotsikogeksen-2-ona i ego proizvodnykh na reproduktsiiu virusa
grippa A v kul'ture tkani. [The inhibiting effect of
2-N-acetylaminocyclohexene-2-one and its derivatives on influenza A virus
reproduction in tissue culture]. Voprosy Virusologii 15(6): 689-93.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antiviral agents pharmacology, cyclohexanes
pharmacology, influenza microbiology, influenza A virus avian drug effects,
virus replication drug effects, antiviral agents adverse effects, cell line,
chick embryo, fibroblasts enzymology, hemagglutinins viral biosynthesis, avian
isolation and purification, neuraminidase metabolism, tissue culture.
Gambaryan, A., R. Webster, and M. Matrosovich (2002).
Differences between influenza virus receptors on target cells of duck and
chicken. Archives of Virology 147(6): 1197-208. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: H5, H7, and H9 subtype influenza viruses in
land-based poultry often differ from viruses of wild aquatic birds by deletions
in the stalk of the neuraminidase, by the presence of additional carbohydrates
on the hemagglutinin, and by occasional changes in the receptor specificity. To
test whether these differences could reflect distinctions between the virus
receptors in different avian species, we compared the binding of duck, chicken
and human influenza viruses to cell membranes and gangliosides from epithelial
tissues of duck, chicken and African green monkey. Human viruses bound to cell
membranes of monkey and chicken but not to those of duck, suggesting that
chicken cells unlike duck cells contain Sia(alpha2-6)Gal-terminated receptors
recognized by human viruses. Duck virus bound to gangliosides with short sugar
chains that were abundant in duck intestine. Human and chicken viruses did not
bind to these gangliosides and bound more strongly than duck virus to
gangliosides with long sugar chains that were found in chicken intestinal and
monkey lung tissues. Our data suggest that the spectrum of
sialylglycoconjugates which can serve as influenza virus receptors in chicken
is more similar to the spectrum of receptors in the respiratory epithelia of
monkey than to that in the epithelial tissues of duck. This notion could
explain the recent emergence of avian H9N2 virus lineage with human virus-like
receptor specificity and emphasizes the role of the chicken as a potential
intermediate host for the transmission of viruses from aquatic birds to humans.
Descriptors: chickens, ducks, influenza A virus avian
metabolism, influenza A virus human metabolism, receptors, virus chemistry,
receptors, virus metabolism, binding sites, cell membrane metabolism,
cercopithecus aethiops, epithelial cells metabolism, gangliosides chemistry, gangliosides metabolism,
oligosaccharides chemistry, oligosaccharides metabolism, receptors, cell
surface chemistry, receptors, cell surface metabolism.
Gambaryan, A.S., A.B. Tuzikov, N.V. Bovin, S.S.
Yamnikova, D.K. Lvov, R.G. Webster, and M.N. Matrosovich (2003). Differences
between influenza virus receptors on target cells of duck and chicken and
receptor specificity of the 1997 H5N1 chicken and human influenza viruses from
Hong Kong. Avian Diseases
47(Special Issue): 1154-1160. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: To study whether influenza virus receptors in
chickens differ from those in other species, we compared the binding of lectins
and influenza viruses with known receptor specificity to cell membranes and
gangliosides from epithelial tissues of ducks, chickens, and African green
monkeys. We found that chicken cells contained Neu5Acalpha(2-6)Gal-terminated
receptors recognized by Sambucus nigra lectin and by human viruses. This
finding explains how some recent H9N2 viruses replicate in chickens despite
their human virus-like receptor specificity. Duck virus bound to gangliosides
with short sugar chains that were abundant in duck intestine. Human and chicken
viruses did not bind to these gangliosides and bound more strongly than duck
virus to gangliosides with long sugar chains that were found in chicken
intestinal and monkey lung tissues. Chicken and duck viruses also differed by
their ability to recognize the structure of the third sugar moiety in
Sia2-3Gal-terminated receptors. Chicken viruses preferentially bound to
Neu5Acalpha(2-3)Galbeta(1-4)GlcNAc-containing synthetic sialylglycopolymer,
whereas duck viruses displayed a higher affinity for
Neu5Acalpha(2-3)Galbeta(1-3)GalNAc-containing polymer. Our data indicate that
sialyloligosaccharide receptors in different avian species are not identical
and provide a potential explanation for the differences between the
hemagglutinin and neuraminidase proteins of duck and chicken viruses.
Descriptors: cell biology, infection, avian influenza,
infectious disease, respiratory system disease, viral disease, receptor
specificity target cells.
Gambaryan, A.S., A.B. Tuzikov, V.E. Piskarev, S.S.
Yamnikova, D.K. Lvov, J.S. Robertson, N.V. Bovin, and M.N. Matrosovich (1997). Specification
of receptor-binding phenotypes of influenza virus isolates from different hosts
using synthetic sialylglycopolymers: non-egg-adapted human H1 and H3 influenza
A and influenza B viruses share a common high binding affinity for
6'-sialyl(N-acetyllactosamine). Virology 232(2): 345-50. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Synthetic sialylglycoconjugates bearing
3'-sialyllactose, 6'-sialyllactose, or 6'-sialyl(N-acetyllactosamine) moieties
attached to the polyacrylic acid carrier (P-3-SL, P-6-SL, and P-6-SLN, respectively)
were prepared and tested for their ability to bind to influenza virus isolates
from different hosts in a competitive solid phase assay. The virus panel
included egg-grown avian and porcine strains, as well as human viruses isolated
and propagated solely in mammalian (MDCK) cells and their egg-adapted variants.
A clear correlation was observed between the pattern of virus binding of two
glycopolymers, P-3-SL and P-6-SLN, and the host species from which the virus
was derived. Avian isolates displayed a high binding affinity for P-3-SL and a
two to three orders of magnitude lower affinity for P-6-SLN. By contrast, all
non-egg-adapted human A and B viruses bound P-6-SLN strongly but did not bind
P-3-SL. Unlike the "authentic" human strains, their egg-adapted
counterparts acquired an ability to bind P-3-SL, indicative of a shift in the
receptor-binding phenotype toward the recognition of Neu5Ac2-3Gal-terminated
sugar sequences. Among the porcine viruses and human isolates with porcine
hemagglutinin, few displayed an avian-like binding phenotype, while others
differed from both avian and human strains by a reduced ability to discriminate
between P-3-SL and P-6-SLN. Our data show that sialylglycopolymers may become a
useful tool in studies on molecular mechanisms of interspecies transfer, tissue
specificity, and other structure-function relationships of the influenza virus
hemagglutinin.
Descriptors: amino sugars metabolism, influenza A virus
avian metabolism, human metabolism, porcine metabolism, influenza B virus
metabolism, lactose analogs and derivatives, receptors, virus metabolism,
sialic acids metabolism, amino sugars chemistry, cell line, chick embryo, dogs,
glycoconjugates metabolism, human isolation and purification, influenza B virus
isolation and purification, lactose chemistry, lactose metabolism, phenotype,
receptors, virus chemistry, sialic acids chemistry.
Gambaryan, A., S. Yamnikova, D. Lvov, A. Tuzikov, A.
Chinarev, G. Pazynina, R. Webster, M. Matrosovich, and N. Bovin (2005). Receptor
specificity of influenza viruses from birds and mammals: new data on
involvement of the inner fragments of the carbohydrate chain. Virology
334(2): 276-283.
NAL
Call Number: 448.8 V81
Abstract: We studied receptor-binding properties of
influenza virus isolates from birds and mammals using polymeric conjugates of
sialooligosaccharides terminated with common Neu5Ac[alpha]2-3Gal[beta] fragment
but differing by the structure of the inner part of carbohydrate chain. Viruses
isolated from distinct avian species differed by their recognition of the inner
part of oligosaccharide receptor. Duck viruses displayed high affinity for
receptors having [beta]1-3 rather than [beta]1-4 linkage between
Neu5Ac[alpha]2-3Gal-disaccharide and penultimate N-acetylhexosamine residue.
Fucose and sulfate substituents at this residue had negative and low effect,
respectively, on saccharide binding to duck viruses. By contrast, gull viruses
preferentially bound to receptors bearing fucose at N-acetylglucosamine
residue, whereas chicken and mammalian viruses demonstrated increased affinity
for oligosaccharides that harbored sulfo group at position 6 of
([beta]1-4)-linked GlcNAc. These data suggest that although all avian influenza
viruses preferentially bind to Neu5Ac[alpha]2-3Gal-terminated receptors, the
fine receptor specificity of the viruses varies depending on the avian species.
Further studies are required to determine whether observed host-dependent
differences in the receptor specificity of avian viruses can affect their
ability to infect humans.
Descriptors: animals, birds, carbohydrate sequence,
chickens, ducks, humans, avian influenza A virus metabolism, avian influenza A
virus pathogenicity, human influenza A virus metabolism, human influenza A
virus pathogenicity, porcine influenza A virus metabolism, porcine influenza A
virus pathogenicity, molecular models, molecular sequence data,
oligosaccharides chemistry, oligosaccharides metabolism, virus receptors
chemistry, virus receptors metabolism, species specificity, swine, U.S.
Government P.H.S. research support, N.I.H. extramural research support,
non-U.S. Government research support.
Gamblin, S.J., L.F. Haire, R.J. Russell, D.J.
Stevens, B. Xiao, Y. Ha, N. Vasisht, D.A. Steinhauer, R.S. Daniels, A. Elliot,
D.C. Wiley, and J.J. Skehel (2004). The structure and receptor binding
properties of the 1918 influenza hemagglutinin. Science 303(5665):
1838-42. ISSN: 1095-9203.
NAL
Call Number: 470 Sci2
Abstract: The 1918 influenza pandemic resulted in about
20 million deaths. This enormous impact, coupled with renewed interest in
emerging infections, makes characterization of the virus involved a priority.
Receptor binding, the initial event in virus infection, is a major determinant
of virus transmissibility that, for influenza viruses, is mediated by the
hemagglutinin (HA) membrane glycoprotein. We have determined the crystal
structures of the HA from the 1918 virus and two closely related HAs in complex
with receptor analogs. They explain how the 1918 HA, while retaining receptor
binding site amino acids characteristic of an avian precursor HA, is able to
bind human receptors and how, as a consequence, the virus was able to spread in
the human population.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, hemagglutinin glycoproteins, influenza virus metabolism, influenza
virology, influenza A virus, human immunology, receptors, virus metabolism,
amino acid sequence, binding sites, birds, crystallography, x-ray, history,
20th century, hydrogen bonding, influenza epidemiology, influenza history,
avian immunology, avian metabolism, human metabolism, human pathogenicity,
porcine immunology, porcine metabolism, membrane glycoproteins chemistry,
membrane glycoproteins metabolism, models, molecular, molecular sequence data,
protein conformation, protein structure, tertiary, sequence alignment, sialic
acids metabolism, species specificity, swine.
Gandhi, S.S., H.B. Bell, and D.C. Burke (1971). Abortive
infection of L cells by fowl plague virus: comparison of RNA and protein
synthesis in infected chick and L cells. Journal of General Virology
13(3): 424-32. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: cultured cells metabolism, influenza A virus
avian pathogenicity, l cells cell line, proteins biosynthesis, RNA
biosynthesis, antigens, viral metabolism, carbon isotopes, cell fractionation,
cell nucleus metabolism, chick embryo,
complement fixation tests, cytopathogenic effect, viral, cytoplasm metabolism,
dactinomycin pharmacology, electrophoresis, disc, hemagglutinins viral
metabolism, avian enzymology, avian growth and development, avian immunology
avian metabolism, neuraminidase metabolism, RNA viral biosynthesis, time
factors, tritium, uridine metabolism,
valine metabolism, viral proteins biosynthesis, virus replication.
Garber, E.A., H.T. Chute, J.H. Condra, L. Gotlib,
R.J. Colonno, and R.G. Smith (1991). Avian cells expressing the murine Mx1
protein are resistant to influenza virus infection. Virology 180(2):
754-62. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The cDNA encoding the murine Mx1 protein, a
mediator of resistance to influenza virus, was inserted into a
replication-competent avian retroviral vector in either the sense (referred to
as Mx+) or the antisense (referred to as Mx-) orientation relative to the viral
structural genes. Both vectors produced virus retaining the Mx insert (Mx
recombinant viruses referred to as Mx+ and Mx-) following transfection into
chicken embryo fibroblasts (CEF). Mx protein of the appropriate size and
nuclear localization was expressed only in CEF cells infected with the Mx+
virus. Mx expression was observed in all Mx(+)-infected cells and was stable
during long-term culture. Cells infected with the Mx+ virus were resistant to
infection by human influenza A/WSN/33 (H1N1) and avian influenza viruses
A/Turkey/Wisconsin/68 (H5N9) and A/Turkey/Massachusetts/65 (H6N2), but were
susceptible to infection by the enveloped RNA viruses Sindbis and vesicular
stomatitis virus (VSV). Normal CEF and cells infected with the Mx virus were
susceptible to influenza A, Sindbis, and VSV. The synthesis of influenza
proteins, especially the larger polymerase and hemagglutinin proteins, was
reduced in Mx+ retrovirus-infected cells superinfected by influenza A.
Descriptors: GTP binding proteins, influenza A virus avian
growth and development, growth and development, proteins physiology,
transfection, virus inhibitors physiology, cell line, cultured cells, chick embryo,
fibroblasts cytology, fluorescent antibody technique, genetic predisposition to
disease, immunoblotting, mice, mice, inbred strains, plaque assay, proteins
genetics.
Garcia Gancedo, A., E. Ronda, M.L. Alonso, and P.
Vilas (1967). Study of a hemagglutination inhibitor from HeLa cells. Microbiologia
Espanola 20(3): 203-17. ISSN:
0026-2595.
NAL
Call Number: 448.3 M583
Descriptors: HeLa cells immunology, hemagglutination
inhibition tests, influenza A virus avian immunology, methods.
Garcia, M., J.M. Crawford, J.W. Latimer, E. Rivera
Cruz, and M.L. Perdue (1996). Heterogeneity in the haemagglutinin gene and
emergence of the highly pathogenic phenotype among recent H5N2 avian influenza
viruses from Mexico. Journal of General Virology 77(Pt.7): 1493-1504. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Molecular changes in the haemagglutinin
(HA)-coding regions and proteolytic cleavage sites from multiple H5N2 subtype
viruses isolated during a recent outbreak of avian influenza (AI) in central
Mexico have been characterized. Eighteen isolates, collected during a 15 month
period (October 1993 to January 1995) from six central states, were sequenced.
None of the 18 predicted HA1 amino acid sequences were identical and changes
were not restricted to a specific region of the sequence. Phylogenetic analyses
of the HA1 sequences demonstrated two virus lineages, designated Puebla and
Jalisco, with sequence variation as high as 10.5% for amino acid and 6.2% for
nucleotide sequences. During the latter months of the surveillance period,
highly pathogenic (HP) strains of AI emerged causing lethal disease in
commercial poultry flocks. In each of the HP strains isolated, the HA protein
was cleaved in chicken embryo fibroblast cells in the absence of trypsin, and
two alterations not found in earlier non-HP isolates were detected. In the HA
protein, HP strains all had a glutamic acid replaced by lysine substitution at
amino acid position 324 and an insertion of arginine and lysine as new residues
325 and 326. The insertion appears to be due to a duplication of the nucleotide
sequence AAAGAA at nucleotide positions 965-970 of the HA1-coding region.
Computer-assisted secondary structure analyses place the target for the
insertion in a predicted RNA stem-loop structure. A mechanism is suggested by
which the polymerase duplicates the sequence.
Descriptors: avian influenza virus, structural genes,
viral hemagglutinins, nucleotide sequences, amino acid sequences,
pathogenicity, phenotypes, heterogeneity, phylogeny, molecular conformation,
Mexico, secondary structure, cleavage site sequence, molecular sequence data,
GENBANK u37165, GENBANK u37166, GENBANK u37167, GENBANK u37168, GENBANK u37168,
GENBANK u37169, GENBANK u37170, GENBANK u37171, GENBANK u37172, GENBANK u37173,
GENBANK u37174, GENBANK u37175, GENBANK u37176, GENBANK u37177, GENBANK u37178,
GENBANK u37179, GENBANK u37180, GENBANK u37181, GENBANK u37182.
Garcia Sastre, A., A. Egorov, D. Matassov, S. Brandt,
D.E. Levy, J.E. Durbin, P. Palese, and T. Muster (1998). Influenza A virus
lacking the NS1 gene replicates in interferon-deficient systems. Virology
252(2): 324-30. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: gene deletion, influenza physiopathology,
influenza A virus avian genetics, viral nonstructural proteins genetics, virus
replication, cell line, Cercopithecus aethiops, chick embryo, DNA
binding proteins genetics, DNA binding proteins physiology, dogs, influenza
genetics, influenza A virus avian physiology, kidney, mice, mice inbred BALB c,
mice, inbred c57bl, mice, knockout, signal transduction, trans activators
genetics, trans activators physiology,
transfection, vero cells, viral nonstructural proteins metabolism.
Gardner, I.D. and K.F. Shortridge (1979). Recombination
as a mechanism in the evolution of influenza viruses: a two-year study of ducks
in Hong Kong. Reviews of Infectious Diseases 1(5): 885-90. ISSN: 0162-0886.
NAL
Call Number: RC111.R4
Abstract: An analysis was made of 149 influenza A
viruses isolated from ducks in Hong Kong during the period of November 1975
through October 1977. The viruses were isolated five times more frequently from
ducks raised in the People's Republic of China than from those raised in Hong
Kong. The isolation rate fo viruses was higher from the cloaca than it was from
the trachea, but this pattern varied over the two years of investifation. The
large number of different combinations (30) of hemagglutinin and neuraminidase
genes suggests that recombination of viruses was taking place. Analysis of
these combinations showed that their distribution was not random and that
certain combinations occured more frequently, and others less frequently, than
was expected. The recombination of influenza viruses and the excess or
restriction of certain combinations may have implications for the evolution of
pandemic strains of influenza virus in humans.
Descriptors: ducks microbiology, influenza A virus avian
genetics, recombination, genetic, China, cloaca microbiology, evolution, gene
frequency, genotype, hemagglutinins viral genetics, Hong Kong, influenza A
virus avian isolation and purification, neuraminidase genetics, paramyxoviridae
isolation and purification, seasons, trachea microbiology.
Garten, W., S. Hallenberger, D. Ortmann, W. Schaefer,
M. Vey, H. Angliker, E. Shaw, and H.D. Klenk (1994). Processing of viral
glycoproteins by the subtilisin-like endoprotease furin and its inhibition by
specific peptidylchloroalkylketones. Biochimie Paris 76(3-4):
217-225. ISSN: 0300-9084.
NAL
Call Number: 383 So1
Abstract: The spike glycoproteins of many enveloped
viruses are proteolytically cleaved at the carboxytermini of sequences
containing the basic motif R-X-K/R-R. Cleavage is often necessary for the
fusion capacity of the glycoproteins and, thus, for virus infectivity. Among
these viruses are pathogenic avian influenza viruses, human parainfluenza
virus, human cytomegalovirus, and human immunodeficiency virus; it has been
demonstrated that these viruses can be activated by furin. Indigenous furin has
been identified in T-lymphocytes, which are host cells for HIV. Furin has been
localized in the TGN and on the surface of cells after vectorial expression.
Peptidylchloroalkylketones have been designed that inhibit with high
specificity cleavage and fusion activity of viral glycoproteins, as well as
virus replication.
Descriptors: blood and lymphatics, cell biology,
enzymology, genetics, infection, membranes, metabolism, microbiology, molecular
genetics, avian influenza viruses, cell surface, cleavage, fusion activity,
glycoprotein fusion, human parainfluenza virus, T lymphocyte, trans Golgi
network, viral infectivity, virus infectivity, virus replication.
Garten, W., D. Linder, R. Rott, and H.D. Klenk
(1982). The cleavage site of the hemagglutinin of fowl plague virus. Virology
122(1): 186-90. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian metabolism, protein precursors metabolism, amino acid sequence,
peptide fragments analysis, protein processing, post translational.
Garten, W., A. Stieneke, E. Shaw, P. Wikstrom, and
H.D. Klenk (1989). Inhibition of proteolytic activation of influenza virus
hemagglutinin by specific peptidyl chloroalkyl ketones. Virology
172(1): 25-31. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Lysates of cultured cells have been analyzed
for arginine-specific endoproteases using peptidyl-p-nitroanilides as
chromogenic substrates. The enzymes present in MDBK, MDCK, VERO, BHK, and chick
embryo cells required lysine-arginine or arginine-arginine pairs as cleavage
sites, whereas chorioallantoic membrane cells contained, in addition, an
activity that could cleave at a single arginine. The effect of peptidyl
chloroalkyl ketones on the activation of the fowl plague virus hemagglutinin by
the proteases specific for paired basic residues has been investigated. When
virions containing uncleaved hemagglutinin were incubated with lysates of
uninfected cells, cleavage was completely inhibited by peptidyl chloroalkyl
ketones containing paired basic residues at a concentration of 1 mM. In
contrast a compound containing a single arginine had no inhibitory activity.
When dibasic peptidyl chloroalkyl ketones were added to infected cell cultures,
cleavage of hemagglutinin and multiple cycles of virus replication were
inhibited at 10 mM. However, a 100- to 200-fold increase of the inhibitory
activity in intact cells could be achieved by N-terminal acylation. These
studies suggest a potential role of peptidyl chloroalkyl ketones as antiviral
agents.
Descriptors: amino acid chloromethyl ketones pharmacology,
hemagglutinins viral metabolism, influenza A virus avian metabolism, protease
inhibitors pharmacology, protein processing, post translational drug effects,
cell membrane enzymology, cultured cells, dogs, molecular weight, protease
inhibitors chemical synthesis, structure activity relationship, virus
replication.
Garten, W., M. Vey, R. Ohuchi, M. Ohuchi, and H.D.
Klenk (1991). Modification of the cleavage activation of the influenza virus
hemagglutinin by site-specific mutagenesis. Behring Institute
Mitteilungen (89): 12-22. ISSN:
0301-0457.
NAL
Call Number: QR180.B4
Abstract: Factors determining cleavability of influenza
virus hemagglutinin which is activated by ubiquitous cellular endoproteases
were analysed by carrying out site-directed mutagenesis on the cloned
hemaglutinin genes of strains A/FPV/Rostock/34 (subtype H7) and A/Port
Chalmers/1/73 (subtype H3). Substitutions at the cleavage site of the H7
hemagglutinin indicate that the tetrapeptide Arg-X-Lys/Arg-Arg is the minimal
consensus sequence recognized by the ubiquitous proteases. The H3 hemagglutinin
also became susceptible to these enzymes, when additional arginines were
inserted at the cleavage site. Three arginines were sufficient, when the
carbohydrate was removed, whereas four additional arginines are needed when
this carbohydrate was present, indicating that the accessibility of the
cleavage motif is important for the protease. The appropriate localization of
the basic cleavage motif within the amino acid sequence and the spatial
structure of the hemagglutinin precursor is an additional prerequisite for
cleavage.
Descriptors: endopeptidases metabolism, genes viral,
hemagglutinins viral genetics, influenza A virus avian genetics, mutagenesis,
site directed, amino acid sequence, base sequence, cell fusion, cell line,
hemagglutinin glycoproteins, influenza virus, hemagglutinins viral metabolism,
influenza A virus avian immunology, molecular sequence data,
oligodeoxyribonucleotides, recombinant proteins metabolism, viral envelope
proteins genetics.
Garten, W., C. Will, K. Buckard, K. Kuroda, D.
Ortmann, K. Munk, C. Scholtissek, H.
Schnittler, D. Drenckhahn, and H.D. Klenk (1992). Structure and assembly of
hemagglutinin mutants of fowl plague virus with impaired surface transport.
Journal of Virology 66(3): 1495-505.
ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Five temperature-sensitive mutants of
influenza virus A/FPV/Rostock/34 (H7N1), ts206, ts293, ts478, ts482, and ts651,
displaying correct hemagglutinin (HA) insertion into the apical plasma membrane
of MDCK cells at the permissive temperature but defective transport to the cell
surface at the restrictive temperature, have been investigated. Nucleotide
sequence analysis of the HA gene of the mutants and their revertants
demonstrated that with each mutant a single amino acid change is responsible
for the transport block. The amino acid substitutions were compared with those
of mutants ts1 and ts227, which have been analyzed previously (W. Schuy, C.
Will, K. Kuroda, C. Scholtissek, W. Garten, and H.-D. Klenk, EMBO J.
5:2831-2836, 1986). With the exception of ts206, the changed amino acids of all
mutants and revertants accumulate in three distinct areas of the
three-dimensional HA model: (i) at the tip of the 80-A (8-nm)-long alpha helix,
(ii) at the connection between the globular region and stem, and (iii) in the
basal domain of the stem. The concept that these areas are critical for HA
assembly and hence for transport is supported by the finding that the mutants
that are unable to leave the endoplasmic reticulum at the nonpermissive
temperature do not correctly trimerize. Upon analysis by density gradient
centrifugation, cross-linking, and digestion with trypsin and
endoglucosaminidase H, two groups can be discriminated among these mutants:
with ts1, ts227, and ts478, the HA forms large irreversible aggregates, whereas
with ts206 and ts293, it is retained in the monomeric form in the endoplasmic
reticulum. With a third group, comprising mutants ts482 and ts651 that enter
the Golgi apparatus, trimerization was not impaired.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian metabolism, membrane glycoproteins metabolism, amino acid sequence,
base sequence, biological transport, cell membrane metabolism, cell polarity,
hemagglutinins viral chemistry, hemagglutinins viral genetics, influenza A
virus avian genetics, macromolecular systems, membrane glycoproteins chemistry,
membrane glycoproteins genetics, molecular sequence data, protein binding,
protein conformation, protein processing, post translational, RNA viral
genetics.
Geisler, B., W. Seidel, and L. Dohner (1987). Untersuchung
zum Vergleich des Nukleoproteins aviarer und humaner Influenzavirusstamme.
[Comparison of nucleoproteins of avian and human influenza virus types]. Archiv
Fur Experimentelle Veterinarmedizin 41(5): 686-91. ISSN: 0003-9055.
NAL
Call Number: 41.8 Ex7
Descriptors: influenza A virus avian genetics, influenza A
virus human genetics, nucleoproteins analysis, birds, electrophoresis,
polyacrylamide gel, peptide mapping.
Geisler, B., W. Seidel, B. Herrmann, and L. Dohner
(1986). Differences of nucleoproteins of human and avian influenza A virus
strains shown by polyacrylamide gel electrophoresis and by the peptide mapping
technique. Archives of Virology 90(3-4): 289-99. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Electrophoretic mobility differences in
polyacrylamide gels were detected between (35S)-methionine-labelled
nucleoproteins (NPs) induced in monolayer cells by 15 human and 4 avian
reference strains of influenza viruses. The (35S)-methionine-labelled tryptic
peptides of nucleoproteins of these strains were also analyzed by peptide mapping
technique. Based on several detectable hydrophilic peptides the NPs could be
arranged in 7 clearly differentiable groups. After radioiodination of NPs from
4 human and 3 avian reference strains the tryptic peptide patterns showed one
clear difference between human and avian strains.
Descriptors: influenza A virus analysis, nucleoproteins
analysis, viral proteins analysis, electrophoresis, polyacrylamide gel,
influenza A virus avian analysis, influenza A virus avian genetics, influenza A
virus human analysis, influenza A virus human genetics, influenza A virus
genetics, peptide fragments analysis, variation genetics.
Geisler, B., V. Zeidel, B. Herrmann, and L. Dener
(1986). Variatsii belka NP virusa grippa, vyiavliaemye posredstvom
peptidnogo kartirovaniia i elektroforeza v poliakrilamidnom gele. [Variations
in the NP protein of the influenza virus detected by peptide mapping and
polyacrylamide gel electrophoresis]. Voprosy Virusologii 31(5):
538-44. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: NP proteins of 19 reference and 42 epidemic
strains of influenza A virus were analysed for their mobility in polyacrylamide
gel electrophoresis and distribution of tryptic peptides. The strains could be
divided into 4 groups by differences in their electrophoretic mobility, and
into 9 groups according to reproducible differences of several hydrophilic
peptides determined by peptide mapping.
Descriptors: influenza A virus avian analysis, influenza A
virus human analysis, nucleoproteins analysis, variation genetics, viral
proteins analysis, birds, electrophoresis, polyacrylamide gel methods, East
Germany, peptide mapping methods, viral structural proteins.
Gendon, I.U.Z. (1977). Vliianie obrabotki
neiraminidazoi fibroblastov kurinogo embriona na adsorpbtsiiu i reproduktsiiu
virusa chumy ptits. [Effect of neuraminidase treatment of chick embryo
fibroblasts on the adsorption and reproduction of the fowl plague virus]. Voprosy
Virusologii (4): 429-32. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Treatment with neuraminidase (100 units/ml)
of chick embryo fibroblasts in vitro only partially inhibits adsorption of fowl
plague virus on these cells. Cultivation of chick embryo fibroblasts in the
presence of 50 units/ml neuraminidase had no effect on the sensitivity of these
cells to fowl plague virus and on the extent of virus reproductions. It is
suggested that neuraminic acid which is a component of the external cell
membrane is not only substance responsible for adsorption of orthomyxoviruses.
Descriptors: influenza A virus avian drug effects,
neuraminidase pharmacology, virus replication drug effects, adsorption, chick
embryo, dose response relationship, drug, fibroblasts drug effects, time
factors, virus cultivation.
Gendon, I.U.Z., V.P. Ginzburg, G.I.A. Solov'ev, and
L.M. Babushkina (1969). Izmenenie sinteza RNK v kletkakh kul'tury tkani,
infitsirovannoi miksovirusami. [Changes in RNA synthesis in tissue culture
cells infected with myxoviruses]. Voprosy Virusologii 14(5):
526-32. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian metabolism, Newcastle
disease virus metabolism, RNA biosynthesis, radiation effects, carbon isotopes,
chick embryo, cycloheximide pharmacology, fibroblasts metabolism, fowl plague metabolism,
influenza A virus avian radiation effects,
Newcastle disease metabolism, Newcastle disease virus radiation effects,
RNA nucleotidyltransferases metabolism, tissue culture, ultraviolet rays,
uridine metabolism.
Gendon, I.U.Z., S.G. Markushin, and S.I.A. Mel'nikova
(1986). Vliianie remantadina na gemoliticheskuiu aktivnost' gemaggliutinina
virusa grippa. [Effect of remantadine on the hemolytic activity of influenza
virus hemagglutinin]. Voprosy Virusologii 31(4): 414-20. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: adamantane analogs and derivatives,
hemagglutinins viral immunology, hemolysis drug effects, influenza A virus
avian drug effects, influenza A virus human drug effects, rimantadine
pharmacology, drug resistance, microbial, genes viral drug effects,
hydrogen-ion concentration, influenza A virus avian genetics, influenza A virus
avian immunology, influenza A virus human genetics, influenza A virus human
immunology, protease inhibitors pharmacology, recombination, genetic drug
effects.
Generalov, V.M., T.S. Bakirov, A.G. Durymanov, A.N.
Sergeev, L.N. Shishkina, V.A. Petrishchenko, V.S. Toporkov, G.I. Tyunnikov, A.A. Medvedev, V.D. Poryvaev,
and O.V. Fefelov (2002). Study of virus-cell interaction by the method of
dielectrophoresis. Doklady. Biochemistry and Biophysics 383:
82-4. ISSN: 1607-6729.
NAL
Call Number: QP501.D65
Descriptors: cell physiology, cells virology, viral
physiology, viruses radiation effects, cells radiation effects, chickens,
electromagnetic fields, erythrocytes physiology, erythrocytes virology, haplorhini, influenza
A virus avian physiology.
Gerber, A., C. Sauter, and J. Lindenmann (1973). Fowl
plague virus adapted to human epithelial tumor cells and human myeloblasts in
vitro. I. Characteristics and replication in monolayer cultures. Archiv
Fur Die Gesamte Virusforschung 40(1): 137-51. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian growth and
development, virus cultivation, virus replication, bone marrow microbiology,
bone marrow cells, carcinoma, bronchogenic, cell line, chick embryo, clone
cells, cytological techniques, cytopathogenic effect, viral, diploidy,
epithelial cells, epithelium microbiology, fibroblasts microbiology, HeLa
cells, hemagglutination inhibition tests, leukemia, myelocytic, acute, plaque
assay.
Gerber, A., C. Sauter, and J. Lindenmann (1973). Fowl
plague virus adapted to human epithelial tumor cells and human myeloblasts in
vitro. II. Replication in human leukemic myoloblast cultures. Archiv Fur
Die Gesamte Virusforschung 40(3): 255-64.
ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: bone marrow microbiology, bone marrow cells,
influenza A virus avian growth and development, leukemia, myelocytic, acute
microbiology, virus replication, adult, aged, cultured cells, hemadsorption,
influenza A virus avian pathogenicity, middle aged, virulence, virus
cultivation.
Gerganov, G. and K. Surtmadzhiev (1982). Kultivirane
na niakoi ptichi virusi v trakhealni organni kulturi ot fazani i kokoshi
zarodishi. [Cultivation of various avian viruses in pheasant trachea organ
cultures and chick embryos]. Veterinarnomeditsinski Nauki 19(2):
18-24. ISSN: 0324-1068.
NAL
Call Number: 41.8 V6468
Abstract: Stationary tracheal organ cultures of
pheasants and chick embryos, treated with a mucolytic agent were used to study
the ciliostatic effect of the following viruses: fowl pest (FPV), Newcastle
disease (NDV), infections laryngotracheitis (ILV), and infections bronchitis
(IBV) - strain Beaudette. In chick embryo tracheal cultures ciliostasis was
found to set in as follows: for FPV - at the 24th hour; for NDV - at the
72nd-120th hour; for ILV - at the 168-192nd hour; and for IBV-at the 72nd-96th
hour. The ciliostatic effect produced by
NDV and IBV coincided in terms of time and dynamics. In pheasant tracheal organ
cultures ciliostasis set in as follows: for FPV - at the 24th hour; for NDV -
at the 72nd-120th hour; and for ILV - at the 168-192nd hour. This system was
shown to be unsusceptible to IBV which produced no effect whatever. In mixed
organic cultures, containing several tracheal segments of pheasants and chick
embryos each per petri dish IBV did bring about ciliostasis in the chick embryo
segments only, within the period after inoculation as cited above. It is stated
that pheasant tracheal organ cultures could be employed in the case of an
express initial differentiation of FPV, NDV, and ILV, recording the time period
for the setting in of full ciliostasis following the inoculation of the
respective viruses. Discussed is the possibility of identifying IBV, using
mixed tracheal organ cultures of pheasants and chick embryos.
Descriptors: coronaviridae growth and development,
herpesviridae growth and development, herpesvirus 1, gallid growth and
development, infectious bronchitis virus growth and development, influenza A
virus avian growth and development, Newcastle disease virus growth and
development, birds, chick embryo, organ culture, trachea, virus cultivation
methods.
Germanov, A.B. (1976). A genetic approach to
studies on the synthesis of the complementary RNA's of fowl plague virus. Journal
of General Virology 31(3): 281-8.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The rate of incorporation of 5-fluorouracil
into complementary strands of replicating RNA of fowl plague virus (FPV) has
been studied. The efficiency of incorporation was estimated by determination of
the reversion frequency in s-mutants with known types of base transitions in
the RNA of the virus particle. It was established that maximum incorporation of
5-fluorouracil into progeny virus particle RNA took place between 2 and 4 h
after infection. The maximum incorporation of the mutagen into complementary
RNA (plus strands) occurred when the cells were exposed to 5-fluorouracil from
1 to 2 h after infection.
Descriptors: influenza A virus avian metabolism, mutation,
RNA viral biosynthesis, base sequence,
ethyl methanesulfonate pharmacology, fluorouracil metabolism,
fluorouracil pharmacology, hydroxylamines pharmacology, influenza A virus avian
growth and development, mutagens, nitrous acid pharmacology, virus replication.
Germanov, A.B., N.A. Parasiuk, and M.I. Sokolov
(1973). Study on the mutagenic action of O-methylhydroxylamine on RNA
viruses (on the model of fowl plague virus). Acta Virologica 17(5):
377-83. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: hydroxylamines pharmacology, influenza A
virus avian drug effects, mutagens pharmacology, mutation drug effects,
cultured cells, chick embryo, cytosine metabolism, hydrogen-ion concentration,
influenza A virus avian metabolism, influenza A virus avian pathogenicity,
plaque assay, RNA viral metabolism, time factors, uracil metabolism.
Germanov, A.B., M.I. Sokolov, I.A. Myasnikova, N.A.
Parasiuk, T.V. Vorontsova, and G.V. Kornilaeva (1972). Some biological and
physico-chemical properties of plaque mutants of fowl plague virus. Brief
report. Archiv Fur Die Gesamte Virusforschung 39(4): 389-92. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian drug effects,
influenza A virus avian radiation effects, mutation, centrifugation, density
gradient, chick embryo, chromatography, DEAE-cellulose, fibroblasts, mutagens,
protamines pharmacology, radiation effects, sodium chloride, temperature,
tissue culture, ultraviolet rays, virus replication.
Germanov, A.B., M.I. Sokolov, and N.A. Parasiuk
(1972). The application of DEAE-cellulose column chromatography to the
selection of S+ revertants and determination of reversion frequency in
populations of S- mutants of fowl plague virus. Journal of General
Virology 17(1): 49-54. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: chromatography, DEAE-cellulose, influenza A
virus avian isolation and purification, mutation, chick embryo, culture media,
evaluation studies, fibroblasts, genetics, microbial, hemagglutination tests, hydroxylamines,
influenza A virus avian growth and development, mutagens, protamines, sodium chloride,
tissue culture.
Germanov, A.B., M.I. Sokolov, and T.V. Vorontsova
(1971). Nekotorye aspekty vzaimodeistviia khimicheskikh mutagenov s
reprodutsiruiushcheisia populiatsiei RNKsoderzhanschikh virusov. [Some aspects
of the interaction of chemical mutagens with reproducing populations of RNA-containing
viruses]. Vestnik Akademii Meditsinskikh Nauk SSSR 26(2):
69-74. ISSN: 0002-3027.
Descriptors: genetics, microbial, influenza A virus avian
drug effects, mutagens, virus replication drug effects, acridines, azirines,
mutation, nitroso compounds.
Gharagozlou, M.J. and B. Samadieh (1980). Cytopathogenicity
of two avian influenza A viruses in different cell cultures. Clinica
Veterinaria 103(3): 132-137. ISSN: 0009-9082.
NAL
Call Number: 41.8 C61
Descriptors: cell culture, cytopathogenicity, avian
influenza virus, turkeys.
Gharagozou, M.J. and B. Samadieh (1994). Cytopathogenicity
of two avian influenza viruses in different cell cultures. Archive of
the Faculty of Veterinary Medicine, Tehran University 6: 174-184.
Descriptors: cell culture, cytopathogenicity, avian
influenza virus, poultry.
Ghendon, Y. and O. Blagoveshienskaya (1975). Polyadenylate
sequences of fowl plague virus complementary RNA (cRNA) synthesized in vivo and
in vitro. Virology 68(2): 330-7.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian analysis, poly A
analysis, RNA viral analysis, adenine nucleotides analysis, base sequence, cell
free system, influenza A virus avian metabolism, RNA viral biosynthesis, viral
isolation and purification, tissue culture, viral proteins analysis, viral
proteins biosynthesis.
Ghendon, Y., V.P. Ginsburg, G.Y. Soloviev, and S.G.
Markushin (1970). The fate of influenza virus RNA in cells treated with
ultraviolet rays. Journal of General Virology 6(2): 249-55. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: fibroblasts radiation effects, influenza A
virus avian metabolism, RNA viral biosynthesis, ultraviolet rays, carbon
isotopes, chick embryo, fibroblasts enzymology, RNA viral analysis, radiation
effects, ribonucleases metabolism, thymidine biosynthesis, tissue culture,
uridine biosynthesis, virus replication.
Ghendon, Y., A. Klimov, O. Blagoveshenskaya, and D.
Genkina (1979). Investigation of recombinants of human influenza and fowl
plague viruses. Journal of General Virology 43(1): 183-91. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Recombinants of human influenza type A
viruses, A/Krasnodar/101/1959 (H2N2) or A/Habarovsk/15/1976 (H3N2), and fowl
plague virus (FPV), strain Weybridge (Hav1Neq1) were obtained. The genome of
the recombinant obtained by recombination of influenza A/Habarovsk/15/1976
virus and FPV contained the genes 4 (HA) and 6 (NA) derived from the influenza
A/Habarovsk virus and all the other genes [1, 2, 3, 5 (NP), 7 (M), 8 (NS)] from
FPV. The genome of the recombinant of A/Krasnodar/101/1959 virus and FPV
contained the genes 2, 4 (HA) and 6 (NA) derived from influenza A/Krasnodar
virus and all the other genes [1, 3, 5, (NP), 7 (M), 8 (NS)] from FPV. The
recombinants, like FPV, gave high virus yields in chick embryos and could
multiply at high temperatures (40 and 42 degrees C), but, like human influenza
viruses, were non-pathogenic for chickens and did not replicate in chick embryo
fibroblast culture, but did replicate in a human conjunctiva cell line, clone
1-5C-4. The virion transcriptase of the recombinants, in a number of properties
determined in vitro, was similar to FPV transcriptase but not to the human
influenza virus enzyme.
Descriptors: influenza A virus avian genetics, influenza A
virus human genetics, recombination, genetic, chick embryo, influenza A virus
avian analysis, influenza A virus human analysis, peptides analysis, RNA viral
analysis, viral proteins analysis, virus replication.
Ghendon, Y., S. Markushin, V. Ginzburg, and A. Hay
(1983). Functional defects of fowl plague virus temperature-sensitive mutant
having mutation in the neuraminidase. Archives of Virology 75(1-2):
55-70. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A fowl plague virus (FPV)
temperature-sensitive mutant ts 5 having mutation lesions in the gene coding
for the neuraminidase has been obtained. The mutant induced synthesis of cRNA,
vRNA and proteins in cells under non-permissive conditions, but formation of
virions including non-infectious ones was defective. The neuraminidase and
haemagglutinin synthesized under non-permissive conditions possessed functional
activity and could migrate from the rough endoplasmic reticulum into plasma
membranes; however, cleavage of the haemagglutinin was reduced. In ts
5-infected cells under non-permissive conditions the synthesis of segments 5
and 8 of cRNA and vRNA was predominant both early and late in the reproduction
cycle, and the synthesis of P1, P2, P3, HA and M proteins was reduced after
approximately 3 hours. The data obtained suggest that involvement of the
neuraminidase in the formation of infectious virions may have no direct
association with the enzymatic activity of this protein, and that the mutation
in the neuraminidase may affect regulation of replication and transcription
processes.
Descriptors: defective viruses genetics, influenza A virus
avian genetics, neuraminidase genetics, cell membrane metabolism, genes viral,
hemagglutinins viral genetics, influenza A virus human genetics, mutation, RNA
viral analysis, recombination, genetic, temperature, viral proteins
biosynthesis.
Ghendon, Y., S. Markushin, H. Heider, S. Melnikov,
and V. Lotte (1986). Haemagglutinin of influenza A virus is a target for the
antiviral effect of Norakin. Journal of General Virology 67(Pt. 6):
1115-22. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The anticholinergic anti-parkinsonism drug
Norakin is an inhibitor of influenza virus multiplication. By crossing a
Norakin-resistant variant of fowl plague virus (FPV) strain Weybridge with the
sensitive FPV/Rostock/34 wild-type virus, Norakin-resistant recombinants were
obtained. Analyses of the gene composition showed that all Norakin-resistant
recombinants had inherited their haemagglutinin gene from the Norakin-resistant
parent strain. The majority of the recombinants had received all the other gene
segments from the sensitive parent strain. Norakin was shown to inhibit red
blood cell lysis induced either by purified virions or by the haemagglutinin of
a sensitive FPV strain at low pH, but failed to affect the Norakin-resistant
FPV variant. No aggregation of autoliposomes containing the haemagglutinin of a
sensitive FPV strain or digestion of the HA1 subunit of haemagglutinin by
trypsin occurred in the presence of Norakin at acid pH. The data suggest that
the haemagglutinin of FPV is the target for the antiviral activity of Norakin,
which acts by inhibiting the conformational change in the haemagglutinin at
acid pH important for lysis.
Descriptors: hemagglutinins viral genetics, hemagglutinins
viral metabolism, influenza A virus avian drug effects, piperidines
pharmacology, cultured cells, chick embryo, drug resistance, microbial, genes
viral, hemagglutination drug effects, hemolysis drug effects, hydrogen-ion
concentration, liposomes, membrane fusion drug effects, recombination, genetic,
trypsin metabolism, virus replication drug effects.
Ghendon, Y., S. Markushin, K. Lisovskaya, C.R. Penn, and
B.W. Mahy (1982). Extragenic suppression of a ts phenotype during
recombination between ts mutants of two fowl plague virus strains with a ts
mutation in gene 1. Journal of General Virology 62(Pt. 2):
239-48. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Fowl plague virus (FPV) ts mutants belonging
to six recombination groups and obtained from the Weybridge strain (in the
U.S.S.R.) or the Rostock strain (in the U.K.) have been studied in a
recombination test. Temperature-sensitive mutants obtained from different FPV
strains were revealed which had a ts mutation in gene 1; however, their
crossing resulted in ts+ recombinants which appeared with a high frequency.
This phenomenon was due not to intragenic complementation but to extragenic suppression,
when the expression of a ts phenotype of the Rostock strain mutant gene 1 is
suppressed by gene 2 products of the Weybridge strain.
Descriptors: influenza A virus avian genetics, gene
expression regulation, genes viral, mutation, recombination, genetic,
suppression, genetic, temperature.
Ghendon, Y.U.Z. and A.I. Klimov (1981). Effects of
edeine, hygromycin B and alpha-Sarcin on influenza virus reproduction. Acta
Virologica 25(3): 129-37. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract:
The effects of edeine, hygromycin B and
alpha-sarcin on the synthesis of virus-specific proteins and formation of
infectious virions was studied in cells infected with fowl plague virus (FPV).
The manifestation of the antiviral effect of edeine depended on the
peculiarities of the FPV strains and the host-cell systems. Hygromycin B
inhibited significantly the synthesis of virus-specific proteins and the
formation of the infectious virions, but did not influence protein synthesis in
uninfected cells. Alpha-Sarcin in the concentrations tested neither showed a
marked antiviral activity nor affected protein synthesis in the uninfected
cells.
Descriptors: anti bacterial agents pharmacology, edeine
pharmacology, endoribonucleases, fungal proteins pharmacology, hygromycin B
pharmacology, influenza A virus avian drug effects, virus replication drug
effects, cell line, chick embryo, hamsters, influenza A virus avian growth and
development, influenza A virus avian metabolism, kidney, tissue culture, viral
proteins biosynthesis.
Ghendon, Y.U.Z. and T.A. Mikhailovskaya (1982). Effect
of kanamycin on the reproduction of orthomyxoviruses. Acta Virologica
26(4): 241-6. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Kanamycin sulphate at a concentration of 8
mmol/l had no effect on the protein synthesis in uninfected chick embryo cell
(CEC) cultures, but caused a 2-fold decrease of virus-specific protein
synthesis in CEC infected with fowl plague virus (FPV). Kanamycin at a
concentration of 2 mmol/l decreased the yield of infectious FPV in one growth
cycle experiments on CEC culture by 1.5 log10 units and when added into the
agar overlay it decreased the plaque number by nearly 1 log10 unit. Inoculation
of 10 mg of kanamycin into a chick embryo decreased the yield of virus by 1.0
log10. Administration of kanamycin to mice (5-10 mg for three days post
infection) reduced mortality of the animals 2--3-fold. Antibiotics of the
streptomycin group presumably may penetrate into orthomyxovirus-infected cells
due to virus-induced impairment of leakiness of the cell membrane and inhibit
both the virus protein synthesis and formation of infectious virions.
Descriptors: influenza A virus avian drug effects,
influenza A virus human drug effects, kanamycin pharmacology, cultured cells,
chick embryo, influenza A virus avian growth and development, influenza A virus
human growth and development, influenza A virus human pathogenicity, mice,
proteins biosynthesis.
Ghendon, Y.Z., V.P. Ginsburg, G.Y. Soloviev, and L.
Babushkina (1969). Effect of myxovirus infection on synthesis of cellular
ribonucleic acid. Journal of Virology 3(3): 351-2. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Descriptors: influenza A virus avian, Newcastle disease
virus, RNA biosynthesis, carbon isotopes, chick embryo, cytosine nucleotides
metabolism, fibroblasts, RNA nucleotidyltransferases metabolism, tissue
culture, uridine metabolism, virus replication.
Ghendon, Y.Z., A.T. Marchenko, S.G. Markushin, D.B.
Ghenkina, A.V. Mikhejeva, and E.E. Rozina (1973). Correlation between TS
phenotype and pathogenicity of some animal viruses. Archiv Fur Die
Gesamte Virusforschung 42(2): 154-9.
ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian pathogenicity,
mutation, polioviruses pathogenicity, brain microbiology, chick embryo,
chickens, cytopathogenic effect, viral, genetic complementation test,
haplorhini, HeLa cells, influenza A virus avian growth and development,
influenza A virus avian isolation and purification, Macaca, mutagens,
phenotype, polioviruses growth and development, polioviruses isolation and
purification, spinal cord microbiology, temperature, tissue culture, virus
cultivation, virus replication.
Ghendon, Y.Z. and S.G. Markushin (1980). Studies
on mutation lesions and physiology of fowl plague virus ts mutants. Philosophical
Transactions of the Royal Society of London. Series B Biological Sciences
288(1029): 383-92. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Abstract:
Temperature-sensitive (ts) mutants of
fowl plague virus (FPV) were divided into six complementation groups.
Experiments with ts mutants having defects of transcription showed that in FPV
strain Weybridge, protein P1 coded by gene N2 takes part in primary transcription,
and protein P3 coded for by gene N1 takes part in secondary transcription. Ts
mutants of FPV with lower pathogenicity were present in all six complementation
groups under study. Simultaneous inoculation of chickens with two pathogenic ts
mutants of FPV caused death of the chickens and a pathogenic virus with ts+
phenotype was isolated from their organs. By recombination of ts multimutant
FPV with human influenza virus a recombinant was obtained that contained genes
coding for the haemagglutinin and neuraminidase of human influenza virus; all
other genes were derived from FPV. In experiments on volunteers this
recombinant appeared to be non-reactogenic but capable of inducing antibody
formation.
Descriptors: influenza A virus avian genetics, mutation,
chickens, hemagglutinins viral genetics, influenza A virus avian pathogenicity,
influenza A virus human genetics, RNA viral biosynthesis, recombination,
genetic, transcription, genetic, translation, genetic, vaccination, virus
replication.
Ghendon, Y.Z., S.G. Markushin, O.V. Blagovezhenskaya,
and D.B. Genkina (1975). Study of fowl plague virus RNA synthesis in
temperature-sensitive mutants. Virology 66(2): 454-63. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, chick embryo, DNA directed RNA polymerases metabolism,
dactinomycin pharmacology, electrophoresis, polyacrylamide gel, fibroblasts,
genetic complementation test, influenza A virus avian enzymology, mutation,
phenotype, temperature, tissue culture, transcription, genetic, uridine
metabolism, viral proteins biosynthesis.
Ghendon, Y.Z., S.G. Markushin, A.I. Klimov, and A.J.
Hay (1982). Studies of fowl plague virus temperature-sensitive mutants with
defects in transcription. Journal of General Virology 63(Pt. 1):
103-11. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Two fowl plague virus temperature-sensitive
(ts) mutants belonging to different complementation groups were studied. Both
were defective in the syntheses of unpolyadenylated complementary RNA
[A(-)cRNA] and virus RNA (vRNA) at non-permissive temperature whereas primary
transcription was unaffected. In addition, ts 29, in which the ts mutation is
in gene 1 coding for polypeptide P3, has a defect in 'secondary' synthesis of
mRNA at non-permissive temperature whereas inhibition of mRNA synthesis by ts
131, in which the ts mutation is in gene 2 coding for polypeptide P1, appeared
to result from a defect in vRNA synthesis. These results indicate, therefore,
that different enzymes are responsible for the syntheses of virus mRNAs and
A(-)cRNAs, which is consistent with the apparent differences in initiation and
termination of transcription in the two reactions. The patterns of synthesis of
the various types of virus RNA during infection are discussed.
Descriptors: genes viral, influenza A virus avian
genetics, transcription, genetic, cycloheximide pharmacology, influenza A virus
avian metabolism, mutation, RNA, messenger biosynthesis, RNA viral
biosynthesis, temperature, viral proteins genetics.
Ghendon, Y.Z., S.G. Markushin, A.I. Klimov, V.D.
Lotte, and V.P. Ginzburg (1983). Studies on a temperature-sensitive mutant
of fowl plague virus having a mutation in gene 7 coding for the M protein. Journal
of General Virology 64(Pt. 2): 291-304.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: A fowl plague virus (FPV)
temperature-sensitive mutant, ts 303/1 having a ts mutation in gene 7 coding
for the matrix (M) protein has been obtained. The mutant induced synthesis of
virus-specific RNA and polypeptides as well as ribonuclear protein (RNP)
formation in cells under non-permissive conditions; however, haemagglutinin
cleavage was reduced, functionally active haemagglutinin and neuraminidase were
absent and virions were not formed. In mutant-infected cells at 36 degrees C
haemagglutinin cleavage was also reduced and virions formed had an altered NP:M
ratio as well as a decreased haemagglutinin content. A population of virions
formed under these conditions was heterogeneous both in morphology and in
buoyant density. The data obtained suggest that a mutation in the M proteins of
orthomyxoviruses can affect processing of the haemagglutinin and impair final
stages of virion morphogenesis.
Descriptors: genes viral, genetic code, influenza A virus
avian genetics, viral proteins genetics,
genetic complementation test, hemagglutinins viral genetics, microscopy,
electron, mutation, neuraminidase genetics, RNA viral genetics, temperature,
viral matrix proteins, virion genetics.
Ghendon, Y.Z., S.G. Markushin, A.T. Marchenko, B.S.
Sitnikov, and V.P. Ginzburg (1973). Biochemical characteristics of fowl
plague virus TS mutants. Virology 55(2): 305-19. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian growth and
development, mutation, carbon radioisotopes, centrifugation, density gradient,
chick embryo, DNA directed RNA polymerases metabolism, electrophoresis,
polyacrylamide gel, genetic complementation test, hemagglutinins viral,
influenza A virus avian enzymology, influenza A virus avian immunology,
influenza A virus avian metabolism, neuraminidase biosynthesis, nucleoproteins
biosynthesis, peptide hydrolases
metabolism, peptide synthesis, protein precursors biosynthesis, RNA viral
biosynthesis, temperature, tissue culture, tritium, viral proteins
biosynthesis, virus replication.
Ghenkina, D.B. and Y.Z. Ghendon (1979). Recombination
and complementation between orthomyxoviruses under conditions of abortive
infection. Acta Virologica 23(2): 97-106. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: On interaction of ts mutants of fowl plague
virus (FPV) belonging to different complementation groups and human influenza A
viruses under conditions of abortive infection for both partners,
complementation was marked and recombinants occurred with a high frequency. The
level and degree of complementation as well as the frequency of recombinants
depended on the stage at which the reproduction of the human influenza A
viruses involved was blocked. On simultaneous inoculation of chicks with two
apathogenic ts mutants of FPV belonging to different complementation groups,
pathogenic ts+ recombinants appeared. On interaction of influenza B virus with
ts mutants of FPV or ultraviolet-irradiated FPV, neither complementation nor
recombination was observed. There was no complementation between influenza B
virus and ts mutants of FPV even at the level of the formation of
virus-specific substructures.
Descriptors: influenza A virus avian genetics, influenza A
virus human genetics, mutation, orthomyxoviridae genetics, recombination,
genetic, chick embryo, genetic
complementation test, influenza A virus avian growth and development, influenza
A virus avian pathogenicity, influenza A virus human growth and development,
tissue culture.
Giesendorf, B., F.X. Bosch, M. Orlich, C.
Scholtissek, and R. Rott (1986). Studies on the temperature sensitivity of
influenza A virus reassortants nonpathogenic for chicken. Virus Research
5(1): 27-42. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Influenza A virus reassortants which are
nonpathogenic for chickens are like mammalian influenza A viruses in that they
are temperature sensitive for growth at 41 degrees C. We have investigated the
mechanism of this temperature sensitivity using reassortants between the two
highly pathogenic strains A/FPV/Rostock/34 (FPV, H7N1) and A/turkey/England/63
(TE, H7N3). These reassortants show a strict correlation between the
pathogenicity for chickens and the constellation of the genes coding for the
ribonucleoprotein complex, RNP. Evidence is presented which shows that all
viral components are synthesized in sufficient amounts and that the block in
the viral replication cycle at the nonpermissive temperature is a late one
affecting virus maturation. It is suggested that the RNP, although still
enzymatically functional, may lose its ability to interact normally with viral
surface components, thus interfering with the process of virus maturation. Some
of the nonpathogenic reassortants which possessed the neuraminidase of TE
showed an interesting temperature-dependent phenomenon: the haemagglutinin
synthesized at the elevated temperature could only agglutinate erythrocytes at
20 degrees C, when the neuraminidase was inhibited or the infected cells
vigorously disrupted by ultrasonication. This phenomenon is possibly not
directly related to the temperature-sensitive block.
Descriptors: influenza A virus avian growth and
development, chick embryo, chickens microbiology, genes viral,
hemagglutination, viral, influenza A virus avian genetics, influenza A virus
avian pathogenicity, influenza A virus avian physiology, neuraminidase
metabolism, RNA viral biosynthesis, recombination, genetic, ribonucleoproteins
genetics, temperature, viral proteins
biosynthesis, virus replication.
Ginzburg, V.P. (1975). Metod polucheniia
monospetsificheskoi antisyvorotki k gemaggliutininu virusa chumy ptits [Method
for preparing monospecific antiserum to fowl plague virus hemagglutinins]. Voprosy
Virusologii (1): 100-2. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A simple method for preparation of
monospecific antiserum for the hemagglutinin of fowl plague virus has been
developed. It is based on selective inactivation of the enzymatic and antigenic
properties of neuraminidase by heating of the virus at 56 degrees for 3 hours
followed by disruption of the preparation with detergent and removal of the
inner proteins by ultracentrifugation. Immunization of animals with such
preparations produced antiserum containing considerable amounts of antibody for
the hemagglutinin in the absence of antibody for other proteins of fowl plague
virus.
Descriptors: hemagglutinins viral, immune sera,
immunologic techniques, influenza A virus avian immunology.
Ginzburg, V.P., S.G. Markushin, and Y.Z. Ghendon
(1982). Studies of biological properties of the recombinants between human
influenza and fowl plague viruses as related to genome composition. Acta
Virologica 26(6): 432-7. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Some biological properties of recombinants
obtained by crossing of fowl plague and human influenza viruses were studied.
The capacity of the recombinants to reproduce in chick embryo fibroblast
cultures was in reverse correlation to the number of genes coding for P
proteins derived from the human influenza virus. The genome composition was of
importance for the expression of ts-phenotype of the recombinants in different
systems. Substitution of at least one gene in the fowl plague virus genome by a
corresponding human influenza virus gene resulted in the decrease of virulence
for 1-day-old chickens. The presence of three P genes from human influenza
virus genome in the genome of the recombinant proved to be insufficient for the
capability of the recombinant to reproduce in organ cultures of human origin.
Descriptors: genes viral, influenza A virus avian
genetics, influenza A virus human genetics, recombination, genetic, cultured
cells, chick embryo, chickens, influenza A virus avian pathogenicity, influenza
A virus avian physiology, influenza A virus human pathogenicity, influenza A
virus human physiology, nasal polyps microbiology, organ culture, plaque assay,
temperature, virus replication.
Ginzburg, V.P., E.E. Rosina, O.K. Sharova, and Y.Z.
Ghendon (1982). The replication of influenza A viruses in organ cultures of
human nasal polyps. Archives of Virology 74(4): 293-8. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Organ cultures of human nasal polyps were
shown to support the replication of five out of seven human influenza A viruses
and three out of six avian strains with varying degrees of efficiency. The
ability to replicate was independent of the antigenic formula of the virus. The
structure of nasal polyps closely resembled that of normal nasal mucosa and
infection with influenza A virus resulted in histological changes analogous to
those seen in natural infections. This system provides an in vitro method for
more detailed studies of influenza A virus and possibly other respiratory virus
infections of man.
Descriptors: influenza microbiology, influenza A virus
physiology, nasal polyps microbiology, virus replication, influenza A virus
avian physiology, influenza A virus human physiology, organ culture, species
specificity.
Ginzburg, V.P., E.E. Rozina, O.K. Sharova, and Y.U.Z.
Ghendon (1985). Reproduction of human and animal influenza viruses in human
nasal polyp organ cultures. Acta Virologica 29(5): 424-7. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Human influenza virus strains were easily
grown and passaged in human nasal polyp organ cultures causing marked damage of
the epithelium. Unlike to human strains, the animal influenza virus strain could
be propagated for no longer than 2 or 3 passages and even the 1st passage
failed to cause significant morphological changes of the epithelium cells.
Descriptors: influenza A virus avian growth and
development, influenza A virus human growth and development, influenza A virus
growth and development, nasal polyps microbiology, DNA replication, deer,
influenza A virus genetics, nasal polyps pathology, organ culture, species
specificity, virus replication.
Gitel'man, A.K., V.B. Martynenko, E.V. Molibog, N.K.
Vorkunova, and A.G. Bukrinskaia (1976). Abortivnaia infektsiia virusa grippa
v kletkakh astsitnogo raka Erlikha. Dal'neishee izuchenie svoistv astsitnogo
virusa [Abortive influenza virus infection in Ehrlich ascitic cancer cells.
Further studies of the properties of ascitic virus]. Voprosy Virusologii
(6): 713-21. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Non-infectious virus particles produced by
influenza virus (classical fowl plague)-infected Ehrlich ascitic carcinoma
cells have the same morphology, size and sedimentation rate as the standard
virions. Their main difference from the allantoic virus is their extreme
fragility. They remain intact upon a short-term centrifugation in sucrose
solutions but desintegrate upon prolonged centrifugation. In isopicnic
fractionation they are detected in two forms, with a density of 1.23 g/ml
retaining the hemagglutinating but not the neuraminidase activity and with a
density of 1.27 g/ml deprived of both hemagglutinating and neuraminidase activity.
In the electron microscopic examination the 1.23 g/ml structure appears as
virus particles with defective areas in the surface spikes layer whereas the
1.27 g/ml structure has no spike layer at all. The protein analysis by
polyacryl amide gel electrophoresis revealed a sharply reduced amount of the
membrane protein in the ascitic virus. A hypothesis is suggested according to
which the reduced amount of the membrane protein is the cause of the unusual
fragility of ascitic virus particle membranes as a result of which they readily
lose glycoproteins which, in its turn, leads to their reduced infectious
activity.
Descriptors: carcinoma, Ehrlich tumor microbiology,
influenza A virus avian isolation and purification, influenza A virus avian
metabolism, cultured cells, centrifugation, centrifugation, density gradient,
centrifugation, isopycnic, hemagglutinins viral analysis, microscopy, electron,
neuraminidase metabolism, viral proteins analysis.
Gitelman, A.K. and A.G. Bukrinskaya (1971). A comparison of influenza and parainfluenza
and RNP properties. Archiv Fur Die Gesamte Virusforschung 34(2):
89-95. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian analysis,
nucleoproteins analysis, parainfluenza virus 1, human analysis, buffers, carbon
isotopes, centrifugation, density gradient, cesium, chick embryo, chlorides,
hemagglutination tests, influenza A virus avian isolation and purification,
nucleoproteins isolation and purification, parainfluenza virus 1, human
isolation and purification, phosphates, phosphorus isotopes, precipitation,
RNA, viral, species specificity, sucrose, surface active agents,
trichloroacetic acid, virus cultivation.
Gitelman, A.K., A.V. Isachenko, and A.G. Bukrinskaya
(1973). Sedimentation and buoyant density characteristics of influenza virus
ribonucleoprotein. Acta Virologica 17(3): 257-60. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: nucleoproteins analysis, orthomyxoviridae
analysis, viral proteins analysis, centrifugation, density gradient, cesium,
chick embryo, chlorides, influenza A virus avian analysis, nucleoproteins
isolation and purification, phosphorus isotopes, sucrose, tissue culture,
tritium, viral proteins isolation and purification, virus cultivation.
Glathe, H., H.U. Strittmatter, M. Kunze, and H.
Sinnecker (1982). Uber den Einfluss niedriger pH-Werte auf die Infektiositat
und Neuraminidaseaktivitat menschlicher und tierischer Stamme des
Influenzavirus Typ A. [Effect of low pH values on the infectivity and neuraminidase
activity of human and animal strains of influenza virus type A]. Acta
Biologica Et Medica Germanica 41(11): 1075-8. ISSN: 0001-5318.
NAL
Call Number: QH301.A25
Abstract: The influence of acidic pH on the infectivity
and neuraminidase activity of human, equine and avian type A influenza virus
strains has been studied. Following exposure to pH 3 human and equine strains
lost their infectivity completely, whereas all investigated strains of the
subtypes Hav6N2 and Hav7Neq2 retained a certain amount of infectivity. In
contrast to human and equine strains the avian strains retained also 38% of
their original neuraminidase activity after acidic treatment. Partial retention
of infectivity and the relative stability of the neuraminidase following exposure
to acidic pH are supposed to be linked together in avian influenza virus
strains implicating neuraminidases for their ability to prevent the aggregation
of virions.
Descriptors: influenza A virus human enzymology, influenza
A virus enzymology, neuraminidase metabolism, hydrogen-ion concentration,
influenza A virus avian enzymology, influenza A virus human pathogenicity,
influenza A virus pathogenicity.
Goetschy, J.F., H. Zeller, J. Content, and M.A.
Horisberger (1989). Regulation of the interferon-inducible IFI-78K gene, the
human equivalent of the murine Mx gene, by interferons, double-stranded RNA,
certain cytokines, and viruses. Journal of Virology 63(6):
2616-22. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The interferon-inducible gene (IFI-78K gene)
that codes for a human protein, p78, of 78,000 Mr is the equivalent of the
mouse Mx gene encoding Mx protein. The IFI-78K gene is located on chromosome 21
together with the alpha/beta interferon (IFN-alpha/beta) receptor. The p78
protein is important since it may be involved in resistance to influenza
viruses. The regulation of the IFI-78K gene was studied in human diploid cells
by using a cDNA probe to p78 mRNA and specific monoclonal antibodies to p78
protein. The IFI-78K gene, a normally quiescent gene, is transcriptionally
regulated by IFN-alpha, and its induction does not require protein synthesis.
The rate of transcription measured in a run-on assay increased rapidly but
transiently. The level of p78 mRNA increased up to 8 h, declining slowly
afterwards. The p78 protein, undetectable in untreated cells, accumulated up to
16 h, and its amount remained stable for at least 36 h after the addition of
IFN-alpha. Cytokines such as tumor necrosis factor, interleukin-1 alpha, and
interleukin-1 beta activated the IFI-78K gene at concentrations comparable to
that of IFN-alpha. However, gene activation by these cytokines required protein
synthesis. Poly(rI)-poly(rC) induced the IFI-78K gene directly at the
transcriptional level without requirement for protein synthesis. Newcastle
disease virus, influenza virus, and to a lesser extent vesicular stomatitis
virus also induced the IFI-78K gene in the absence of any protein synthesis.
Induction of transcription by viruses was markedly enhanced by pretreatment of
cells with IFN-gamma (which by itself is a poor inducer of the IFI-78K gene),
resulting in accumulation of p78 protein during the course of infection; this
suggests that IFN-gamma programs cells to full antiviral activity upon virus
infection.
Descriptors: chromosomes, human, pair 21, GTP binding
proteins, gene expression regulation, proteins genetics, blotting, northern,
blotting, western, influenza A virus avian physiology, interferon type I,
recombinant pharmacology, interferon gamma, recombinant pharmacology,
interleukin 1 pharmacology, Newcastle disease virus physiology, RNA, double
stranded pharmacology, recombinant proteins pharmacology, transcription,
genetic, translation, genetic, tumor necrosis factor pharmacology, vesicular
stomatitis Indiana virus physiology.
Goncharskaia, T.I.A. (1978). Eksperimental'noe
izuchenie protivovirusnykh svoistv antibiotika
6734-21. [Experimental study of the antiviral properties of antibiotic
6734-21]. Antibiotiki 23(1):
58-62. ISSN: 0003-5637.
NAL
Call Number: 396.8 An84
Abstract: The effect of antibiotic 6734-21 on the
viruses of variolovaccine, Herpes simplex, influenza and classical avian plague
was studied on various experimental models. Antibiotic 6734-21 inhibited
development of the variolovaccine virus in the tissue culture, in chick
embryos, in rabbits with variolovaccine infection, as well as the development
of the viruses of Herpes simplex, Aueski, and Newcastle diseases in the tissue
culture. It had a virulicidic effect on the viruses of variolovaccine,
influenza and classical avian plague.
Descriptors: anti bacterial agents pharmacology, antiviral
agents, anti bacterial agents therapeutic use, chick embryo, herpes simplex
drug therapy, herpesvirus 1, suid drug effects, influenza A virus avian drug
effects, influenza A virus drug effects, mice, Newcastle disease virus drug
effects, rabbits, simplexvirus drug effects, smallpox drug therapy, variola
virus drug effects.
Goncharskaia, T.I.A., S.M. Navashin, S.L.
Grokhovskii, and A.L. Zhuze (1977). Izuchenie protivovirusnykh svoistv
analogov distamitsina A. [Antiviral properties of analogs of distamycin A].
Antibiotiki 22(11):
998-1002. ISSN: 0003-5637.
NAL
Call Number: 396.8 An84
Abstract: The effect of 9 analogues of distamycin A was
studied in a tissue culture with respect to the virus of a smallpox vaccine and
classical avian plague. Three analogues of distamycin A (I, VI, VII) were
studied in chick embryos with respect to the smallpox and influenza viruses.
The analogues were characterized by a loss or decrease of the activity against
the smallpox vaccine virus as compared to distamycin A. In contrast to
distamycin A analogue VII had an inhibitory effect on influenza infection in
chick embryos.
Descriptors: antiviral agents, distamycins pharmacology,
influenza A virus avian drug effects, orthomyxoviridae drug effects, pyrroles
pharmacology, variola virus drug effects.
Gonzalez Salazar, V.D., A. Hernandez Magdaleno, J.I. Monroy Basilio,
H. Rodriguez Velazco, and J. Garcia Garcia. (1996). Avances sobre la
distribucion de la replicacion de diferentes cepas del virus de la influenza
aviar en embrion de pollo y aves por histopatologia e inmunohistoquimica.
[Distribution of avian influenza virus in chickens and chick embryos by histopathology
and immunihistochemistry]. In: Reunion Nacional de Investigacion
Pecuaria, Cuernavaca, Morelos, (Mexico), p. 136.
Abstract: El objetivo fue analizar mediante
histopatologia e inmunohistoquimica (IH), el tipo de lesiones y el patron de
infectividad que producen en el embrion de pollo y aves al inocular los
aislamientos del virus de influenza aviar (IA), provenientes de diferentes
zonas del pais. Como cepas de IA de alta patogenicidad, se utilizaron los
aislamientos Queretaro y Puebla y como cepa de baja patogenicidad, la cepa
vacunal.
Descriptors: avian influenza virus, infection,
histopathology, disease transmission, influenza virus, orthomyxoviridae,
pathogenesis, pathology, viruses.
Gorman, O.T., W.J. Bean, Y. Kawaoka, and R.G. Webster
(1990). Evolution of the nucleoprotein gene of influenza A virus. Journal
of Virology 64(4): 1487-97. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Nucleotide sequences of 24 nucleoprotein (NP)
genes isolated from a wide range of hosts, geographic regions, and influenza A
virus serotypes and 18 published NP gene sequences were analyzed to determine
evolutionary relationships. The phylogeny of NP genes was determined by a
maximum-parsimony analysis of nucleotide sequences. Phylogenetic analysis
showed that NP genes have evolved into five host-specific lineages, including
(i) Equine/Prague/56 (EQPR56), (ii) recent equine strains, (iii) classic swine
(H1N1 swine, e.g., A/Swine/Iowa/15/30) and human strains, (iv) gull H13
viruses, and (v) avian strains (including North American, Australian, and Old
World subgroups). These NP lineages match the five RNA hybridization groups
identified by W. J. Bean (Virology 133:438-442, 1984). Maximum nucleotide
differences among the NPs was 18.5%, but maximum amino acid differences reached
only 10.8%, reflecting the conservative nature of the NP protein. Evolutionary
rates varied among lineages; the human lineage showed the highest rate (2.54
nucleotide changes per year), followed by the Old World avian lineage (2.17
changes per year) and the recent equine lineage (1.22 changes per year). The
per-nucleotide rates of human and avian NP gene evolution (1.62 x 10(-3) to
1.39 x 10(-3) changes per year) are lower than that reported for human NS genes
(2.0 x 10(-3) changes per year; D. A. Buonagurio, S. Nakada, J. D. Parvin, M.
Krystal, P. Palese, and W. M. Fitch, Science 232:980-982, 1986). Of the five NP
lineages, the human lineage showed the greatest evolution at the amino acid
level; over a period of 50 years, human NPs have accumulated 39 amino acid
changes. In contrast, the avian lineage showed remarkable conservatism; over
the same period, avian NP proteins changed by 0 to 10 amino acids. The
specificity of the H13 NP in gulls and its distinct evolutionary separation
from the classic avian lineage suggests that H13 NPs may have a large degree of
adaptation to gulls. The presence of avian and human NPs in some swine isolates
demonstrates the susceptibility of swine to different virus strains and
supports the hypothesis that swine may serve as intermediates for the
introduction of avian influenza virus genes into the human virus gene pool.
EQPR56 is relatively distantly related to all other NP lineages, which suggests
that this NP is rooted closest to the ancestor of all contemporary NPs. On the
basis of estimation of evolutionary rates from nucleotide branch distances,
current NP lineages are at least 100 years old, and the EQPR56 NP is much
older.(ABSTRACT TRUNCATED AT 400 WORDS)
Descriptors: evolution, genes viral, influenza A virus
genetics, nucleoproteins genetics, viral proteins genetics, adaptation,
biological, amino acid sequence, base sequence, cloning, molecular, DNA, viral
analysis, influenza A virus classification, molecular sequence data, phylogeny,
software, species specificity.
Goto, H. (2004). [Novel function of
plasminogen-binding activity of the NA determines the pathogenicity of
influenza A virus]. Uirusu Journal of Virology 54(1): 83-91. ISSN: 0042-6857.
Abstract: Because cleavage of the hemagglutinin (HA) molecule
by proteases is a prerequisite for infectivity of influenza A viruses, this
molecule is a major determinant of viral pathogenicity. Although well
documented in the pathogenicity of avian influenza viruses, the role of HA
cleavage in the pathogenicity of mammalian viruses is not well understood.
Therefore, we studied a mouse-adapted human isolate A/WSN/33 (WSN), a
neurovirulent influenza virus strain that causes systemic infection when
inoculated intranasally into mice. We found a novel mechanism of HA cleavage
for WSN virus: the neuraminidase (NA) of WSN virus binds and sequesters
plasminogen on the cell surface, leading to enhanced cleavage of the HA. The
structural basis of this novel function of the NA molecule appears to be the
presence of a carboxyl-terminal lysine and the absence of an oligosaccharide
side chain at position 146. To obtain direct evidence that the
plasminogen-binding activity of the NA enhances the pathogenicity of WSN virus,
we generated mutant viruses that are deficient in plasminogen-binding activity
by reverse genetics. The mutant viruses showed attenuated growth in mice and
failed to grow at all in the brains of these animals. Therefore, we concluded
that the novel function of plasminogen-binding activity of the NA determines
the pathogenicity of WSN virus in mice.
Descriptors: influenza A virus enzymology, influenza A
virus pathogenicity, neuraminidase metabolism, plasminogen metabolism,
virulence, hemagglutinins metabolism, mice, neuraminidase chemistry, protein
binding.
Govorkova, E.A., A.S. Gambaryan, E.C. Claas, and Y.A.
Smirnov (2000). Amino acid changes in the hemagglutinin and matrix proteins
of influenza a (H2) viruses adapted to mice. Acta Virologica 44(5):
241-8. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Mouse-adapted (MA) variants of human and
avian influenza A (H2) viruses were generated and characterized with respect to
acquisition of virulence in mice. From the nucleotide sequence the amino acid
sequence was deduced. The HA1 subunit of the hemagglutinin (HA) contained three
amino acid substitutions in the A/black duck/New Jersey/1580/78-MA variant
(Glu216-->Asp, Lys307-->Arg, and Thr318-->Ile) and two substitutions
in the A/JapanxBellamy/57-MA variant (Lys25-->Thr and Ser203-->Phe). In
the M1 protein, there were two substitutions in the A/black duck/New
Jersey/1580/78-MA variant (Asn30-->Asp and Gln214-->His) and a single
substitution in the A/JapanxBellamy/57-MA variant (Met179-->Lys). The M2
protein amino acid sequences of the parental virus and the MA variants differed
by a single identical mutation (Asn93-->Ser). The localization and atomic
distances of the observed mutations on the three-dimensional (3D) structure of
the HA protein were analyzed for influenza H2 viruses. The obtained results were
similar to those published earlier on H1, H3 and H5 subtypes. The amino acid
changes in the HA protein could be divided into two groups. In one group the
substitutions were situated at the top of the molecule, while in the other
group they were clustered in the stem area at the interface region between
three HA monomers. The analysis revealed that the substitutions observed in the
MA variants probably increase the flexibility of the HA molecule and/or weaken
the interactions between monomers or subunits in the HA trimer. The
relationships of the observed amino acid changes in the HA and M proteins to
the biological properties of the respective viruses and possible mechanisms
involved in the acquisition of viral virulence are discussed.
Descriptors: bacterial outer membrane proteins,
hemagglutinin glycoproteins, influenza virus genetics, influenza A virus avian
genetics, influenza A virus human genetics, viral matrix proteins genetics,
amino acid substitution, bacterial proteins chemistry, bacterial proteins
genetics, birds, carrier proteins chemistry, carrier proteins genetics, cell
line, chick embryo, hemagglutinin glycoproteins, influenza virus chemistry,
influenza A virus avian pathogenicity, influenza A virus human pathogenicity,
lung virology, mice, viral matrix proteins chemistry.
Govorkova, E.A., V.M. Kibardin, A.A. Kizina, G.M.
Nazarova, and I.U.A. Smirnov (1991). Vzaimosviazi virusov grippa A(H2)
cheloveka i ptits, opredeliaemye matematicheskoi obrabotkoi dannykh ob
antigennoi strukture gemagglutinina. [The interrelations of the human and avian
influenza viruses A(H2) determined by the mathematical processing of data on
the antigenic structure of their hemagglutinin]. Voprosy Virusologii
36(6): 463-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Mathematical methods were used to analyse the
data on the antigenic specificity of H2 subtype hemagglutinin of human and
avian influenza A viruses. This approach allowed the evaluation of possible
evolutional relationships in this little-studied group of viruses. Influenza A
(H2) viruses isolated from birds in the USA were found to represent a
sufficiently isolated group, whereas European avian strains
(A/duck/Germany/1215/73, A/pintail duck/Primor'e/695/76, A/duck/Marseilles/46/76)
were close to "human" viruses. The A/Leningrad/1468/65, A/laughing
gull/New Jersey/75/85, and A/pintail duck/Alberta/2728/77 strains represent
marked antigenic variants apparently rather far gone as a result of
hemagglutinin drift.
Descriptors: antigens, viral immunology, hemagglutinins
viral immunology, influenza A virus avian immunology, influenza A virus human
immunology, algorithms, antigenic variation immunology, antigens, viral
classification, cluster analysis, ducks microbiology, evolution, hemagglutinins
viral classification, influenza A virus avian classification, influenza A virus
human classification.
Govorkova, E.A., J.E. Rehg, S. Krauss, H.L. Yen, Y.
Guan, M. Peiris, T.D. Nguyen, T.H. Hanh, P. Puthavathana, H.T. Long, C.
Buranathai, W. Lim, R.G. Webster, and E. Hoffmann ( 2005). Lethality to
ferrets of H5N1 influenza viruses isolated from humans and poultry in 2004.
Journal of Virology 79(4): 2191-8.
ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The 2004 outbreaks of H5N1 influenza viruses
in Vietnam and Thailand were highly lethal to humans and to poultry; therefore,
newly emerging avian influenza A viruses pose a continued threat, not only to
avian species but also to humans. We studied the pathogenicity of four human
and nine avian H5N1/04 influenza viruses in ferrets (an excellent model for
influenza studies). All four human isolates were fatal to intranasally
inoculated ferrets. The human isolate A/Vietnam/1203/04 (H5N1) was the most
pathogenic isolate; the severity of disease was associated with a broad tissue
tropism and high virus titers in multiple organs, including the brain. High
fever, weight loss, anorexia, extreme lethargy, and diarrhea were observed. Two
avian H5N1/04 isolates were as pathogenic as the human viruses, causing lethal
systemic infections in ferrets. Seven of nine H5N1/04 viruses isolated from
avian species caused mild infections, with virus replication restricted to the
upper respiratory tract. All chicken isolates were nonlethal to ferrets. A
sequence analysis revealed polybasic amino acids in the hemagglutinin
connecting peptides of all H5N1/04 viruses, indicating that multiple molecular
differences in other genes are important for a high level of virulence.
Interestingly, the human A/Vietnam/1203/04 isolate had a lysine substitution at
position 627 of PB2 and had one to eight amino acid changes in all gene
products except that of the M1 gene, unlike the A/chicken/Vietnam/C58/04 and
A/quail/Vietnam/36/04 viruses. Our results indicate that viruses that are lethal
to mammals are circulating among birds in Asia and suggest that pathogenicity
in ferrets, and perhaps humans, reflects a complex combination of different
residues rather than a single amino acid difference.
Descriptors: influenza virus infection, respiratory system
disease, viral disease complications, etiology, mortality, pathology,
transmission, Vietnam, Thailand, ferrets, chickens, humans.
Govorkova, E.A. and Y.U.A. Smirnov (1997). Cross-protection
of mice immunized with different influenza A (H2) strains and challenged with
viruses of the same HA subtype. Acta Virologica 41(5): 251-7. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Cross-protection of mice immunized with
inactivated preparations of human and avian influenza A (H2) viruses was
determined after lethal infection with mouse-adapted (MA) variants of human
A/Jap x Bell/57 (H2N1) and avian A/NJers/78 (H2N3) viruses. The MA variants
differed from the original strains by acquired virulence for mice and changes
in the HA antigenicity. These studies indicated that mice vaccinated with human
influenza A (H2) viruses were satisfactorily protected against challenge with
A/Jap x Bell/57-MA variant; the survival rate was in the range of 61%-88.9%.
Immunization of mice with the same viral preparations provided lower levels of
protection against challenge with A/NJers/78-MA variant. Vaccination of mice
with the avian influenza A (H2) viruses induced better protection than with
human strains against challenge with both MA variants. Challenge with
A/NJers/78-MA variant revealed that 76.2%-95.2% of animals were protected when
vaccinated with avian influenza virus strains isolated before 1980, and that
the protection reached only 52.4%-60.0% in animals vaccinated with strains
isolated in 1980-1985. The present study revealed that cross-protection
experiments in a mouse model could provide necessary information for the
development of appropriate influenza A (H2) virus vaccines with a potential for
these viruses to reappear in a human population.
Descriptors: influenza prevention and control, influenza A
virus avian immunology, influenza A virus human immunology, influenza vaccine
immunology, cross reactions, disease models, animal, influenza mortality,
influenza A virus avian classification, influenza A virus avian pathogenicity,
influenza A virus human classification, influenza A virus human pathogenicity,
mice, vaccination, vaccines, attenuated immunology.
Grambas, S., M.S. Bennett, and A.J. Hay (1992). Influence
of amantadine resistance mutations on the pH regulatory function of the M2
protein of influenza A viruses. Virology 191(2): 541-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Mutations in the influenza M2 membrane
protein which confer resistance to the antiviral drug amantadine are
exclusively located within the transmembrane region of the molecule. The
influence of specific amino acid substitutions on the activity of the M2
protein in influenza A virus-infected cells is assessed in this report by their
effects upon haemagglutinin (HA) stability and virus growth. A number of amino
acid substitutions, e.g., L26H, A30T, S31N and G34E reduced the activity of the
M2 protein of A/chicken/Germany/34 (Rostock) and caused a substantial increase
in expression of the low-pH form of HA. The adverse effects of the mutations on
virus replication were evident from changes selected during subsequent passage
of the mutant viruses in the presence or absence of amantadine: reversion to
wt, the acquisition of a second suppressor mutation in M2, or the appearance of
a complementary mutation in HA which increased its pH stability. In contrast,
127T and 127S, mutations which were most readily selected following passage of
the wt virus in the presence of drug, caused an increase in M2 activity.
Furthermore, in double mutants the 127T mutation suppressed the attenuating
effects of the A30T and S31N mutations on M2 activity. The influence of primary
structure on the consequences of particular amino acid changes was further
emphasized by the contrasting effects of the G34E mutation on the activities of
two closely related proteins, causing an increase in the activity of the M2 of
A/chicken/Germany/27 (Weybridge) as opposed to the decrease in activity of the
Rostock protein. Estimates of differences in trans Golgi pH based on the degree
of conversion of HA to the low-pH form, or complementation of differences in pH
stability of mutant HAs, indicate that changes in M2 may influence pH within
the transport pathway by as much as 0.6. The results thus provide further
evidence that M2 regulates transmembrane pH gradients in the trans Golgi.
Incompatibility between particular HA and M2 components and the selection of M2
mutants with suboptimal activity stresses the essential relationship between
the structures and functions of these two virus proteins.
Descriptors: amantadine pharmacology, influenza A virus
avian metabolism, viral matrix proteins drug effects, viral matrix proteins
genetics, water electrolyte balance genetics, amino acid sequence, drug
resistance, microbial, genetic complementation test, hemagglutinins viral
biosynthesis, hydrogen-ion concentration, influenza A virus avian growth and
development, molecular sequence data, mutagenesis, mutation, structure activity
relationship, variation genetics.
Gribkova, N.V., N.V. Kaverin, I.V. Tsvetkova, and
M.A. Lipkind (1973). Occurence of unstability of hemagglutinin and
neuraminidase in cells infected with different myxoviruses. Archiv Fur Die
Gesamte Virusforschung 43(1): 98-102.
ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: hemagglutinins viral, influenza A virus avian
immunology, neuraminidase metabolism, Newcastle disease virus enzymology,
Newcastle disease virus immunology, orthomyxoviridae immunology, chick embryo,
cycloheximide pharmacology, drug stability, fetal membranes, influenza A virus
avian enzymology, influenza A virus avian growth and development, Newcastle
disease virus growth and development, orthomyxoviridae enzymology,
orthomyxoviridae growth and development, tissue culture.
Gribkova, N.V., N.F. Kazak, and V.I. Votyakov (1984).
Development of resistance to 2-(1-amino-ethyl)-bicyclo (2.2.1) heptane
chlorohydrate in influenza A virus. Acta Virologica 28(1): 69-72. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: A resistant influenza virus has been obtained
during successive passages of influenza A virus in 10 to 11-day-old chick
embryos (CE) in the presence of 2-(1'-amino-ethyl)-bicyclo(2.2.1) heptane
chlorohydrate possessing a high antiviral activity. The virus resistance to the
inhibitor was not lost after one passage in the absence of the drug.
Descriptors: antiviral agents pharmacology, influenza A
virus avian drug effects, norbornanes pharmacology, drug resistance, microbial,
virus replication drug effects.
Grinev, A.A., N.A. Petrov, S.I.A. Golovin, L.V.
Mamaev, and T.P. Mikriukova (1988). Pervichnaia struktura polnorazmernoi
DNK-kopii gena neiraminidazy antigennogo podtipa N7 virusa grippa ptits.
[Primary structure of the full-length DNA copy of the neuraminidase gene in the
avian influenza virus of the N7 antigenic subtype]. Bioorganicheskaia
Khimiia 14(3): 416-8. ISSN:
0132-3423.
NAL
Call Number: QD415.A1S62
Abstract: Complete nucleotide sequence of the cloned
full-length DNA copy of the influenza virus A/FPV Weybridge (H7N7)
neuraminidase gene has been determined.
Descriptors: base sequence, DNA, viral genetics, genes
viral, influenza A virus avian genetics, neuraminidase genetics, sequence
homology, nucleic acid, antigens, viral analysis, cloning, molecular, DNA
genetics, influenza A virus avian classification, influenza A virus avian
enzymology, molecular sequence data.
Guan, Y., K.F. Shortridge, S. Krauss, P.S. Chin, K.C.
Dyrting, T.M. Ellis, R.G. Webster, and M. Peiris (2000). H9N2 influenza
viruses possessing H5N1-like internal genomes continue to circulate in poultry
in southeastern China. Journal of Virology 74(20): 9372-80. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The transmission of H9N2 influenza viruses to
humans and the realization that the A/Hong Kong/156/97-like (H5N1) (abbreviated
HK/156/97) genome complex may be present in H9N2 viruses in southeastern China
necessitated a study of the distribution and characterization of H9N2 viruses
in poultry in the Hong Kong SAR in 1999. Serological studies indicated that
H9N2 influenza viruses had infected a high proportion of chickens and other
land-based birds (pigeon, pheasant, quail, guinea fowl, and chukka) from southeastern
China. Two lineages of H9N2 influenza viruses present in the live-poultry
markets were represented by A/Quail/Hong Kong/G1/97 (Qa/HK/G1/97)-like and
A/Duck/Hong Kong/Y280/97 (Dk/HK/Y280/97)-like viruses. Up to 16% of cages of
quail in the poultry markets contained Qa/HK/G1/97-like viruses, while about 5%
of cages of other land-based birds were infected with Dk/HK/Y280/97-like
viruses. No reassortant between the two H9N2 virus lineages was detected
despite their cocirculation in the poultry markets. Reassortant viruses
represented by A/Chicken/Hong Kong/G9/97 (H9N2) were the major H9N2 influenza
viruses circulating in the Hong Kong markets in 1997 but have not been detected
since the chicken slaughter in 1997. The Qa/HK/G1/97-like viruses were frequently
isolated from quail, while Dk/HK/Y280/97-like viruses were predominately
associated with chickens. The Qa/HK/G1/97-like viruses were evolving relatively
rapidly, especially in their PB2, HA, NP, and NA genes, suggesting that they
are in the process of adapting to a new host. Experimental studies showed that
both H9N2 lineages were primarily spread by the aerosol route and that neither
quail nor chickens showed evidence of disease. The high prevalence of quail
infected with Qa/HK/G1/97-like virus that contains six gene segments
genetically highly related to HK/156/97 (H5N1) virus emphasizes the need for
surveillance of mammals including humans.
Descriptors: genome, viral, influenza A virus avian
isolation and purification, poultry virology, China, hemagglutination
inhibition tests, influenza A virus avian genetics, phylogeny, temperature,
virus replication.
Gubareva, L.V., R. Bethell, G.J. Hart, K.G. Murti,
C.R. Penn, and R.G. Webster (1996). Characterization of mutants of influenza
A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en. Journal
of Virology 70(3): 1818-27. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: The development of viral resistance to the
neuraminidase (NA) inhibitor, 4-guanidino-Neu5Ac2en, of influenza viruses was
studied by serial passage of A/Turkey/Minnesota/833/80 (H4N2) in Madin-Darby
canine kidney cells in the presence of increasing concentrations of inhibitor.
Resistant mutants selected after eight passages, had a 10,000-fold reduction in
sensitivity to the inhibitor in plaque assays, but their affinity (1/Kd) to the
inhibitor was similar to that of the parental virus. Electron microscopic
analysis revealed aggregation of the mutant virus at the cell surface in the
presence of the inhibitor. Sequence analysis established that a substitution
had occurred in the NA (Arg-249 to Lys) and in the HA2 subunit of the
hemagglutinin (Gly-75 to Glu), in the vicinity of the proposed second sialic
acid binding site. The change of residue 249 appears to be a chance mutation,
for we were unable to reisolate this mutant, whereas subsequent experiments
indicate changes in the hemagglutinin. After 13 passages of the parental virus,
mutants that were resistant to the high concentrations of inhibitor tested were
obtained. These viruses retained their drug-resistant phenotype even after five
passages without the inhibitor. Electron microscopic analysis revealed no
aggregation of virus on the surface of infected cells in the presence of the
inhibitor. Sequence analysis of the NA gene from these drug-resistant mutants
revealed an additional substitution of Glu to Ala at the conserved amino acid
residue 119. This substitution is responsible for reducing the affinity of the
inhibitor to the NA. Our findings suggest that the emergence of mutants
resistant to 4-guanidine-Neu5Ac2en is a multistep process requiring prolonged
exposure to the inhibitor.
Descriptors: antiviral agents pharmacology, enzyme
inhibitors pharmacology, influenza A virus avian drug effects, mutation,
neuraminidase antagonists and inhibitors, sialic acids pharmacology, base
sequence, cell line, DNA, viral, dogs, drug resistance, microbial genetics,
influenza A virus avian enzymology, influenza A virus avian genetics, influenza
A virus avian ultrastructure, molecular sequence data, neuraminidase chemistry,
turkeys virology.
Gubareva, L.V., J.A. McCullers, R.C. Bethell, and
R.G. Webster (1998). Characterization of influenza A/HongKong/156/97 (H5N1)
virus in a mouse model and protective effect of zanamivir on H5N1 infection in
mice. Journal of Infectious Diseases 178(6): 1592-6. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: A recent outbreak of influenza in Hong Kong
was caused by a highly virulent virus of avian origin. Concern that the
appearance of such a virus in the human population may be a harbinger of a new
pandemic has brought increased attention to the issue of antivirals available
for treatment of influenza. A/HongKong/156/97 (H5N1), the first virus of H5N1
subtype isolated from a human host, is highly virulent in the mouse model and
can infect mouse lungs without requiring adaptation. High mortality and
evidence of systemic disease, including spread to the brain after intranasal
inoculation, are observed. Zanamivir, a novel neuraminidase inhibitor, is
effective at decreasing replication of the virus in vitro. In a model of lethal
challenge in mice, Zanamivir reduces lung titers of the virus and decreases
morbidity and mortality.
Descriptors: antiviral agents therapeutic use, influenza
prevention and control, influenza A virus avian physiology, sialic acids
therapeutic use, chick embryo, Hong Kong, influenza physiopathology, influenza
A virus avian drug effects, influenza A virus avian isolation and purification,
influenza A virus avian pathogenicity, influenza A virus human, lung virology,
mice, mice inbred BALB c, organ specificity, virulence, virus replication drug
effects.
Gubareva, L.V., C.R. Penn, and R.G. Webster (1995). Inhibition
of replication of avian influenza viruses by the neuraminidase inhibitor
4-guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid. Virology
212(2): 323-330. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The sialidase inhibitor
4-guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic
acid(4-guanidino-Neu5Ac2en), designed with computer assistance and knowledge of
the crystal structure of influenza virus neuraminidase, has shown antiviral
effects in animal models of human influenza (M. von Itzstein et al., Nature,
363, 418-423, 1993). Here we demonstrate that the compound efficiently inhibits
the enzyme activity of all nine subtypes of avian influenza A neuraminidase in
vitro. When administered intranasally to chickens infected with lethal viruses,
high doses of the compound (1000 microgram/kg) protected 85% of birds harboring
A/Chick/Victoria/1/85 (H7N7), a fowl plague virus, but not chickens infected
with other highly virulent viruses of the N1, N2, or N3 subtype. This
differential inhibitory effect was also seen in a plaque reduction assay with
Madin-Darby canine kidney cells (MDCK), where 4-guanidino-Neu5Ac2en was more
effective against A/Chick/Vic/85 (H7N7) than A/FPV/Rostock/34 (H7N1). In
contrast to the substantial plaque reduction observed in MDCK cells, the drug
failed to inhibit plaque formation in chicken embryo fibroblasts infected with
either A/Chick/Vic/85 or A/FPV/Rostock/34, regardless of its concentration. The
different levels of drug efficacy seen in two cell systems most likely reflect
the location of virus budding and release in polarized versus nonpolarized
cells, as well as the compound's mode of extracellular action.
Descriptors: avian influenza virus, glycosidases, enzyme
inhibitors, enzymic activity, inhibition, animal models, influenza virus,
mankind, antimetabolites, chemicophysical properties, enzymes, hydrolases,
influenza virus, orthomyxoviridae, viruses, sialidase.
Guo, C.T., S. Ohta, A. Yoshimoto, K. Nakata, K.F.
Shortridge, T. Takahashi, T. Suzuki, D. Miyamoto, K.I. Jwa Hidari, and Y.
Suzuki (2001). A unique phosphatidylinositol bearing a novel branched-chain
fatty acid from Rhodococcus equi binds to influenza virus hemagglutinin
and inhibits the infection of cells. Journal of Biochemistry 130(3):
377-84. ISSN: 0021-924X.
NAL
Call Number: 385 J822
Abstract: From the aquatic bacterium Rhodococcus
equi strain S(420), we isolated a substance that strongly binds to
influenza viruses. Structural analyses revealed that it is a unique type of
phosphatidylinositol (PtdIns) bearing a branched-chain fatty acid
(14-methyloctadecanoic acid). In a TLC/virus-binding immunostaining assay, this
PtdIns bound to all subtypes of hemagglutinin (HA) of influenza A viruses tested,
isolated from humans, ducks and swine, and also to human influenza B viruses.
Furthermore, the PtdIns significantly prevented the infection of MDCK cells by
influenza viruses, and also inhibited the virus-mediated hemagglutination and
low pH-induced hemolysis of human erythrocytes, which represents the fusogenic
activities of the viral HA. We also used purified hemagglutinin instead of
virions to examine the interaction between viral HA and PtdIns, showing that
the PtdIns binds to hemagglutinin. These findings indicate that the inhibitory
mechanism of PtdIns on the influenza virus infection may be through its binding
to viral HA spikes and host cell endosomal/lysosomal membranes, which are
mediated by the function of viral HA.
Descriptors: hemagglutinins viral metabolism, influenza
prevention and control, influenza A virus human metabolism,
phosphatidylinositols metabolism, phosphatidylinositols pharmacology, Rhodococcus
equi, binding sites physiology, cultured cells, dogs, ducks, fatty acids
chemistry, hemagglutination drug effects, hemolysis drug effects, influenza A
virus avian metabolism, influenza A virus, porcine metabolism, influenza B
virus chemistry, kidney cytology, orthomyxoviridae metabolism,
phosphatidylinositols isolation and purification, swine.
Guo, X., M. Liao, and C. Xin (2003). Sequence of
HA gene of avian influenza A/Chicken/Guangdong/SS/1994 (H9N2) virus. Avian
Diseases 47(Special Issue): 1118-1121.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The RNA of the hemagglutinin (HA) gene of
A/Chicken/Guangdong/SS/1994 (H9N2) was reverse transcription-polymerase chain
reaction amplified, and the cDNA was cloned into a plasmid vector. The complete
coding sequence of the HA gene was sequenced and included 1683 nucleotides,
which encoded for a protein of 560 amino acids. The potential glycosylation
sites related to HA protein function were highly conserved. The amino acid
sequence of the HA proteolytic cleavage was G-S-S-R/G. This cleavage site
sequence is compatible with a low-pathogenic avian influenza virus. Sequence
comparison of this HA gene with other H9 influenza virus sequences in the
GenBank database showed a 82%-97% nucleotide and amino acid sequence
similarity.
Descriptors: infection, virology, avian influenza,
infectious disease, respiratory system disease, viral disease, cloning genetic
techniques, laboratory techniques, reverse transcriptase polymerase chain
reaction, RT PCR, genetic techniques, protein function sequence similarity.
Guo, Y., M. Wang, and J. Guo (1999). [The complete
nucleotide sequences of A/Goose/Guangdong/2/96(H5N1) virus RNA segment 1-3 and
5]. Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi Zhonghua Shiyan He
Linchuang Bingduxue Zazhi [Chinese Journal of Experimental and Clinical
Virology]. 13(3): 205-8. ISSN:
1003-9279.
Abstract: OBJECTIVE: To determine the nucleotide and
amino acid sequences of PB2, PB1, PA and NP genes and compared them with
sequences of A/HK/156/97(H5N1) virus for revealing the relationship between
A/Googs/Guangdong/2/96(H5N1) and A/HK/156/97(H5N1) viruses. METHODS: Virion RNA
was transcribed into cDNA by reverse transcriptase, cDNA amplified by PCR, the
productions of PCR were purified. Afterward, RNA sequence analysis was
performed by the dideoxynucleotide chain termination method, using synthetic
oligodeoxynucleotide primers. RESULTS: The lengths of
A/Goose/Guangdong/2/96(H5N1) virus RNA segment 1-3 and 5 contain 2,341, 2,341,
2,233 and 1,565 nucleotides, respectively. They encode for PB2 (759 amino
acids), PB1 (757 amino acids), PA (716 amino acids) and NP (498 amino acids)
proteins. The homologies of amino acid sequences of PB2, PB1, PA and NP
proteins between A/Goose/Guangdong/2/96 (H5N1) and A/HK/156/97 (H5N1) virus are
96.4%, 97.2%, 97.3% and 97.0%, respectively. CONCLUSION: The lengths of RNA
segment 1-3 and 5 of Goose strain are 2,341, 2,341, 2,233 and 1,565
nucleotides, respectively. The nucleotide sequences of these genes are
distinguish able from those of Hong Kong virus.
Descriptors: geese virology, influenza A virus avian
genetics, poultry diseases virology, RNA viral genetics, amino acid sequence,
influenza A virus avian classification, influenza A virus avian isolation and
purification, molecular sequence data,
sequence analysis, RNA.
Guo, Y., M. Wang, and X. Xu (1999). [Nucleotide
sequence of A/Goose/Guangdong/2/96 (H5N1) virus M and NS RNA]. Zhonghua
Shi Yan He Lin Chuang Bing Du Xue Za Zhi Zhonghua Shiyan He Linchuang Bingduxue
Zazhi [Chinese Journal of Experimental and Clinical Virology]. 13(4):
305-8. ISSN: 1003-9279.
Abstract: OBJECTIVE: To determine the nucleotide
sequences of M and NS genes of A/Goose/Guangdong/2/96(H5N1) virus and also to
compare them with the sequences of A/HK/156/97(H5N1) strain for revealing the
relationship between the two viruses, as well as for setting up a solid base
for studying M and NS genes of influenza A viruses in the future. METHODS:
Virion RNA was transcribed into cDNA by reverse transcriptase, cDNA was
amplified by PCR, the products of PCR were purified. Afterward, RNA sequence
analysis was performed by the dideoxynucleotide chain termination method using
synthetic oligodeoxynucleotide primers. RESULTS: The segment length of
A/Goose/Guangdong/2/96(H5N1) virus RNA 7 is 1,027 nucleotides. It codes M1 (252
amino acids) and M2 (97 amino acids) proteins. However, the segment length of
RNA 8 of A/Goose/Guangdong/2/96(H5N1) virus is 890 nucleotides coding NS1 (230
amino acids) and NS2 (121 amino acids) proteins. The amino acid sequence
homologies of M1, M2, NS1 and NS2 protein molecules between
A/Goose/Guangdong/2/9(H5N1) and A/HK/156/97 (H5N1) viruses are 97.6%, 92.8%,
65.7% and 76.9%, respectively. CONCLUSION: The lengths of
A/Goose/Guangdong/2/96(H5N1) virus RNA 7 and RNA 8 and 1,027 are 890
nucleotides, respectively. These two RNA segments belong to those of avian
influenza A virus. The A/HK/156/97(H5N1) virus RNA 7 and RNA 8 segments are not
derived from those of A/Goose/Guangdong/2/96(H5N1) virus directly.
Descriptors: nucleotide sequence, influenza A virus,
goose, Guangdong, RNA.
Guo, Y., M. Wang, G.S. Zheng, W.K. Li, Y. Kawaoka,
and R.G. Webster (1995). Seroepidemiological and molecular evidence for the
presence of two H3N8 equine influenza viruses in China in 1993-94. Journal
of General Virology 76(Pt. 8): 2009-14.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: In May 1993, a severe epidemic of respiratory
disease began in horses in Inner Mongolia and spread throughout horses in
China. The disease affected mules and donkeys as well as horses but did not
spread to other species, including humans. The severity of the disease raised
the question of whether the outbreak might have been caused by the new
avian-like influenza viruses detected in horses in China in 1989 or by current
variants ofA/equine/Miami/1/63 (H3N8) (equine-2) or by a reassortant between
these viruses. Antigenic and sequence analysis established that all gene segments
of the influenza virus causing the epidemic were of recent equine-2 origin and
that the virus was not a reassortant. Serological analysis of post-infection
horse sera provided evidence for the continued circulation of the
A/Equine/Jilin/1/89 (Eq/Jilin) (H3N8) avian-like viruses in horses in
Heilongjiang province with original antigenic sin-like responses. It is
noteworthy that prior infection with the avian-like Eq/Jilin strain did not
afford cross-protection against a current equine-2 strain. Serological evidence
for the continued circulation of the avian-like H3N8 influenza virus in horses
indicates that this virus has probably established itself in horses in Asia.
Descriptors: horse diseases epidemiology, influenza
veterinary, influenza A virus genetics, antibodies, viral blood, antigens,
viral immunology, base sequence, China epidemiology, disease outbreaks
veterinary, genome, viral, horse
diseases virology, horses, influenza epidemiology, influenza virology,
influenza A virus classification, influenza A virus immunology, molecular
sequence data, phylogeny, sequence analysis, DNA, sequence homology, nucleic
acid, seroepidemiologic studies, serotyping.
Guo, Y., X. Xu, and X. Wan (1998). [Genetic
characterization of an avian influenza A (H5N1) virus isolated from a sick
goose in China]. Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi
Zhonghua Shiyan He Linchuang Bingduxue Zazhi [Chinese Journal of Experimental
and Clinical Virology]. 12(4): 322-5.
ISSN: 1003-9279.
Abstract: Genetic analysis of viral HA gene showed that
there were 22 nucleotide differences in HA gene between goose and human H5N1
viruses. The sequence analysis of amino acid on viral protein molecules
indicated that there were 7 and 9 position differences between goose and human,
chicken H5N1 viruses, respectively. All the three viruses share multiple basic
amino acids (R-E-R-R-R-K-K-R) at the cleavage site between HA1 and HA2 domain,
that is associated with highly pathogenic H5 avian viruses. Except one more
glycosylation site located at 156 position in the chicken strain, there were 7
glycosylation sites at same positions in three virus HA protein molecules. The
analysis of NA protein molecule indicated that the stalk region which extends
from the viral membrane up to amino acid 85, human and chicken viruses had a 19
amino-acid deletion as compared with that of goose virus, while the goose NA
gene was closely related to A/Parrot/Ulster/73 (H7N1) virus. Therefore, goose
H5N1 virus HA and NA genes were avian in origin and were different from those
of human and chicken H5N1 viruses. In our knowledge, this is the first time
that the avian H5N1 virus was found causing influenza outbreak in goose. Why
was A/Goose/Guangdong/2/96(H5N1) virus virulent for geese? It might be related
to the substitution of amino acid located at 138 position near by RBS on HA
protein molecule and 19 amino acids insertion on NA protein molecule as
compared with those of human and chicken H5N1 viruses.
Descriptors: influenza virology, influenza A virus avian
genetics, influenza A virus human genetics, poultry diseases virology, amino
acid sequence, chick embryo, geese virology, influenza veterinary, influenza A
virus avian isolation and purification, influenza A virus human isolation and
purification, molecular sequence data, sequence homology, amino acid.
Ha, Y., D.J. Stevens, J.J. Skehel, and D.C. Wiley
(2002). H5 avian and H9 swine influenza virus haemagglutinin structures:
possible origin of influenza subtypes. EMBO Journal 21(5):
865-75. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: There are 15 subtypes of influenza A virus
(H1-H15), all of which are found in avian species. Three caused pandemics in
the last century: H1 in 1918 (and 1977), H2 in 1957 and H3 in 1968. In 1997, an
H5 avian virus and in 1999 an H9 virus caused outbreaks of respiratory disease
in Hong Kong. We have determined the three-dimensional structures of the
haemagglutinins (HAs) from H5 avian and H9 swine viruses closely related to the
viruses isolated from humans in Hong Kong. We have compared them with known
structures of the H3 HA from the virus that caused the 1968 H3 pandemic and of
the HA--esterase--fusion (HEF) glycoprotein from an influenza C virus.
Structure and sequence comparisons suggest that HA subtypes may have originated
by diversification of properties that affected the metastability of HAs
required for their membrane fusion activities in viral infection.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, influenza A virus avian chemistry, porcine chemistry,
orthomyxoviridae classification, amino acid motifs, amino acid sequence, amino
acid substitution, crystallography,
x-ray, evolution, molecular, hemagglutinin glycoproteins, influenza virus
genetics, hemagglutinin glycoproteins, influenza virus physiology, hydrogen-ion
concentration, avian classification, influenza A virus avian genetics, avian
physiology, porcine classification, porcine genetics, porcine physiology,
membrane fusion, models, molecular, molecular sequence data, protein conformation,
protein structure, secondary, rotation, sequence alignment, sequence homology,
amino acid, structure activity relationship.
Ha, Y., D.J. Stevens, J.J. Skehel, and D.C. Wiley
(2001). X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins
bound to avian and human receptor analogs. Proceedings of the National
Academy of Sciences of the United States of America 98(20): 11181-6. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: The three-dimensional structures of avian H5
and swine H9 influenza hemagglutinins (HAs) from viruses closely related to
those that caused outbreaks of human disease in Hong Kong in 1997 and 1999 were
determined bound to avian and human cell receptor analogs. Emerging influenza
pandemics have been accompanied by the evolution of receptor-binding
specificity from the preference of avian viruses for sialic acid receptors in
alpha2,3 linkage to the preference of human viruses for alpha2,6 linkages. The
four new structures show that HA binding sites specific for human receptors
appear to be wider than those preferring avian receptors and how avian and
human receptors are distinguished by atomic contacts at the glycosidic linkage.
alpha2,3-Linked sialosides bind the avian HA in a trans conformation to form an
alpha2,3 linkage-specific motif, made by the glycosidic oxygen and 4-OH of the
penultimate galactose, that is complementary to the hydrogen-bonding capacity
of Gln-226, an avian-specific residue. alpha2,6-Linked sialosides bind in a cis
conformation, exposing the glycosidic oxygen to solution and nonpolar atoms of
the receptor to Leu-226, a human-specific residue. The new structures are
compared with previously reported crystal structures of HA/sialoside complexes
of the H3 subtype that caused the 1968 Hong Kong Influenza virus pandemic and
analyzed in relation to HA sequences of all 15 subtypes and to receptor
affinity data to make clearer how receptor-binding sites of HAs from avian
viruses evolve as the virus adapts to humans.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, hemagglutinin glycoproteins, influenza virus metabolism, influenza A
virus avian physiology, porcine physiology, receptors, virus chemistry,
receptors, virus physiology, amino acid sequence, binding sites, conserved sequence,
crystallography, x -ray, ducks, hydrogen bonding, models, molecular,
N-acetylneuraminic acid, protein conformation, swine.
Hablolvarid, M.H., I.S. Haghdost, S.A. Pourbakhsk,
and M.R. Gholami (2003). A study on histopathologic changes in chicken following
intravenous inoculation with avian influenza virus
A/Chicken/Iran/259/1998(H9N2). Archives of Razi Institute (55):
41-53. ISSN: 0365-3439.
NAL
Call Number: QR189.A73
Descriptors: avian influenza virus, clinical aspects,
experimental infections, histopathology, poultry.
Haller, O. (1975). A mouse hepatotropic variant of
influenza virus. Archives of Virology 49(2-3): 99-116. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A hepatotropic variant of avian influenza
virus A/Turkey/England 63 (Hav 1, Nav 3) was selected by serial passages in
mouse liver. Adaptation to this organ was established after 13 in vivo passages
and was found to improve during further passages as shown by increasing rates
of replication in livers of ICR mice. The mutant virus finally selected was
stable and differed from the original virus mainly in lethality upon
intraperitoneal injection in mice, in its ability to grow to high titers in
livers of susceptible animals and in plaque morphology in chick embryo fibroblasts.
No differences were detected in hemagglutination inhibition and neutralization
by standard mouse antisera. Pathogenicity for the liver was independent of the
route of inoculation, included other laboratory animals sensitive to influenza
virus and could be inhibited by amantadine. Fatal hepatitis in 50 per cent of
susceptible mice by the intraperitoneal route required from 10 to 20 EID50-.
Pathological changes consisted of severe necrosis of liver parenchyma
accompanied by release of F antigen into the serum and were apparently due to
virus replication in hepatic cells as evidenced by immunofluorescence. The main
implications of this animal model for studies on experimental hepatitis and on
myxovirus-host interactions in an organ not usually associated with influenza
are discussed.
Descriptors: adaptation, physiological, hepatitis A
microbiology, liver microbiology, mutation, orthomyxoviridae growth and
development, amantadine therapeutic use, antigens, viral, disease models,
animal, guinea pigs, hamsters, hepatitis A pathology, hepatitis A prevention
and control, liver immunology, liver pathology, mice, mice inbred strains,
orthomyxoviridae immunology, orthomyxoviridae pathogenicity, rats, virus
replication.
Haller, O., H. Arnheiter, and J. Lindenmann (1976). Genetically
determined resistance to infection by hepatotropic influenza A virus in mice:
effect of immunosuppression. Infection and Immunity 13(3):
844-54. ISSN: 0019-9567.
NAL
Call Number: QR1.I57
Abstract: Mice carrying the gene Mx were resistant to
the lethal action of a hepatotropic line of avian influenza A virus. In
resistant animals, foci of liver necrosis were self-limiting, and maximal virus
titers reached were much below those in susceptible animals. Resistance could
not be abrogated by immunosuppressive treatment with cyclophosphamide,
methotrexate, or procarbazine, although such treatment prevented cellular
infiltration at sites of virus replication and appeared to delay virus
clearance. Silica and thorium dioxide, thought to inhibit macrophage function,
likewise failed to abolish resistance. Regenerating liver tissue did not
support more extensive virus replication than did intact adult liver.
Descriptors: immunosuppression, influenza prevention and
control, liver microbiology, orthomyxoviridae pathogenicity, antigens viral
analysis, cyclophosphamide pharmacology,
hepatectomy, influenza genetics, liver pathology, liver regeneration,
methotrexate pharmacology, mice, mice inbred A, mice inbred c57bl, mice inbred
ICR, orthomyxoviridae growth and development, procarbazine pharmacology,
reticuloendothelial system microbiology, silicon dioxide pharmacology, thorium
dioxide pharmacology.
Haller, O., H. Arnheiter, and J. Lindenmann (1979). Natural,
genetically determined resistance toward influenza virus in hemopoietic mouse
chimeras. Role of mononuclear phagocytes. Journal of Experimental
Medicine 150(1): 117-26. ISSN:
0022-1007.
NAL
Call Number: 448.8 J822
Abstract: Radiation chimeras produced by crosswise
transfers of bone-marrow cell among histocompatible mice susceptible, or
genetically resistant, to lethal challenge by a number of myxoviruses were used
to test whether macrophage resistance (as assessed in vitro) and resistance of
the animal (as measured in vivo), both previously shown to be brought about by
the gene Mx, were causally related. 49 chimeras were tested individually, both
of resistance of their macrophages to in vitro challenge with M-TUR (a strain
of avian influenza virus A/Turkey/England/63 adapted to grow in cultured mouse
peritoneal macrophages), and for resistance of the animal in vivo upon
challenge with pneumotropic, neurotropic, or hepatotropic influenza viruses.
Cultivated Kupffer cells and peritoneal macrophages harvested from chimeric
mice expressed the resistance phenotype of the bone-marrow donor irrespective
of the host environment in which they had differentiated. However,
susceptibility or resistance in vivo was according to the genotype of the host.
Thus, inborn resistance of radiation chimeras was found to be independent of
Mx-gene expression in cells of the hemopoietic system.
Descriptors: hematopoietic stem cells immunology,
immunity, natural, orthomyxoviridae immunology, phagocytes immunology,
radiation chimera, genotype, hematopoietic stem cell transplantation, influenza
immunology, mice, mice inbred strains genetics, homologous transplantation.
Hamzehei, M. and N. Ledinko (1980). Inhibition of
influenza A virus replication by rifampicin and selenocystamine. Journal
of Medical Virology 6(2): 169-74.
ISSN: 0146-6615.
Abstract: The effects of selenocystamine, an inhibitor
of influenza virus RNA-dependent RNA polymerase in vitro activity, in the
antibiotic rifampicin were studied on influenza A/PR/8/34 (HON1) infection in
embryonated eggs. Both drugs completely inhibited hemagglutinating and
infective virus yields when added at relatively early times postinfection.
Maximal inhibition was produced by apparently noncytotoxic concentrations of 50
microgram of selenocystamine, or of 400 microgram of rifampicin, per egg.
Descriptors: cystamine analogs and derivatives, influenza
A virus avian drug effects, organoselenium compounds, rifampin pharmacology,
selenium pharmacology, virus replication drug effects, chick embryo, cystamine
administration and dosage, cystamine pharmacology, avian growth and
development, rifampin administration and dosage, selenium administration and
dosage, time factors, tissue culture.
Hannoun, C. (1977). Isolation from birds of
influenza viruses with human neuraminidase. Developments in Biological
Standardization 39: 469-72. ISSN:
0301-5149.
NAL
Call Number: QR180.3.D4
Abstract: Attempts at virus isolation from cloacal
swabs resulted in the recovery of 10 strains of hemagglutinating viruses from a
total of 349 ducks, mainly shelducks (Tadorna tadorna) captured in the
north of France. Four of these isolates were identified as influenza strains
corresponding to the following antigenic composition: Hav6-N2, Hav6-Nav4 and
Hav1-N2 (2 strains). Shelduck is known to be a partially migratory species,
wintering in western Europe, some of them migrating northward to Scandinavia
during the summer. The captures were made between November 1976 and February
1977: one of the birds was caught four times and was found to be negative for
virus in November, positive in December (isolation of a strain Hav6-Nav4),
negative again in January and February. Blood taken in February did not show
the presence of HI antibodies to the homologous virus.
Descriptors: antigens, viral, ducks microbiology, influenza
A virus avian isolation and purification, neuraminidase immunology, antibodies,
viral, cloaca microbiology, France, hemagglutination inhibition tests,
hemagglutinins viral, avian enzymology, avian immunology, human enzymology,
seasons.
Harboe, A., R. Schoyen, and A. Bye Hansen (1966). Haemagglutination
inhibition by antibody to host material of fowl plague virus grown in different
tissues of chick chorioallantoic membranes. Acta Pathologica Et
Microbiologica Scandinavica 67(4): 573-8.
ISSN: 0365-5555.
Descriptors: endoderm, fetal membranes, hemagglutination
inhibition tests, influenza A virus avian immunology, antibodies, chick embryo,
glycosaminoglycans, hemagglutination tests, orthomyxoviridae immunology, virus
cultivation.
Harley, V.R., P.J. Hudson, B.E. Coupar, P.W. Selleck,
H. Westbury, and D.B. Boyle (1990). Vaccinia virus expression and sequence
of an avian influenza nucleoprotein gene: potential use in diagnosis. Archives
of Virology 113(1-2): 133-41. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The nucleoprotein (NP) gene from avian
influenza strain A/Shearwater/Aust/1/72 (H6N5) was cloned, sequenced, and
expressed in vaccinia virus for the production of potent sera in immunised
rabbits. The NP gene is 1565 bp and shares greater than 95% amino acid sequence
identity with other NPs of the avian subtype. The recombinant NP expressed by
vaccinia virus comigrated with endogenous A/Shearwater/Aust/1/72 NP by Western
blot analysis. Polyclonal rabbit sera raised against recombinant NP was
evaluated in an antigen capture ELISA system as a potential diagnostic tool for
the detection of avian influenza. All type A strains, comprising several HA and
NA subtypes, but not type B nor other avian viruses, were detected.
Descriptors: fowl plague diagnosis, genes viral, influenza
A virus avian genetics, nucleoproteins genetics, vaccinia virus genetics, viral
core proteins, viral proteins genetics, amino acid sequence, antibodies, viral
immunology, base sequence, blotting, southern, cloning, molecular, DNA, viral,
enzyme linked immunosorbent assay, avian immunology, molecular sequence data,
nucleoproteins immunology, predictive value of tests, thymidine kinase
genetics, vaccinia virus immunology, viral proteins immunology.
Harley, V.R., K.A. Mather, B.E. Power, J.L. McKimm
Breschkin, and P.J. Hudson (1990). Characterisation of an avian influenza
virus nucleoprotein expressed in E. coli and in insect cells. Archives
of Virology 113(3/4): 267-277. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The nucleoprotein (NP) gene from influenza
virus A/Shearwater/Australia/72 has been expressed intracellularly in both E.
coli and insect cells. E. coli-derived NP was identified by Western
blot analysis as a 56 kDa protein which co-migrates with virion-derived NP.
This protein was purified by immunoaffinity chromatography and a nitrocellulose
binding assay showed that NP formed complexes with positive- and negative-sense
influenza neuraminidase RNA transcribed in vitro. ELISA and Western blot analysis
revealed that recombinant NP of 56 kDa was produced in high yields in insect
cells using a baculovirus vector. Immunofluorescence microscopy revealed that
NP was localised to the nucleus of infected insect cells.
Descriptors: avian influenza virus, viral proteins,
nucleoproteins, RNA, recombination, purification, characterization, Escherichia
coli, Autographa californica, nuclear polyhedrosis viruses.
Harley, V.R., C.W. Ward, and P.J. Hudson (1989). Molecular
cloning and analysis of the N5 neuraminidase subtype from an avian influenza
virus. Virology 169(1): 239-43.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The neuraminidase (NA) gene from the
prototype N5 influenza virus, A/Shearwater/Australia/72, has been cloned and
completely sequenced. An open reading frame of 1404 bp (468 amino acids) is
flanked by 20-bp 5'- and 31-bp 3'-untranslated regions. The deduced amino acid
sequence of the N5 gene was compared with sequences from N2, N1, N7, N8, and N9
subtypes. One hundred thirteen amino acid residues (24%) are completely
conserved across subtypes and include active site residues, cysteines,
potential glycosylation sites, and certain glycines which suggests that these
subtypes share a common ancestor and adopt the same 3-D conformation. Three
groups can be assigned from amino acid homologies: (i) N5, N8, N1; (ii) N7, N9;
and (iii) N2 where the percentage identity within groups is 55-68% and between
groups is 40-46%, the N5-N8 pair bearing the closest identity (68%).
Phylogenetic analysis suggests that these groups diverged concurrently.
Descriptors: DNA, viral genetics, influenza A virus avian
genetics, neuraminidase genetics, amino acid sequence, base sequence, cloning,
molecular, DNA probes, deoxyribonuclease ecori,
avian enzymology, molecular sequence data, phylogeny.
Harms, E., W. Rohde, F. Bosch, and C. Scholtissek
(1978). Biochemical studies on influenza viruses. II. Assignment of gene
functions to RNA segments 5, 7, and 8 of fowl plague virus and virus N. Virology
86(2): 413-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian analysis, influenza A
virus analysis, RNA viral analysis, genes viral, avian genetics, influenza A
virus genetics, nucleic acid hybridization, peptides analysis, recombination,
genetic, viral proteins analysis.
Harms, E., W. Rohde, and C. Scholtissek (1978). Minor
nucleic acids in influenza virus. Journal of General Virology 40(3):
691-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: A nucleic acid fraction consisting of RNA and
DNA sequences with an apparent mol. wt. of 1.4 to 1.5 x 10(6) is present in
minor amounts in purified influenza virus. The RNA is virus-specific and in the
case of fowl plague virus (FPV) contains sequences of genes 2 and 7 which code
for one of the proteins constituting the polymerase complex and for the matrix
protein respectively.
Descriptors: DNA analysis, influenza A virus avian
analysis, RNA viral analysis, genes viral, avian genetics, molecular weight,
nucleic acid hybridization, viral genetics, viral proteins biosynthesis.
Harvey, R., A.C. Martin, M. Zambon, and W.S. Barclay
(2004). Restrictions to the adaptation of influenza a virus H5 hemagglutinin
to the human host. Journal of Virology 78(1): 502-7. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The binding specificities of a panel of avian
influenza virus subtype H5 hemagglutinin (HA) proteins bearing mutations at key
residues in the receptor binding site were investigated. The results
demonstrate that two simultaneous mutations in the receptor binding site
resulted in H5 HA binding in a pattern similar to that shown by human viruses.
Coexpression of the ion channel protein, M2, from most avian and human strains
tested protected H5 HA conformation during trafficking, indicating that no
genetic barrier to the reassortment of the H5 surface antigen gene with
internal genes of human viruses existed at this level.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus, avian pathogenicity, avian classification,
influenza A virus, avian genetics, receptors, cell surface metabolism,
adaptation, physiological genetics, binding sites genetics, erythrocytes
metabolism, hemagglutinin glycoproteins, influenza virus chemistry, hemagglutinin
glycoproteins, influenza virus metabolism, models, molecular, point mutation,
species specificity.
Hastie, N.D. and B.W. Mahy (1973). RNA-dependent
RNA polymerase in nuclei of cells infected with influenza virus. Journal
of Virology 12(5): 951-61. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Descriptors: cell nucleus enzymology, DNA directed RNA
polymerases metabolism, orthomyxoviridae enzymology, RNA metabolism, cell
fractionation, centrifugation, density
gradient, chick embryo, cytochrome reductases analysis, cytochrome C group,
DNA, viral isolation and purification, dactinomycin pharmacology, enzyme
induction, fibroblasts, hemagglutination tests, influenza A virus avian
enzymology, magnesium pharmacology, manganese pharmacology, microsomes
enzymology, NAD, nucleic acid hybridization, proteins metabolism, sucrose, time
factors, tritium.
Hatta, M., P. Gao, P. Halfmann, and Y. Kawaoka
(2001). Molecular basis for high virulence of Hong Kong H5N1 influenza A
viruses. Science 293(5536): 1840-2. ISSN: 0036-8075.
NAL
Call Number: 470 Sci2
Abstract: In 1997, an H5N1 influenza A virus was
transmitted from birds to humans in Hong Kong, killing 6 of the 18 people
infected. When mice were infected with the human isolates, two virulence groups
became apparent. Using reverse genetics, we showed that a mutation at position
627 in the PB2 protein influenced the outcome of infection in mice. Moreover,
high cleavability of the hemagglutinin glycoprotein was an essential
requirement for lethal infection.
Descriptors: influenza epidemiology, influenza virology,
influenza A virus genetics, influenza A virus pathogenicity, amino acid
sequence, birds virology, DNA, recombinant genetics, hemagglutinin
glycoproteins, influenza virus chemistry, hemagglutinin glycoproteins,
influenza virus genetics, hemagglutinin glycoproteins, influenza virus
metabolism, Hong Kong epidemiology, influenza mortality, influenza transmission
, influenza A virus avian genetics, avian pathogenicity, avian physiology,
human genetics, human pathogenicity, human physiology, influenza A virus
physiology, lung virology, mice, mutation, missense genetics, reassortant
viruses genetics, reassortant viruses pathogenicity, reassortant viruses
physiology, viral proteins chemistry, viral proteins genetics, viral proteins
metabolism.
Hatziioannou, T., E. Delahaye, F. Martin, S.J.
Russell, and F.L. Cosset (1999). Retroviral display of functional binding
domains fused to the amino terminus of influenza hemagglutinin. Human
Gene Therapy 10(9): 1533-44. ISSN:
1043-0342.
Abstract: We have previously shown that retroviral
vector particles derived from Moloney murine leukemia virus (Mo-MuLV) can
efficiently incorporate influenza hemagglutinin (HA) glycoproteins from fowl
plague virus (FPV), thus conferring a broad tropism to the vectors. To modify
its host range, we have engineered the FPV HA to display four different
polypeptides on its N terminus: the epidermal growth factor, an anti-human MHC
class I molecules scFv (single-chain antibody), an anti-melanoma antigen scFv,
and an IgG Fc-binding polypeptide. All recombinant HA glycoproteins were
correctly expressed and processed, and efficiently incorporated into Mo-MuLV
retroviral particles, indicating that amino-terminal insertion of large
polypeptides did not alter the conformation of HA chimeras. Virions carrying
the different chimeras bound specifically to cells expressing the targeted cell
surface molecules of each ligand. In addition, all virion types were infectious
but exhibited various degrees of specificity regarding the use of the targeted
cell surface molecule versus the wild-type FPV HA receptor for cell entry and
infection. For some ligands tested, infectivity was significantly increased on
cells that express the targeted receptor, compared with cells that express only
the wild-type HA receptor. Furthermore, some polypeptides could abolish
infectivity via the wild-type FPV HA receptor. Our data therefore indicate that
it is possible to engineer the HA envelope glycoprotein by fusing ligands to its
amino-terminal end without affecting its fusion activity.
Descriptors: genetic vectors, hemagglutinin glycoproteins,
influenza virus genetics, moloney murine leukemia virus, peptides genetics, 3T3
cells, antibodies, neoplasm genetics, binding sites, epidermal growth factor
genetics, gene fusion, hemagglutinin glycoproteins, influenza virus metabolism,
immunoglobulin fragments genetics, immunoglobulin variable region genetics,
influenza A virus avian genetics, mice, peptides metabolism, recombinant fusion
proteins genetics, tumor cultured cells, virion metabolism.
Hatziioannou, T., S. Valsesia Wittmann, S.J. Russell,
and F.L. Cosset (1998). Incorporation of fowl plague virus hemagglutinin
into murine leukemia virus particles and analysis of the infectivity of the
pseudotyped retroviruses. Journal of Virology 72(6): 5313-7. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: We describe retrovirus particles carrying the
fowl plague virus (FPV) hemagglutinin (HA). When expressed in cells providing
Moloney murine leukemia virus (MoMLV) Gag and Pol proteins and a lacZ
retroviral vector, FPV HA was found to be efficiently expressed, correctly
processed, and stably incorporated into retroviral particles. HA-bearing
retroviruses were infectious with a wide host range and were only 10-fold less
infectious than retroviruses carrying wild-type MLV retroviral envelopes. We
also coexpressed HA proteins in retroviral particles with chimeric
MoMLV-derived envelope glycoproteins that efficiently retarget virus attachment
but are only weakly fusogenic. Our results suggest that HA can in some cases
enhance the fusion ability of these retroviral particles, depending on the cell
surface molecule that is used as a receptor.
Descriptors: hemagglutinins genetics, influenza A virus
avian genetics, leukemia virus, murine genetics, viral fusion proteins
genetics, gene products, gag genetics, gene products, pol genetics, lac operon,
mice, recombination, genetic, virion genetics.
Hausmann, J., E. Kretzschmar, W. Garten, and H.D.
Klenk (1997). Biosynthesis, intracellular transport and enzymatic activity
of an avian influenza A virus neuraminidase: role of unpaired cysteines and
individual oligosaccharides. Journal of General Virology 78(Pt. 12):
3233-45. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Intracellular transport, glycosylation,
tetramerization and enzymatic activity of the neuraminidase (NA) of fowl plague
virus (FPV) were analysed in vertebrate cells after expression from a vaccinia
virus vector. Tetramerization occurred with a half-time of 15 min, whereas
passage through the medial Golgi apparatus and transport to the plasma membrane
occurred with half-times of 2 and 3 h, respectively, suggesting a step in NA
maturation beyond tetramerization that limits the rate of transport to the
medial Golgi. NA transport rates were about fourfold slower than those of
haemagglutinin (HA). Slow transport and processing of FPV NA was not altered by
coexpression of FPV HA, nor was the transport rate of HA influenced by NA. The
slow transport kinetics of NA were also observed in FPV-infected CV-1 cells. As
deduced from the coding sequence, FPV NA has the shortest stalk of all
naturally occurring NAs described to date and contains only three potential
N-glycosylation sites, which are all located in the globular head domain.
Elimination of each of the three N-glycosylation sites revealed that the two
oligosaccharides at positions 124 and 66 are of the complex type, whereas the one
at Asn-213 remains in mannose-rich form. The glycosylation mutants showed also
that oligosaccharides at positions 124 and 213 of FPV NA modulate enzymatic
activity. Transport of NA is not influenced by single elimination of any of the
three oligosaccharide attachment sites. Mutational analysis of the three Cys
residues not involved in intrachain disulfide pairing revealed that Cys-49 in
the stalk of the NA molecule is responsible for the formation of
disulfide-linked dimers. Analysis of cysteine mutants of FPV NA also
demonstrated that disulfide-linked dimers are not absolutely necessary for the
formation of enzymatically active tetramers but may stabilize the quaternary
structure of NA.
Descriptors: birds virology, influenza A virus avian
enzymology, neuraminidase metabolism, biological transport, cysteine, enzyme
activation, glycosylation, oligosaccharides.
Hay, A.J. (1974). Studies on the formation of the
influenza virus envelope. Virology 60(2): 398-418. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: hemagglutinins viral, orthomyxoviridae growth
and development, virus replication, autoradiography, cell membrane analysis,
cell membrane enzymology, chick embryo, chromatography, affinity,
dihydrolipoamide dehydrogenase analysis, electrophoresis, polyacrylamide gel,
endoplasmic reticulum analysis, fibroblasts, glycopeptides analysis,
glycoproteins analysis, influenza A virus avian growth and development,
influenza A virus avian immunology, methionine, microscopy, electron,
neuraminic acids analysis, nucleotidases analysis, orthomyxoviridae immunology,
peptides analysis, sulfur radioisotopes.
Hay, A.J., B. Lomniczi, A.R. Bellamy, and J.J. Skehel
(1977). Transcription of the influenza virus genome. Virology
83(2): 337-55. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus avian
genetics, RNA, messenger biosynthesis, viral biosynthesis, transcription,
genetic, cell line, avian metabolism, poly A, viral analysis, virion
metabolism.
Hay, A.J. and J.J. Skehel (1979). Characterization
of influenza virus RNA transcripts synthesized in vitro. Journal of
General Virology 44(3): 599-608.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Polyadenylated transcripts synthesized in
vitro by detergent-disrupted influenza virus resemble virus mRNAs in that they
possess the complement of the 3' terminus of the genome RNAs but lack sequences
corresponding to the same 5' terminal region, including the homologous sequence
of nucleotides 1 to 22. Transcription is initiated at the 3' terminus by both
ApG and GpG as well as in the absence of added primer.
Descriptors: influenza A virus avian analysis,
orthomyxoviridae analysis, RNA viral analysis, transcription, genetic, base
sequence, cell free system, avian metabolism, nucleic acid hybridization,
nucleotides analysis, poly A analysis, viral biosynthesis.
Hay, A.J., J.J. Skehel, and J. McCauley (1982). Characterization
of influenza virus RNA complete transcripts. Virology 116(2):
517-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian genetics, RNA viral
analysis, adenosine metabolism, base sequence, chromatography, DEAE-cellulose,
chromatography, thin layer, phosphorylation, ribonucleases pharmacology,
ribonucleotides analysis, transcription, genetic.
Hay, A.J., A.J. Wolstenholme, J.J. Skehel, and M.H.
Smith (1985). The molecular basis of the specific anti-influenza action of
amantadine. EMBO Journal 4(11): 3021-4. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: Amantadine (1-aminoadamantane hydrochloride)
is effective in the prophylaxis and treatment of influenza A infections. In
tissue culture this selective, strain-specific antiviral activity occurs at
relatively low concentrations (5 microM or less), which inhibit either the
initiation of infection or virus assembly. The data reported here demonstrate
that the basis of these actions is similar and resides in the virus-coded M2
membrane protein, the product of a spliced transcript of RNA segment 7.
Mutations which confer resistance to amantadine are restricted to four amino
acids within a hydrophobic sequence, indicating that the drug is targetted
against the putative membrane-associated portion of the molecule. The influence
of the virus haemagglutinin on the amantadine sensitivity of virus strains
implies that the drug may interfere with interactions between these two virus
proteins.
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, human drug effects, membrane proteins genetics, chick embryo,
chickens, drug resistance, microbial, fibroblasts cytology, avian genetics,
human genetics, mutation, RNA splicing, species specificity, transcription,
genetic drug effects.
Hayman, M.J., J.J. Skehel, and M.J. Crumpton (1973). Purification
of virus glycoproteins by affinity chromatography using Lens culinaris
phytohaemagglutinin. FEBS Letters 29(2): 185-8. ISSN: 0014-5793.
NAL
Call Number: QD415.F4
Descriptors: glycoproteins isolation and purification,
mammary tumor virus, mouse analysis, orthomyxoviridae analysis, parainfluenza
virus 1, human analysis, viral proteins isolation and purification,
chromatography, affinity, electrophoresis, polyacrylamide gel, influenza A
virus avian analysis, lectins, polysaccharides,
sodium dodecyl sulfate.
He Houjun and Dai Yimi (Apr 2004)). Progress in
molecular biology of avian influenza virus. Journal of Jiangxi
Agricultural University (China) [Jiangxi Nongye Daxue Xuebao (China)] 26(2): 289-293. ISSN: 1000-2286.
Descriptors: avian influenza virus A, molecular biology,
progress.
Heller, E. and C. Scholtissek (1980). Evidence for
intracistronic complementation of the product of the influenza virus gene Ptra
(P3 of fowl plague virus). Journal of General Virology 49(1):
133-9. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The ts lesion of the fowl plague virus (FPV)
mutants ts 18 and ts 236 has been located in RNA segment 2 (Ptra gene,
corresponding to P3). After double-infection with these mutants and ts 90 or ts
93, which also carry a ts lesion in segment 2, plaques were formed at the
non-permissive temperature (40 degrees C). These plaques cannot be passaged at
40 degrees C and exhibit a morphology which differs from those formed by the
wild-type virus. The yield of infectious particles after double-infection shows
a non-linear correlation between the plaque number and dilution, indicating
that at least two particles are needed for infection of a cell. All
experimental evidence points to an intracistronic complementation within the P3
protein.
Descriptors: genes, structural, genes viral, influenza A
virus avian genetics, recombination, genetic, cultured cells, chick embryo,
genetic complementation test, avian growth and development, mutation, plaque
assay, temperature.
Henkel, J.R., G.A. Gibson, P.A. Poland, M.A. Ellis,
R.P. Hughey, and O.A. Weisz (2000). Influenza M2 proton channel activity
selectively inhibits trans-Golgi network release of apical membrane and
secreted proteins in polarized Madin-Darby canine kidney cells. Journal
of Cell Biology 148(3): 495-504.
ISSN: 0021-9525.
NAL
Call Number: 442.8 J828
Abstract: The function of acidification in protein
sorting along the biosynthetic pathway has been difficult to elucidate, in part
because reagents used to alter organelle pH affect all acidified compartments
and are poorly reversible. We have used a novel approach to examine the role of
acidification in protein sorting in polarized Madin-Darby canine kidney (MDCK)
cells. We expressed the influenza virus M2 protein, an acid-activated ion
channel that equilibrates lumenal and cytosolic pH, in polarized MDCK cells and
examined the consequences on the targeting and delivery of apical and
basolateral proteins. M2 activity affects the pH of only a subset of acidified
organelles, and its activity can be rapidly reversed using ion channel blockers
(Henkel, J.R., G. Apodaca, Y. Altschuler, S. Hardy, and O.A. Weisz. 1998. Mol.
Biol. Cell. 8:2477-2490; Henkel, J.R., J.L. Popovich, G.A. Gibson, S.C.
Watkins, and O.A. Weisz. 1999. J. Biol. Chem. 274:9854-9860). M2 expression
significantly decreased the kinetics of cell surface delivery of the apical
membrane protein influenza hemagglutinin, but not of the basolaterally
delivered polymeric immunoglobulin receptor. Similarly, the kinetics of apical
secretion of a soluble form of gamma-glutamyltranspeptidase were reduced with
no effect on the basolaterally secreted fraction. Interestingly, M2 activity
had no effect on the rate of secretion of a nonglycosylated protein (human growth
hormone [hGH]) that was secreted equally from both surfaces. However, M2 slowed
apical secretion of a glycosylated mutant of hGH that was secreted
predominantly apically. Our results suggest a role for acidic trans-Golgi
network pH in signal-mediated loading of apical cargo into forming vesicles.
Descriptors: Golgi apparatus metabolism, influenza A virus
avian metabolism, ion channels metabolism, viral matrix proteins metabolism,
cell line, cell membrane metabolism, cell polarity, dogs, gene expression,
hemagglutinin glycoproteins, influenza virus biosynthesis, hemagglutinin
glycoproteins, influenza virus genetics, protons, receptors, polymeric
immunoglobulin biosynthesis, receptors, polymeric immunoglobulin genetics,
viral matrix proteins genetics.
Henkel, J.R. and O.A. Weisz (1998). Influenza
virus M2 protein slows traffic along the secretory pathway. pH perturbation of
acidified compartments affects early Golgi transport steps. Journal of Biological Chemistry
273(11): 6518-24. ISSN: 0021-9258.
NAL
Call Number: 381 J824
Abstract: M2, an acid-activated ion channel, is an
influenza A virus membrane protein required for efficient nucleocapsid release
after viral fusion with the endosomal membrane. Recombinant M2 slows protein
traffic through the Golgi complex (Sakaguchi, T., Leser, G. P)., and Lamb, R.
A. (1996) J. Cell Biol. 133, 733-47). Despite its critical role in viral
infection, little is known about the subcellular distribution of M2 or its fate
following delivery to the plasma membrane (PM). We measured the kinetics of M2
transport in HeLa cells, and found that active M2 reached the PM considerably more
slowly than inactive M2. In addition, M2 delayed intra-Golgi transport and cell
surface delivery of influenza hemagglutinin (HA). We hypothesized that the
effects of M2 on transport through non-acidified compartments are due to
inefficient retrieval from the trans-Golgi of machinery required for
intra-Golgi transport. In support of this, acutely activated M2 had no effect
on intra-Golgi transport of HA, but still slowed HA delivery to the PM. Thus,
M2 has an indirect effect on early transport steps, but a direct effect on late
steps in PM delivery. These findings may help explain the conflicting and
unexplained effects on protein traffic observed with other perturbants of
intraorganelle pH such as weak bases and inhibitors of V-type ATPases.
Descriptors: Golgi apparatus metabolism, influenza A virus
avian metabolism, ion channels secretion, viral matrix proteins secretion,
amantadine pharmacology, antiviral agents pharmacology, biological transport
drug effects, cell compartmentation, cell membrane metabolism, HeLa cells,
hemagglutinin glycoproteins, influenza virus metabolism, hydrogen-ion
concentration, imidazoles pharmacology, spiro compounds pharmacology.
Herget, M. and C. Scholtissek (1993). A
temperature-sensitive mutation in the acidic polymerase gene of an influenza A
virus alters the regulation of viral protein synthesis. Journal of
General Virology 74(Pt. 9): 1789-94.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The temperature-sensitive defect of mutant ts
263 of fowl plague virus (FPV) is located in the acidic polymerase (PA) gene
and is due to a single base substitution (C2036T), which leads to an amino acid
replacement (Ala671 to Val) in a highly conserved region of the protein. During
passage at 33 degrees C ts 263 stably carries over a ninth RNA segment, which
consists of a truncated PA gene. Although the deletion is in-frame and it is
transcribed into mRNA, no corresponding protein is detected in vivo. After
reversion to wild-type this extra RNA segment is immediately lost. At the
non-permissive temperature of 40 degrees C no significant viral products of ts
263 are synthesized. Under semi-permissive conditions there is a relative, but
very significant over-production of the M1 protein, which is not accompanied by
a corresponding elevated M1 mRNA synthesis. These results are in agreement with
the idea that the PA protein is involved in the regulation of viral protein
synthesis at the level of expression of mRNA. Preinfection of chicken embryo
cells with ts 263 at a semi-permissive temperature interferes with the
replication of FPV wild-type indicating that premature availability of M1 might
be detrimental for influenza virus replication.
Descriptors: DNA directed RNA polymerases genetics, gene
expression regulation, viral, genes viral, influenza A virus avian genetics,
avian metabolism, mutation, viral proteins biosynthesis, amino acid sequence,
blotting, northern, cultured cells, chick embryo, cloning, molecular, conserved
sequence, crosses, genetic, DNA directed RNA polymerases metabolism, avian
physiology, polymerase chain reaction, RNA, messenger biosynthesis, messenger metabolism, viral isolation and
purification, viral metabolism, temperature, virus replication.
Hernandez Magdaleno, A., M.T. Casaubon Hugening, and
J. Garcia Garcia. (1998). Viremia durante la infeccion del virus de
influenza aviar (h5n2) altamente patogeno en aves susceptibles y en aves
inmunizadas. [Study of the viremia during the infecction of a highly pathogenic
avian influenza virus (h5n2) on susceptible and immunized chickens]. In: 34
Reunion Nacional de Investigacion Pecuaria, Queretaro, Qro. (Mexico), p. 250.
Abstract: El objetivo de la presente
investigacion fue contribuir al estudio de la patogenia del virus de influenza
aviar (H5N2) altamente patogeno, en aves susceptibles (Av-Susc) y en aves
inmunizadas (Av-Inm), durante las primeras 72 horas post-inoculacion (hpi), a
traves del estudio de la viremia. Se formaron dos grupos de 100 aves libres de
patogenos especificos. A los 8 dias de edad, uno de los grupos fue inmunizado
con una vacuna emulsionada contra influenza aviar (IA) y el otro grupo
permanecio sin inmunizar. A las cuatro semanas de edad, ambos grupos de aves
fueron inoculados via intranasal con 1 x 103 DLEP50 del virus A/Chicken/Queretaro/14588-19/95
(H5N2), altamente patogeno. Se tomaron aleatoriamente 3 aves de cada grupo a
las 2, 4, 8, 12, 16, 20, 24, 28, 32, 36, 40, 44, 48, 52, 56, 60, 64, 68 y 72
hpi. De cada ave se tomo una muestra de sangre directamente del corazon para
aislamiento y titulacion viral. A partir de las muestras de sangre se pudo
identificar y cuantificar el virus de influenza aviar de alta patogenicidad,
solo en las Av-Susc. El aislamiento e identificacion del virus se realizo a
partir de las 28 hpi en el 100% de las Av-Susc. El titulo del virus circulante
en las Av-Susc a las 28 hpi fue de 106.12 DLEP50/ml de sangre; posteriormente
el titulo de virus circulante se mantuvo en un rango de 105.69 a 108.06
DLEP50/ml, entre las 32 y 68 hpi. La mayor cantidad de virus circulante, fue
detectado a las 72 hpi, con un titulo de 109.04 DLEP50/ml de sangre. La
conversion del titulo viral a numeros naturales, indica que entre las 28 y 68
hpi, las Av-Susc, tuvieron menos de 200,000,000 DLEP50/ml de sangre. A las 72
hpi, el titulo de virus circulante fue de 109.04 DLEP50/ml de sangre, lo que al
convertirse a numeros naturales equivale a 1,096,478,196 DLE50/ml de sangre,
siendo este el valor maximo que se identifico. La titulacion del virus
circulante en sangre, sugiere que el virus tuvo varios ciclos de replicacion
local, antes de diseminarse. La replicacion viral fue muy eficiente, si se toma
en cuenta que la dosis inoculada contenia 1,000 DLEP50 de virus y a las 72 hpi,
la cantidad de virus circulante fue de 1,096,478,196 DLEP50/ml de sangre. Las
Av-Inm no presentaron viremia, lo que sugiere que uno de los mecanismos por el
cual la vacunacion previene la mortalidad es que evita la viremia.
Descriptors: broiler chickens, avian influenza
virus, pathogenicity, immunity, Septicaemia, bacterioses, biological
properties, birds, chickens, domestic animals, Galliformes, infectious
diseases, influenza virus, livestock, meat animals, microbial properties,
orthomyxoviridae, poultry, useful animals, viruses.
Hess, W.R. and A.H. Dardiri (1968). Some
properties of the virus od duck plague. Archiv Fur Die Gesamte
Virusforschung 24(1): 148-53. ISSN:
0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: ducks, influenza A virus avian drug effects,
acridines, biometry, chick embryo, chloroform pharmacology, enzymes
pharmacology, ethyl ethers pharmacology, filtration, heat, hydrogen-ion
concentration, staining and labeling.
Hietanen, T.E. and K.S. Wise (1976). Avian
influenza virus adapted to grow in L1210 mouse leukemia in vitro. Archives
of Virology 51(3): 243-9. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian growth and
development, adaptation, biological, cell line, leukemia L1210, mice, virus
cultivation, virus replication.
Higgins, D.A., K.F. Shortridge, and P.L. Ng (1987). Bile
immunoglobulin of the duck (Anas platyrhynchos). II. Antibody response
in influenza A virus infections. Immunology 62(3): 499-504. ISSN: 0019-2805.
NAL
Call Number: 448.3 Im6
Abstract: The capacity of the IgM-like bile
immunoglobulin (IgX) of the duck (Anas platyrhynchos) to express
antibody activity to H3N2 influenza A viruses, and the dependence of this
activity on the co-existence of serum IgM antibodies were investigated.
Ducklings infected orally and intranasally at 15-29 days of age with viruses
isolated from different host species were examined for
haemagglutination-inhibiting (HI) antibodies in biles and sera 16-29 days after
infection (p.i.). All biles had antibodies associated with IgX; all sera had
antibodies associated only with the 7.8S IgG. Following oral infection of birds
42-days-old with influenza A/duck/HK/7/75 virus, serum HI antibodies were an
initial IgM response occurring from 5-12 days p.i., followed by the appearance
of 7.8S IgG antibodies. Virus-neutralizing (VN) antibodies in serum were also
biphasic; isotype classification was not attempted. Bile IgX developed HI and
VN activity. HI antibodies reached peak titres 12 days p.i. and fell to low
levels by 24 days p.i. VN antibodies also reached peak titres 12 days p.i., but
thereafter persisted at quite high levels throughout the experiment.
Development of high titres of antibody in bile coincided with the termination
of virus excretion in faeces. These experiments confirm that bile IgX of the
duck can function as antibody in response to influenza A viruses, and that its
activity appears to be independent of serum IgM. Its possible relevance in
determining survival of virus in the intestine is discussed.
Descriptors: antibodies, viral analysis, bile immunology,
fowl plague immunology, immunoglobulins analysis, influenza A virus avian
immunology, ducks, hemagglutination inhibition tests, immunoglobulin G
analysis, immunoglobulin M analysis.
Hinshaw, V.S., D.J. Alexander, M. Aymard, P.A.
Bachmann, B.C. Easterday, C. Hannoun, H. Kida, M. Lipkind, J.S. MacKenzie, K.
Nerome, and et al. (1984). Antigenic comparisons of swine-influenza-like
H1N1 isolates from pigs, birds and humans: an international collaborative
study. Bulletin of the World Health Organization 62(6): 871-8.
ISSN: 0042-9686.
NAL
Call Number: 449.9 W892B
Descriptors: antigens, viral analysis, influenza A virus,
porcine immunology, influenza A virus immunology, antibodies, monoclonal
immunology, hemagglutination inhibition tests, hemagglutination tests, immune
sera, avian immunology, influenza A virus human immunology, porcine isolation
and purification.
Hinshaw, V.S., W.J. Bean, R.G. Webster, and G. Sriram
(1980). Genetic reassortment of influenza A viruses in the intestinal tract
of ducks. Virology 102(2): 412-419.
NAL
Call Number: 448.8 V81
Descriptors: avian influenza virus, surveys, genetic
reassortment, ducks.
Hinshaw, V.S., C.W. Olsen, N. Dybdahl Sissoko, and D.
Evans (1994). Apoptosis: a mechanism of cell killing by influenza A and B
viruses. Journal of Virology 68(6): 3667-3673. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: In previous studies, we observed that the
virulent avian influenza A virus A/Turkey/Ontario/7732/66 (Ty/Ont) induced
severe lymphoid depletion in vivo and rapidly killed an avian lymphocyte cell
line (RP9) in vitro. In examining the mechanism of cell killing by this virus,
we found that Ty/Ont induced fragmentation of the RP9 cellular DNA into a
200-bp ladder and caused ultrastructural changes characteristic of apoptotic
cell death by 5 h after infection. We next determined that the ability to
induce apoptosis was not unique to Ty/Ont. In fact, a variety of influenza A
viruses (avian, equine, swine, and human), as well as human influenza B
viruses, induced DNA fragmentation in a permissive mammalian cell line,
Madin-Darby canine kidney (MDCK), and this correlated with the development of
cytopathic effect during viral infection. Since the proto-oncogene bcl-2 is a known
inhibitor of apoptosis, we transfected MDCK cells with the human bcl-2 gene;
these stably transfected cells (MDCKbcl-2) did not undergo DNA fragmentation
after virus infection. In addition, cytotoxicity assays at 48 to 72 h after
virus infection showed a high level of cell viability for MDCKbcl-2 compared
with a markedly lower level of viability for MDCK cells. These studies indicate
that influenza A and B viruses induce apoptosis in cell cultures: thus,
apoptosis may represent a general mechanism of cell death in hosts infected
with influenza viruses.
Descriptors: dogs, avian influenza virus, equine influenza
virus, swine influenza virus, pathogenicity, DNA, pathogenesis, kidneys, cell
culture, genes, mankind, toxicity, acids, animal morphology, biological
properties, canidae, Carnivora, cell structure, chromosomes, culture
techniques, in vitro culture, influenza virus, mammals, microbial properties,
nucleic acids, nucleic compounds, nucleus, organic acids, urinary tract,
urogenital system, viruses, cell death, DNA fragmentation, bcl-2 gene,
cytopathogenicity, DNA modification, infections, cell lines, transfection, man,
cytotoxicity.
Hinshaw, V.S., R.G. Webster, and R.J. Rodriguez
(1981). Influenza A viruses: combinations of hemagglutinin and neuraminidase
subtypes isolated from animals and other sources. Archives of Virology
67(3): 191-201. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Descriptors: antigens, viral classification,
hemagglutinins viral classification, influenza A virus classification, neuraminidase
immunology, birds microbiology, epitopes, horses microbiology, avian
classification, human classification, influenza A virus immunology, swine
microbiology, terminology.
Hioe, C.E., N. Dybdahl Sissoko, M. Philpott, and V.S.
Hinshaw (1990). Overlapping cytotoxic T-lymphocyte and B-cell antigenic
sites on the influenza virus H5 hemagglutinin. Journal of Virology
64(12): 6246-51. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: To define the recognition site of cytotoxic T
lymphocytes (CTLs) on influenza virus H5 hemagglutinin (HA), an H5 HA-specific
CTL clone was examined for the ability to recognize monoclonal
antibody-selected HA variants of influenza virus A/Turkey/Ontario/7732/66
(H5N9). On the basis of 51Cr release assays with the variants, a CTL epitope
was located near residue 168 of H5 HA. To define the epitope more precisely, a
series of overlapping peptides corresponding to this region was synthesized and
tested for CTL recognition. The minimum peptide recognized by the CTL clone
encompassed residues 158 to 169 of H5 HA. Relative to the H3 HA
three-dimensional structure, this CTL epitope is located near the distal tip of
the HA molecule, also known as a major B-cell epitope on H3 HA. A single
mutation at residue 168 (Lys to Glu) in the H5 HA variants abolished CTL
recognition; this same amino acid was shown previously to be critical for
B-cell recognition (M. Philpott, C. Hioe, M. Sheerar, and V. S. Hinshaw, J.
Virol. 64:2941-2947, 1990). Additionally, mutations within this region of the
HA molecule were associated with attenuation of the highly virulent
A/Turkey/Ontario/7732/66 (H5N9) (M. Philpott, B. C. Easterday, and V.S.
Hinshaw, J. Virol. 63:3453-3458, 1989). When tested for recognition of other H5
viruses, the CTL clone recognized the HA of A/Turkey/Ireland/1378/83 (H5N8) but
not that of A/Chicken/Pennsylvania/1370/83 (H5N2), even though these viruses
contain identical HA amino acid 158-to-169 sequences. These results suggest
that differences outside the CTL epitope affected CTL recognition of the intact
HA molecule. The H5 HA site defined in these studies is, therefore, important
in both CTL and B-cell recognition, as well as the pathogenesis of the virus.
Descriptors: B lymphocytes immunology, epitopes
immunology, hemagglutinins viral immunology, influenza A virus avian
immunology, T lymphocytes, cytotoxic immunology, amino acid sequence, cell
line, chickens, cytotoxicity, immunologic, hemagglutinin glycoproteins,
influenza virus, hemagglutinins viral genetics, avian genetics, mice, mice
inbred BALB c, molecular models, molecular sequence data, mutagenesis, site
directed, protein conformation, turkeys, variation genetics.
Hirabayashi, T., H. Ochiai, S. Sakai, K. Nakajima,
and K. Terasawa (1995). Inhibitory effect of ferulic acid and isoferulic
acid on murine interleukin-8 production in response to influenza virus
infections in vitro and in vivo. Planta
Medica 61(3): 221-6. ISSN:
0032-0943.
NAL
Call Number: 450 P697
Abstract: We investigated the effect of ferulic acid (FA)
and isoferulic acid (IFA), which are active components of the rhizoma of
Cimicifuga species used frequently as anti-inflammatory drugs in Japanese
Oriental medicines, on murine interleukin-8 (IL-8) production in response to
influenza virus infections in vitro and in vivo by antibody-sandwich
enzyme-linked immunosorbent assay. In the in vitro study, the murine macrophage
cell line RAW 264.7 was infected with influenza virus at a dose of 10 plaque
forming units (PFU)/cell and cultured in the presence or absence of drugs. Both
FA and IFA reduced the IL-8 levels in the 20-h conditioned medium in comparison
with control in a dose-dependent manner. The effect of IFA was greater than
that of FA: IL-8 levels were reduced to 43% and 56% of the control in the presence
of 100 micrograms/ml of IFA and FA, respectively. In the in vivo study, mice
were infected with 1,000 PFU of virus and received daily oral administrations
of Cimicifuga heracleifolia extract (5 mg/mouse/day), FA (0.5
mg/mouse/day), IFA (0.125 mg/mouse/day), or phosphate buffered saline. The
three drugs showed a tendency to reduce IL-8 levels in bronchoalveolar lavage
(BAL) obtained 2 days after infection. Moreover, both FA and IFA also
significantly reduced the number of exuded neutrophils into BAL. However, the
drug administrations did not affect the virus yields in BAL. These data suggest
that FA and IFA are novel and potent inhibitors of murine IL-8 production and
might act as one of the main components of anti-inflammatory rhizoma of
Cimicifuga species.
Descriptors: cinnamates pharmacology, coumaric acids
pharmacology, influenza immunology, influenza A virus avian immunology,
interleukin 8 biosynthesis, antihypertensive agents pharmacology, cell line,
chick embryo, lipopolysaccharides pharmacology, lung virology, macrophages drug
effects, macrophages immunology, mice, mice inbred ICR, neutrophils drug
effects, neutrophils physiology, medicinal plants, plants.
Hiti, A.L., A.R. Davis, and D.P. Nayak (1981). Complete
sequence analysis shows that the hemagglutinins of the H0 and H2 subtypes of
human influenza virus are closely related. Virology 111(1):
113-24. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus human immunology, amino acid sequence, base sequence, DNA,
viral, avian immunology, human classification, human genetics.
Hof, H. and H.J. Gerth (1972). Independence of
release of influenza A viruses from protein synthesis. Brief report. Archiv
Fur Die Gesamte Virusforschung 37(2): 293-6. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: hemagglutinins viral biosynthesis,
orthomyxoviridae metabolism, chick embryo, cycloheximide pharmacology,
fibroblasts microbiology, hemadsorption, hemagglutination tests, influenza A
virus avian growth and development, avian isolation and purification, avian
metabolism, orthomyxoviridae growth and development, orthomyxoviridae isolation
and purification, time factors, tissue culture, viral proteins biosynthesis.
Hoffmann, E., S. Krauss, D. Perez, R. Webby, and R.G.
Webster (2002). Eight-plasmid system for rapid generation of influenza virus
vaccines. Vaccine 20(25-26): 3165-70. ISSN: 0264-410X.
NAL
Call Number: QR189.V32
Descriptors: genetic vectors genetics, influenza A virus
avian genetics, human genetics, influenza vaccine biosynthesis, reassortant
viruses genetics, antigenic variation genetics, birds virology, cell line,
chick embryo, China, Czechoslovakia, DNA, recombinant genetics, dogs, genes
viral, avian immunology, avian isolation and purification, human immunology,
human isolation and purification, influenza vaccine genetics, influenza vaccine
immunology, influenza vaccine isolation and purification, New Caledonia,
Panama, phenotype, reassortant viruses immunology, reassortant viruses
isolation and purification, reproducibility of results, reverse transcriptase
polymerase chain reaction, transfection, virus cultivation.
Hoffmann, E., G. Neumann, Y. Kawaoka, G. Hobom, and
R.G. Webster (2000). A DNA transfection system for generation of influenza A
virus from eight plasmids. Proceedings of the National Academy of
Sciences of the United States of America 97(11): 6108-13. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: We have developed an eight-plasmid DNA
transfection system for the rescue of infectious influenza A virus from cloned
cDNA. In this plasmid-based expression system, viral cDNA is inserted between
the RNA polymerase I (pol I) promoter and terminator sequences. This entire pol
I transcription unit is flanked by an RNA polymerase II (pol II) promoter and a
polyadenylation site. The orientation of the two transcription units allows the
synthesis of negative-sense viral RNA and positive-sense mRNA from one viral
cDNA template. This pol I-pol II system starts with the initiation of
transcription of the two cellular RNA polymerase enzymes from their own
promoters, presumably in different compartments of the nucleus. The interaction
of all molecules derived from the cellular and viral transcription and
translation machinery results in the generation of infectious influenza A
virus. The utility of this system is proved by the recovery of the two
influenza A viruses: A/WSN/33 (H1N1) and A/Teal/HK/W312/97 (H6N1). Seventy-two
hours after the transfection of eight expression plasmids into cocultured 293T
and MDCK cells, the virus yield in the supernatant of the transfected cells was
between 2 x 10(5) and 2 x 10(7) infectious viruses per milliliter. We also used
this eight-plasmid system for the generation of single and quadruple
reassortant viruses between A/Teal/HK/W312/97 (H6N1) and A/WSN/33 (H1N1).
Because the pol I-pol II system facilitates the design and recovery of both
recombinant and reassortant influenza A viruses, it may also be applicable to
the recovery of other RNA viruses entirely from cloned cDNA.
Descriptors: DNA, complementary genetics, viral genetics,
influenza A virus avian genetics, human genetics, plasmids genetics,
transfection methods, base sequence, cell line, dogs, avian growth and
development, human growth and development, molecular sequence data, promoter
regions genetics, RNA polymerase I genetics, polymerase II genetics, messenger
biosynthesis, RNA viral biosynthesis, recombination, genetic, regulatory
sequences nucleic acid, transcription, genetic.
Holt, P. and J. Latimer (1989). Stimulatory
effects of avian influenza virus on chicken lymphocytes. FASEB Journal,
Federation of American Societies for Experimental Biology 3(4): A1340.
NAL
Call Number: QH301.F3
Descriptors: lymphocytes, avian influenza virus, chicken.
Holt, P.S. (1990). Enhancement of chicken
lymphocyte activation and lymphokine release by avian influenza virus. Developmental
and Comparative Immunology 14(4): 447-55.
ISSN: 0145-305X.
NAL
Call Number: QR180.D4
Abstract: We had previously found that inactivated
avian influenza virus (AIV) could enhance the response of chicken lymphocytes
to mitogen or antigen activation. An investigation into the possible mechanisms
of this enhancement was undertaken. Peripheral blood lymphocytes (PBL) were
incubated with AIV expressing different hemagglutinin (HA) types (H1-H13) along
with doses of concanavalin A (Con A) which induce maximum (0.5 microgram) or
submaximum (0.125 microgram) PBL activation. The lymphocyte activation was
measured 72 h later. All of the HA types except H13 enhanced the Con A
response. Diminished but significant enhancement could be observed when AIV
administration was delayed by as much as 48 h of the 72-h incubation time. The
AIV A/ck/Ala/75 (H4N8) was also examined for its effect on interleukin 2 (IL 2)
synthesis by Con A-activated PBL and was found to modestly increase the
synthesis of this lymphokine. All of the AIV hemagglutinin types agglutinated
the PBL with titers slightly lower than that observed for the chicken
erythrocyte agglutination. These results indicate that the AIV-induced
enhancement of Con A responsiveness by chicken PBL is due, at least partly, to
increased synthesis of IL 2 and that the effect may be due to some viral
component other than the agglutinin.
Descriptors: influenza A virus avian immunology,
interleukin 2 secretion, lymphocyte activation, agglutination, chickens,
concanavalin a pharmacology, hemagglutination, viral, avian classification,
lymphocytes immunology, species specificity.
Holt, P.S. and J.W. Latimer (1989). Stimulatory
effect of avian influenza virus on chicken lymphocytes. Avian Diseases
33(4): 743-9. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: A study was conducted to examine the effect
of avian influenza virus (AIV) on chicken lymphocyte activation. Unprimed or Brucella
abortus antigen (Ag)-primed lymphocytes were incubated with various doses
of the T-cell mitogen concanavalin A (Con A) or Ag, respectively, plus serial
dilutions of inactivated AIV for 72 hr, and cell proliferation was measured via
uptake of tritiated thymidine. AIV enhanced the proliferative response to Con A
or Ag by 150% or better, and the enhancement decreased in a viral
dose-dependent manner. The effects were more readily observed in cells that had
not been maximally activated by the Con A or Ag. The enhanced response was
observed in lymphocytes from both white rock and white leghorn breeds of
chicken and in mature peripheral blood lymphocytes or immature thymocytes. The
viral activity could be abrogated by pre-treatment of the viral preparation
with AIV-specific antisera or prior adsorption of the AIV with chicken
erythrocytes. These results indicate that AIV can interact with and modify the
in vitro activity of chicken lymphocytes and may exert modulatory effects on
the avian immune system.
Descriptors: chickens immunology, lymphocyte activation
immunology, lymphocytes immunology, orthomyxoviridae pathogenicity, chickens
microbiology, concanavalin A, erythrocytes immunology, specific pathogen free
organisms.
Hooper, P.T. (1989). Lesions in chickens
experimentally infected with 1985 H7N7 avian influenza virus. Australian
Veterinary Journal 66(5): 155-156.
ISSN: 0005-0423.
NAL
Call Number: 41.8 Au72
Abstract: In groups receiving intranasal inoculations,
22 of 24 birds became affected. Illnesses were usually less than 2 d with
clinical signs generally depression and dullness. Examination of lesions showed
that this strain of virus produced in the laboratory a consistent,
characteristic disease pattern, affecting predominantly the bursa of Fabricius,
the pancreas and the brain.
Descriptors: chickens, avian influenza virus, wounds,
pathology, birds, domestic animals, domesticated birds, Galliformes, influenza
virus, lesions, livestock, poultry, useful animals, viruses.
Hooper, P.T., G.W. Russell, P.W. Selleck, and W.L.
Stanislawek (1995). Observations on the relationship in chickens between the
virulence of some avian influenza viruses and their pathogenicity for various
organs. Avian Diseases 39(3): 458-464. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Comparative histological and
immunocytochemical studies were conducted on formalin-fixed tissues from
chickens infected with avian influenza viruses of varying virulence. Results
showed a distinct pattern of disease that depended on the virulence of the
virus and the susceptibility of the birds. At 3 days post-intranasal
inoculation with a highly virulent H7N7 virus, all 6-to-8-week-old
specific-pathogen-free (SPF) birds were affected, and all developed pancreatic
necrosis and encephalitis associated with specific immunoperoxidase staining.
Other same-aged SPF birds were only occasionally affected 6 to 8 days after
intravenous inoculation with almost avirulent H4N4, H6N2, or H3N8 virus.
Specific lesions and immunoperoxidase staining were noted in the kidneys only.
The H7N7 virus in older commercial birds and an H7N3 virus in young SPF and
older commercial birds caused intermediate mortality rates at 4 to 11 days
postinoculation, and there was a broad range of lesions and specific
immunoperoxidase staining in the pancreas, brain, kidney, heart, and skeletal
muscle. Two exceptional birds had immunostaining of small blood vessels
throughout their bodies with or without lesions or staining in the tissues,
which may have represented a transitory pre-localizing phase occurring in many
birds. There was necrosis without virus antigen detection in the bursae,
thymuses, and cecal tonsils, possibly secondary to stress or only transitory
infection of virus. These data indicate that rapid, retrospective diagnosis of
avian influenza in fixed tissues is possible by using an immunoperoxidase test
on pancreas, brain, and kidney.
Descriptors: chickens, avian influenza virus,
pathogenicity, disease resistance, body parts, animal tissues, antigens,
histopathology, immunology, biological properties, birds, body parts, domestic
animals, domesticated birds, Galliformes, immunological factors, influenza
virus, livestock, microbial properties, orthomyxoviridae, pathology, poultry,
resistance to injurious factors, useful animals, viruses, susceptibility, viral
antigens, immunocytochemistry.
Horimoto, T., T. Ito, D.J. Alexander, and Y. Kawaoka
(1995). Cleavability of hemagglutinin from an extremely virulent strain of
avian influenza virus containing a unique cleavage site sequence. Journal
of Veterinary Medical Science the Japanese Society of Veterinary Science
57(5): 927-30. ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Abstract:
An avian influenza virus,
A/turkey/England/50-92/91 (H5N1), showed extremely high virulence in chickens,
although its hemagglutinin (HA) cleavage site sequence (R-K-R-K-T-R), having a
nonbasic (Thr) residue at the second position (P-2) from the carboxyl terminus
of HA1, does not conform to the previously established consensus sequence
motif, X-X-R/K-X-R/K-R (X = nonbasic residue), for highly virulent phenotype of
the H5 virus. When we evaluated the HA cleavability of this strain in chicken
embryo fibroblast culture, we observed that, unlike other HAs with a Thr
residue at P-2, this HA was efficiently cleaved. These findings suggest that a
nonbasic residue at the P-2 does not affect its recognition and catalyzation by
cleavage enzymes that are otherwise influenced by steric structure around the
cleavage site.
Descriptors: chickens virology, fowl plague virology,
hemagglutinins viral metabolism, influenza A virus avian pathogenicity, turkeys
virology, amino acid sequence, cultured cells, chick embryo, fibroblasts
cytology, fibroblasts virology, hemagglutinins viral chemistry, molecular
sequence data, virulence.
Horimoto, T. and Y. Kawaoka (1997). Biologic
effects of introducing additional basic amino acid residues into the
hemagglutinin cleavage site of a virulent avian influenza virus. Virus
Research 50(1): 35-40. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: We mutated the virulent avian influenza virus
A/turkey/Ontario/7732/66 (H5N9)[Q-R-R-R-K-K-R?G at the hemagglutinin (HA)
cleavage site] to create a mutant, R(MO-0), with additional basic residues at
this site (Q-R-R-R-R-R-K-K-R?G) by reverse genetics. When tested in chicken
embryo fibroblast culture, this mutant showed reduced HA cleavability compared
to that of the wild-type virus, but its plaque size was not appreciably
altered. Virulence of the R(MO-0) virus in chickens was lower than that of the
wild-type virus. These findings indicate that addition of excessive basic
residues to an optimal recognition sequence for HA cleavage enzymes at the
cleavage site is deleterious for HA cleavability. Previously, we showed that a
mutant containing the suboptimal HA cleavage site sequence for cleavage enzyme
recognition also had reduced HA cleavability and virulence compared to the
wild-type virus. We conclude that the data presented here further substantiate
our belief that the level of HA cleavability correlates with the degree of
virulence when all other genetic characteristics are considered equal,
irrespective of the mechanisms by which HA cleavability is reduced.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian genetics, avian pathogenicity, administration, intranasal, chick
embryo, chickens, fowl plague virology, hemagglutinins viral chemistry,
hemagglutinins viral genetics, avian chemistry, injections, intramuscular,
mutagenesis, site directed, plaque assay.
Horimoto, T. and Y. Kawaoka (1995). The
hemagglutinin cleavability of a virulent avian influenza virus by
subtilisin-like endoproteases is influenced by the amino acid immediately
downstream of the cleavage site. Virology 210(2): 466-470. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Many viral membrane glycoproteins are
post-translationally processed by intracellular endoproteases such as
subtilisin-like proteases. These proteases recognize a cleavage site sequence
comprising basic amino acids positioned upstream of the cleavage site of the
viral proteins. Here, we mutated the glycine residue immediately downstream of
the cleavage site (P1) of hemagglutinin (HA) from a virulent avian influenza
virus, A/turkey/Ontario/7732/66 (H5N9) (R-R-R-K-K-R/G), to examine the effect
of this mutation on its cleavability. Substitution of Gly with Ile, Leu, Val,
or Pro, but not Ala, Asp, Phe, His, Ser, or Thr, resulted in substantial
reduction of HA cleavage by endogenous endoproteases in CV-1 cells and by
vaccinia-expressed PC6 and, albeit to a lesser extent, furin. We conclude that
HA cleavage by subtilisin-like proteases is influenced by the downstream P1
amino acid in the absence of upstream cleavage site sequence alterations.
Descriptors: avian influenza virus, agglutinins, chemical
composition, mutation, proteases, proteolysis, pathogenicity, biological
properties, chemical reactions, enzymes, genetics, hydrolases, hydrolysis,
influenza virus, microbial properties, orthomyxoviridae, proteins, viruses,
viral hemagglutinins, amino acid sequences, proteinases, virulence.
Horimoto, T. and Y. Kawaoka (1995). Molecular
changes in virulent mutants arising from avirulent avian influenza viruses
during replication in 14-day-old embryonated eggs. Virology 206(1):
755-759. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The emergence of virulent avian influenza
viruses in poultry is unpredictable. To gain insight into the mechanism for
this event, we sought to identify the molecular changes in virulent mutants
that occur during replication in 14-day-old embryonated chicken eggs. After
three passages in 14-day-old eggs, avirulent H5 viruses with the K/R-K-K/T-R
sequence at the hemagglutinin (HA) cleavage site became virulent in chickens,
concomitantly acquiring high HA cleavability, whereas those with the R-E-T-R
sequence did not. None of the test viruses converted to a virulent phenotype
when passaged in 10-day-old eggs. Nucleotide sequence analysis indicated that
the virulent mutants either lost a glycosylation site near the HA cleavage site
or acquired an additional arginine at the latter. Avirulent viruses that became
virulent after passage in older eggs included an H5N2 avian strain with the
R-K-T-R sequence that was isolated in 1993, indicating that viruses with this
sequence motif, which are currently circulating in bird populations, should be
considered potentially virulent. Failure to generate virulent mutants from
viruses with R-E-T-R at the HA cleavage site underscores the pathogenic
heterogeneity among avian influenza viruses.
Descriptors: chicks, avian influenza virus,
pathogenicity, mutants, agglutinins,
nucleotide sequence, chemical composition, biological properties, birds,
chickens, domestic animals, domesticated birds, Galliformes, genomes, influenza
virus, livestock, microbial properties, orthomyxoviridae, poultry, progeny,
proteins, useful animals, viruses, young animals, virus replication, cleavage site, virulence,
viral hemagglutinins, amino acid sequences.
Horimoto, T. and Y. Kawaoka (1998). A possible
mechanism for selection of virulent avian influenza A viruses in 14-day-old
embryonated eggs. Journal of Veterinary Medical Science the Japanese
Society of Veterinary Science 60(2): 273-5.
ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Abstract: The emergence of virulent avian influenza
viruses in poultry is unpredictable. To gain insight into the mechanism of this
event, we previously examined the possible role of older (14-day-old)
embryonated eggs, in which virulent mutants were preferably selected (Horimoto
and Kawaoka, Virology 206: 755-759, 1995). However, it is unknown why virulent mutants
replicate predominantly in older eggs. In the present study, we compared
protease activities responsible for cleavage activation of the hemagglutinin
(HA) in allantoic fluids in 10-day and 14-day-old eggs. In vitro assays showed
that the protease activities were stronger in the 14-day-old than 10-day-old
eggs. The allantoic fluids with strong protease activity degraded HA. These
results indicate that replication of avirulent viruses is hampered in older
eggs, while that of virulent viruses whose HAs are activated by other
intracellular proteases was not, possibly leading to a replicative advantage
for virulent mutants in the older eggs.
Descriptors: influenza A virus avian pathogenicity, avian
physiology, virulence, virus replication, allantois physiology, allantois
virology, chick embryo, chickens, endopeptidases metabolism, glycosylation,
hemagglutinins viral chemistry, hemagglutinins viral genetics, hemagglutinins
viral physiology, avian isolation and purification, kinetics, mutation,
polymerase chain reaction, substrate specificity.
Horimoto, T. and Y. Kawaoka (1994). Reverse
genetic provides direct evidence for a correlation of hemagglutinin
cleavability and virulence of an avian influenza A virus. Journal of
Virology 68(5): 3120-3128. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: To obtain direct evidence for a relationship
between hemagglutinin (HA) cleavability and the virulence of avian influenza A
viruses, we generated a series of HA cleavage mutants from a virulent virus,
A/turkey/ Ontario/7732/66 (H5N9), by reverse genetics. A transfectant virus
containing the wild-type HA with R-R-R-K-K-R at the cleavage site, which was
readily cleaved by endogenous proteases in chicken embryo fibroblasts (CEF),
was highly virulent in intramuscularly or intranasally/orally inoculated
chickens. By contrast, a mutant containing the HA with an avirulent-like
sequence (R-E-T-R) at the cleavage site, which was not cleaved by the proteases
in CEF, was avirulent in chickens, indicating that a genetic alteration
confined to the HA cleavage site can affect cleavability and virulence. Mutant
viruses with HA cleavage site sequences of T-R-R-K-K-R or T-T-R-K-K-R were as
virulent as viruses with the wild-type HA, whereas a mutant with a
two-amino-acid deletion but retention of four consecutive basic residues
(R-K-K-R) was as avirulent as a virus with the avirulent-type HA.
Interestingly, although a mutant containing an HA with R-R-R-K-T-R, which has
reduced cleavability in CEF, was as virulent as viruses with high HA
cleavability when given intramuscularly, it was less virulent when given
intranasally/orally. We conclude that the degree of HA cleavability in CEF
predicts the virulence of avian influenza viruses.
Descriptors: chickens, avian influenza virus, agglutinins,
proteolysis, mutants, induced mutation, pathogenicity, biological properties,
birds, chemical reactions, domestic animals, domesticated birds, Galliformes,
genetics, hydrolysis, influenza virus, livestock, microbial properties,
mutation, poultry, progeny, proteins,
useful animals, viruses, posttranslational proteolysis, viral hemagglutinins,
amino acid sequences.
Horimoto, T., K. Nakayama, S.P. Smeekens, and Y.
Kawaoka (1994). Proprotein-processing endoproteases PC6 and furin both
activate hemagglutinin of virulent avian influenza viruses. Journal of
Virology 68(9): 6074-6078. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Among the proprotein-processing
subtilisin-related endoproteases, furin has been a leading candidate for the
enzyme that activates the hemagglutinin (HA) of virulent avian influenza
viruses. In the present study, we examined the cleavage activity of two other
recently isolated ubiquitous subtilisin-related proteases, PACE4 and PC6, using
wild-type HA of A/turkey/Ireland/1378/83 (H5N8) and a series of its mutant HAs.
Vaccinia virus-expressed wild-type HA was not cleaved in human colon
adenocarcinoma LoVo cells, which lack active furin. This processing defect was
correlated by the expression of furin and PC6 but not of PACE4 and a control
wild-type vaccinia virus. PC6 showed a sequence specificity similar to that
with the endogenous proteases in cultured cells. When LoVo cells were infected
with a virulent avian virus, A/turkey/Ontario/7732/66 (H5N9), only noninfectious
virions were produced because of the lack of HA cleavage. However, when the
cells were coinfected with vaccinia virus that expressed either furin or PC6,
the avian virus underwent multiple cycles of replication, indicating that both
furin and PC6 specifically cleave the virulent virus HA at the authentic site.
These data suggest that PC6, as well as furin, can activate virulent avian
influenza virus in vivo implying the presence of multiple HA cleavage enzymes
in animals.
Descriptors: avian influenza virus, agglutinins,
proteolysis, proteases, chemical reactions, enzymes, hydrolases, hydrolysis, influenza virus,
proteins, viruses, proteolytic activation, proteolytic cleavage, viral
hemagglutinins, precursors, proteinases.
Horimoto, T., E. Rivera, J. Pearson, D. Senne, S.
Krauss, Y. Kawaoka, and R.G. Webster (1995). Origin and molecular changes
associated with emergence of a highly pathogenic H5N2 influenza virus in
Mexico. Virology 213(1): 223-230.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: In October of 1993, there was decreased egg
production and increased mortality among Mexican chickens, in association with
serologic evidence of an H5N2 influenza virus. First isolated from chickens in
May of 1994, after spreading widely in the country, the virus caused only a
mild respiratory syndrome in specific pathogen-free chickens. Because
eradication of the virus by destruction of infected birds posed major obstacles
to the poultry industry in Mexico, we were able to conduct a "field
experiment" to determine the fate of an avirulent virus after repeated
cycles of replication in millions of chickens. By the end of 1994, the virus
had mutated to contain a highly cleavable hemagglutinin (HA), but remained only
mildly pathogenic in chickens. Within months, however, it had become lethal in
poultry. Nucleotide sequence analysis of the HA cleavage site of the original
avirulent strain revealed R-E-T-R, typical of avirulent viruses and unlike the
K-K-K-R sequence characterizing viruses responsible for the 1983 outbreak in
poultry in the United States. Both mildly and highly pathogenic isolates
contained insertions and a substitution of basic residues in the HA connecting
peptide, R-K-R-K-T-R, which made the HA highly cleavable in trypsin-free
chicken embryo fibroblasts. Phylogenetic analysis of the HA of H5 avian
influenza viruses, including the Mexican isolates, indicated that the epidemic
virus had originated from the introduction of a single virus of the North
American lineage into Mexican chickens. This sequence of events demonstrates,
apparently for the first time, the stepwise acquisition of virulence by an
avian influenza virus in nature.
Descriptors: chickens, Mexico, United States, avian
influenza virus, agglutinins, pathogenicity, chemical composition, phylogeny,
America, biological properties, birds, domestic animals, domesticated birds,
evolution, Galliformes, influenza virus, Latin America, livestock, microbial
properties, North America, orthomyxoviridae, poultry, proteins, useful animals,
viruses, cleavage site, viral hemagglutinins, virulence, amino acid sequences,
outbreaks.
Horisberger, M.A. (1982). Identification of a
catalytic activity of the large basic P polypeptide of influenza virus. Virology
120(2): 279-86. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, viral proteins metabolism, base sequence, cytidine triphosphate
metabolism, DNA directed RNA polymerases metabolism, guanosine triphosphate
metabolism, kinetics, mutation, messenger biosynthesis, temperature.
Horisberger, M.A., G.K. McMaster, H. Zeller, M.G.
Wathelet, J. Dellis, and J. Content (1990). Cloning and sequence analyses of
cDNAs for interferon- and virus-induced human Mx proteins reveal that they
contain putative guanine nucleotide-binding sites: functional study of the
corresponding gene promoter. Journal of Virology 64(3):
1171-81. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The human protein p78 is induced and
accumulated in cells treated with type I interferon or with some viruses. It is
the human homolog of the mouse Mx protein involved in resistance to influenza
virus. A full-length cDNA clone encoding the human p78 protein was cloned and
sequenced. It contained an open reading frame of 662 amino acids, corresponding
to a polypeptide with a predicted molecular weight of 75,500, in good agreement
with the Mr of 78,000 determined on sodium dodecyl sulfate gels for the
purified natural p78 protein. The cloned gene was expressed in vitro and corresponded
in size, pI, antigenic determinant(s), and NH2 terminus sequence to the natural
p78 protein. A second cDNA was cloned which encoded a 633-amino-acid protein
sharing 63% homology with human p78. This p78-related protein was translated in
reticulocyte lysates where it shared an antigenic determinant(s) with p78. A
putative 5' regulatory region of 83 base pairs contained within the gene
promoter region upstream of the presumed p78 mRNA cap site conferred human
alpha interferon (IFN-alpha) inducibility to the cat reporter gene. The p78
protein accumulated to high levels in cells treated with IFN-alpha. In
contrast, the p78-related protein was not expressed at detectable levels. The
rate of decay of p78 levels in diploid cells after a 24-h treatment with
IFN-alpha was much slower than the rate of decay of the antiviral state against
influenza A virus and vesicular stomatitis virus, suggesting that the p78
protein is probably not involved in an antiviral mechanism. Furthermore, we
showed that these proteins, as well as the homologous mouse Mx protein, possess
three consensus elements in proper spacing, characteristic of GTP-binding
proteins.
Descriptors: DNA genetics, gtp binding proteins, genes,
structural, guanine nucleotides metabolism, influenza A virus genetics,
interferon type I, recombinant pharmacology, promoter regions genetics,
proteins genetics, vesicular stomatitis Indiana virus genetics, virus
inhibitors genetics, amino acid sequence, base sequence, binding sites, cell
line, cloning, molecular, DNA isolation and purification, Escherichia coli
genetics, gene library, influenza A virus avian genetics, molecular sequence
data, molecular weight, proteins biosynthesis, proteins metabolism, RNA,
messenger genetics, sequence homology, nucleic acid, transcription, genetic.
Huang Jianwen, Jiang Yanfen, and He Weimin (2002). Effects
of the transfer factor on artificial infected chickens by AIV. Journal
of Gansu Agricultural University (China). Gansu Nongye Daoxue Xuebao (China)
37(2): 170 173. ISSN: 1003-4315.
NAL
Call Number: S471.C62K352
Descriptors: transfer factor, avian influenza virus,
chickens.
Huang, R.T. (1974). Adsorption of influenza virus
to charged groups on natural and artificial surfaces. Medical
Microbiology and Immunology 159(2): 129-35.
ISSN: 0300-8584.
Descriptors: adsorption, influenza A virus avian
immunology, anions, cations, divalent, cations, monovalent, erythrocytes,
hemagglutination.
Huang, R.T. (1976). Labeling of animal
cells with fluorescent dansyl cerebroside. Zeitschrift Fur
Naturforschung. Section C Biosciences 31(11-12): 737-40. ISSN: 0341-0382.
NAL
Call Number: QH301.Z4
Abstract: A dansyl (diaminoaphthalenesulfonyl)-derivative
of cerebroside was prepared which could be effectively incorporated into the
plasma membranes of tissue culture cells and erythrocytes. The cells which had
assimilated the glycolipid fluoreced intensely and could be observed under a
fluorescent microscope. Cells were initially labeled rather homogeneously over
the whole surface. With longer incubation time organization of the fluorescent
glycolipid took place and patches of the lipid in the membrane were formed. The
redistribution and organization of the membrane lipid could be demonstrated
most clearly when cells labeled with this fluorescent glycolipid were infected
with myxoviruses. After infection of MDBK and BHK cells with fowl plaque virus
areas of dense fluorescence appeared at margines of neighboring cells. When BHK
cells were infected with Newcastle disease virus fusion of the cells was
accompanied by complete redistribution of the glycolipid. Erythrocytes could
also easily incorporate dansyl cerebroside. Chicken erythrocytes which contain cytoplsmic
and nuclear membranes incorporated the fluorescent glycolipid in both
membranes.
Descriptors: cerebrosides blood, dansyl compounds,
erythrocytes metabolism, binding sites, cell line, cell membrane metabolism,
cell membrane ultrastructure, chickens, erythrocyte membrane metabolism,
erythrocyte membrane ultrastructure, fluorescent dyes, influenza A virus avian,
Newcastle disease virus, spectrometry, fluorescence.
Huang, R.T. (1991). On the penetration mechanism
of influenza viruses. Behring Institute Mitteilungen (89):
23-6. ISSN: 0301-0457.
NAL
Call Number: QR180.B4
Abstract: The envelopes of influenza viruses contain in
addition to lipids also two glycoproteins, the hemagglutinin and the
neuraminidase, that are responsible for the adsorption, receptor splitting,
penetration and budding processes of these viruses. In this article, hypotheses
presented in the past with regard to the virus penetration are reconsidered.
Based on results obtained with the fowl plague virus (influenza A/FPV/Rostock/34,
H7N1) and MDCK-cells, we conclude that a fusion between the viral envelope and
the plasma membrane is the initial step of virus entry.
Descriptors: influenza A virus avian physiology, membrane
fusion, cell line, cell membrane physiology, hemagglutination, viral envelope
proteins metabolism.
Huang, R.T. (1976). On the structure of the
carbohydrate chains of different strains of the influenza virus. Medical
Microbiology and Immunology 162(3-4): 169-73. ISSN: 0300-8584.
Abstract: Structural features of the glycosyl chains of
the influenca virus have been determined. It was found that fucose was solely
terminal, whereas mannose and galactose were present at the terminal as well as
subterminal and core positions. Mannose and glucose molecules were shown to be
branching points in the glycosyl chains. Furthermore, linkage positions of
carbohydrates within the chains were characterized.
Descriptors: carbohydrates analysis, influenza A virus
avian analysis, orthomyxoviridae analysis, fucose analysis, galactose analysis,
glucose analysis, mannose analysis.
Huang, R.T. (1983). The role of neutral
glycolipids and phospholipids in myxovirus-induced membrane fusion. Lipids
18(7): 489-92. ISSN: 0024-4201.
NAL
Call Number: QP751.L5
Abstract: Myxoviruses (influenza virus and
paramyxovirus) enter host cells by two successive steps consisting of
attachment and fusion between viral and cellular membranes. The initial
attachment is known to occur through specific binding of the viruses with the
neuraminic acid-containing receptors of cellular membranes. Evidence is
presented here that, in the following step of membrane fusion, neutral
glycolipids terminating in galactose and certain phospholipids (primarily
lecithin and sphingomyelin) interact with the viral envelopes and that this
interaction may be fundamental to the fusion process.
Descriptors: cell membrane physiology, glycolipids
physiology, influenza A virus avian physiology, membrane lipids physiology,
parainfluenza virus 1, human physiology, phospholipids physiology, receptors,
virus physiology, chick embryo,
glycolipids pharmacology, hemolysis drug effects, phospholipids pharmacology,
receptors, virus drug effects.
Huang, R.T. (1976). Sphingolipids of influenza
viruses. Biochimica Et Biophysica Acta 424(1): 90-7. ISSN: 0006-3002.
NAL
Call Number: 381 B522
Abstract: Total lipid of four egg grown influenza
viruses (A2-Asia, A2-England, A2-Taiwan and fowl plague virus) were extracted
with chloroform-methanol. After mild alkali treatment of the extracts,
glycosphingolipids and sphingomyelin were separated by a silicic acid column,
and finally purified by thin layer chromatography. Fatty acid, sphingosine and
carbohydrate components of individual lipid classes were then analysed by
gas-liquid chromatography. Nearly identical results were obtained with all
viruses investigated. Approximately 20% of the total lipid was
monohexosylceramide, distributed equally between glucosyl- and galactosyl-
analogues. Lactosylceramide and oligohexosylceramides were found in much
smaller concentrations (approx. 2%). About 15% of the total lipid was
attributed to sphingomyelin. A large proportion of fatty acids (around 25% in
sphingomyelin and 60% in glycolipids) belonged to the long chain (C19-C26)
normal- and 2-hydroxy series. C18-sphingosine was found to be the only base
present in all lipid classes investigated.
Descriptors: influenza A virus avian analysis,
orthomyxoviridae analysis, sphingolipids analysis, fatty acids analysis,
hexoses analysis, oligosaccharides analysis, sphingomyelins analysis.
Huang, R.T. and E. Dietsch (1988). Anti-influenza
viral activity of aspirin in cell culture. New England Journal of
Medicine 319(12): 797. ISSN:
0028-4793.
NAL
Call Number: 448.8 N442
Descriptors: antiviral agents pharmacology, aspirin
pharmacology, influenza A virus avian drug effects, human drug effects,
cultured cells.
Huang, R.T., E. Dietsch, and R. Rott (1985). Further
studies on the role of neuraminidase and the mechanism of low pH dependence in
influenza virus-induced membrane fusion. Journal of General Virology
66(Pt. 2): 295-301. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The role of neuraminidase and the mechanism
of low pH dependence in influenza virus-induced membrane fusion have been
studied further using fowl plague virus (FPV, H7N1). Two specific anti-FPV
neuraminidase antisera obtained from chickens immunized with recombinant virus
strains inhibited viral neuraminidase activity without influencing its
haemagglutinating activity. These sera totally inhibited the FPV-induced fusion
of erythrocytes and partially reduced haemolysis. But both fusion and
haemolysis activities could be restored by external addition of Vibrio cholerae
neuraminidase, indicating participation of neuraminidase in FPV-induced
membrane fusion. With regard to low pH-dependent fusion by influenza virus, it
was found that erythrocytes of various species showed different pH optima for
haemolysis by FPV and that erythrocytes could be sensitized for fusion and
haemolysis by FPV at neutral pH if they had been pretreated with a low pH
buffer. These results demonstrated that surface properties of erythrocytes
rather than that of the virus are critical in the low pH-dependent fusion and
haemolysis by influenza viruses.
Descriptors: cell fusion, influenza A virus avian
physiology, neuraminidase physiology, viral proteins physiology, bacterial
proteins physiology, chick embryo, erythrocytes, hemagglutination, viral,
hemolysis, hydrogen-ion concentration, rabbits, rats, Vibrio cholerae
enzymology.
Huang, R.T., B. Lichtenberg, and O. Rick (1996). Involvement
of annexin V in the entry of influenza viruses and role of phospholipids in
infection. FEBS Letters 392(1): 59-62. ISSN: 0014-5793.
NAL
Call Number: QD415.F4
Abstract: Influenza viruses bind to annexin V, a widely
spread non-glycosylated phospholipid-binding protein. Externally added
phospholipids as well as antiserum against this protein specifically inhibit
infection of these viruses in cell cultures. We conclude that annexin V plays
an important role in the entry of these viruses.
Descriptors: annexin V metabolism, influenza A virus avian
metabolism, human metabolism, phospholipids metabolism, receptors, virus
metabolism, antibodies, viral immunology, capsid metabolism, cell line, dogs,
avian immunology, avian pathogenicity, human immunology, human pathogenicity,
phosphatidylethanolamines metabolism, plaque assay, recombinant fusion proteins
metabolism, time factors, viral core proteins metabolism.
Huang, R.T. and M. Orlich (1972). Substrate
specificities of the neuraminidases of Newcastle disease and fowl plague
viruses. Hoppe Seyler's Zeitschrift Fur Physiologische Chemie
353(3): 318-22. ISSN: 0018-4888.
NAL
Call Number: 384 Z38
Descriptors: influenza A virus avian enzymology,
neuraminidase, Newcastle disease virus enzymology, chickens, colloids, enzyme
tests, gangliosides, glycolipids, hydrolysis, macromolecular systems, milk,
human, oligosaccharides, structure activity relationship.
Huang, R.T., R. Rott, and H.D. Klenk (1973). On
the receptor of influenza viruses. 1. Artificial receptor for influenza virus.
Zeitschrift Fur Naturforschung. Teil C Biochemie, Biophysik, Biologie,
Virologie 28(5): 342-5. ISSN:
0341-0471.
NAL
Call Number: QH301.Z4
Descriptors: glycoproteins metabolism, neuraminic acids
metabolism, orthomyxoviridae metabolism, adsorption, binding sites,
erythrocytes drug effects, hemagglutination, viral, hemagglutinins viral,
influenza A virus avian metabolism, neuraminidase pharmacology, Newcastle
disease virus metabolism, respirovirus metabolism, sindbis virus metabolism.
Huang, R.T., R. Rott, K. Wahn, H.D. Klenk, and T.
Kohama (1980). The function of the neuraminidase in membrane fusion induced
by myxoviruses. Virology 107(2): 313-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cell membrane physiology, glycoproteins
physiology, influenza A virus avian immunology, neuraminidase physiology,
Newcastle disease virus immunology, cultured cells, chick embryo,
hemagglutinins viral metabolism, hemagglutinins viral physiology, liposomes
metabolism, viral proteins metabolism, viral proteins physiology.
Huang, R.T., K. Wahn, H.D. Klenk, and R. Rott (1980).
Fusion between cell membrane and liposomes containing the glycoproteins of
influenza virus. Virology 104(2): 294-302. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cell membrane physiology, hemagglutinins
viral, influenza A virus avian physiology, human physiology, orthomyxoviridae
physiology, cultured cells, chick embryo,
glycoproteins, liposomes,
microinjections, receptors, virus physiology, viral proteins.
Huang, R.T., K. Wahn, M.F. Schmidt, and R. Rott
(1981). Productive infection of chick embryo cells by influenza viruses
tightly bound on substratum. Medical Microbiology and Immunology
170(2): 91-8. ISSN: 0300-8584.
Abstract: To test whether penetration of influenza
viruses could occur at the plasma membrane of host cells, virus particles were
tightly bound on Concanavalin A-coated substratum of plastic culture plates and
then overlayed with embryo cells. Under these conditions, endocytosis of the
viruses was prevented but the cells were found to be effectively infected. The
results indicate, that infection by influenza viruses can occur through fusion
between the viral membrane and the host cell plasma membrane.
Descriptors: cell membrane permeability, influenza A virus
avian physiology, orthomyxoviridae physiology, cultured cells, chick embryo,
endocytosis, avian ultrastructure, microscopy, electron, virus cultivation
methods.
Hulse, D.J., R.G. Webster, R.J. Russell, and D.R.
Perez (2004). Molecular determinants within the surface proteins involved in
the pathogenicity of H5N1 influenza viruses in chickens. Journal of
Virology 78(18): 9954-64. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Descriptors: influenza A virus, avian genetics, avian
pathogenicity, viral matrix proteins genetics, base sequence, chickens, DNA,
viral genetics, glycosylation, hemagglutinins, viral chemistry, viral genetics,
avian classification, influenza, avian etiology, models, molecular,
neuraminidase chemistry, neuraminidase genetics, viral matrix proteins
chemistry, virulence genetics.
Iamnikova, S.S., E.A. Dubova, I.G. Shemiakin, M.K.h.
Saiatov, and D.K. L'vov (1984). Selektsiia antigennykh variantov virusos
grippa H1N1 posredstvom monoklonal'nykh antitel. [Selection of antigenic
variants of H1N1 influenza viruses by means of monoclonal antibodies]. Voprosy
Virusologii 29(2): 207-10. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Six different monoclonal antibodies to
influenza A/Brazil/11/78 virus hemagglutinin were used for selection of
antigenic variants of H1N1 viruses: A/USSR/090/77 and A/black-headed gull/ Kaz
. SSR/470/79. The group-specific monoclonal antibody completely neutralized the
infective activity of the parental viruses (dilutions 1:5 to 1:640). Two
antigenic variants of wild type viruses were obtained using cross-reactive
antibody. A comparative study of the antigenic structure, biological
properties, and peptide maps of the heavy chain of the original viruses,
antigenic variants, and some epidemic H1N1 strains was carried out. The
selected variants of A/black-headed gull/ Kaz. SSR/470/77 and A/USSR/090/79
viruses were shown to be similar to epidemic H1N1 strains isolated in 1953 and
1978.
Descriptors: antibodies, monoclonal analysis, antigens,
viral isolation and purification, influenza A virus human immunology, selection
genetics, variation genetics, antigens, viral analysis, birds, cross
reactions, electrophoresis, polyacrylamide gel, hemagglutination inhibition
tests, avian immunology, peptides analysis.
Iamnikova, S.S., T.O. Kovtun, G.A. Dmitriev, I.G.
Shemiakin, N.P. Semenova, D.K. L'vov, T. Chambers, and R. Vebster (1989). Antigennaia
varibel'nost' virusov grippa ptits A/H13, izolirovannykh v SSSR. [Antigenic
variability of avian influenza virus A/H13, isolated in the USSR]. Voprosy
Virusologii 34(5): 568-72. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The antigenic structure of influenza H13
viruses isolated from wild birds in the USSR in 1976-1985 was studied.
Antiserum against the reference A/gull/Maryland/704/77 (H13N6) strain was used
to demonstrate the antigenic variations among the viruses. The homology of
nucleotide sequences in the region 99-215 for the two A/H13N6 strains,
A/gull/Maryland/704/77 and A/great black-headed gull/Astrakhan/227/84, were 75%
and 86%, respectively. The 9-base segment deletion in A/grey black-headed
gull/Astrakhan/277/84 was observed. Comparison of the predicted amino acid
sequences of the strains' hemagglutinin in the appropriate region (amino acids
2-40) revealed 5 replacements (86% homology). Two replacements of arginine by
lysine and asparagine by serine in positions 15 and 16, respectively, are the
most significant. The latter replacement is accompanied by a change in the
glycosylation site and might alter its three-dimensional structure. Further
studies of the isolate genome are under way.
Descriptors: antigenic variation, antigens, viral
immunology, influenza A virus avian immunology, amino acid sequence, antigens,
viral genetics, base sequence, hemagglutinins viral genetics, avian genetics,
molecular sequence data, radioimmunoassay, sequence homology, nucleic acid, viral
proteins analysis.
Ilyushina, N.A., I.A. Rudneva, N.L. Varich, A.S.
Lipatov, R.G. Webster, and N.V. Kaverin (2003). Antigenic structure of
influenza A virus H5 hemagglutinin: Mechanisms of the acquisition of resistance
towards monoclonal antibodies in escape mutants. Molekuliarnaia Genetika, Mikrobiologiia i
Virusologiia (1): 40-45. ISSN:
0208-0613.
NAL
Call Number: QH506.M65F2
Abstract: The analysis of escape mutants of the avian
influenza virus of H5 subtype (strain A/Mallard/Pennsylvania/10218/84) revealed
the location and structure of two antigenic sites in the hemagglutinin (HA)
molecule. Several escape mutants exhibited unusual features in the reactions
with monoclonal antibodies (Mabs), being completely resistant in the
infectivity neutralization test to the Mabs used for their selection, and
retaining the ability to bind the Mabs as revealed by enzyme-linked
immunosorbent assay. An enhancement of the binding by an amino acid change in a
different antigenic site was demonstrated, as well as a complete abolishment of
the binding by a mutation selected by passage in the presence of an excess of
the non-neutralizing Mab of high binding ability. The observed effects did not
result from the changes in the affinity of the mutant HA toward sialic receptors.
The data suggest that one amino acid change in HA may prevent the virus
neutralization by different mechanisms for different Mabs: either the binding
of the Mab to HA is prevented, or the bound Mab is unable to block the
receptor-binding pocket of HA. Different mechanisms of the acquisition of
resistance to Mabs in the course of the selection of escape mutants are
discussed.
Descriptors: immune system, infection, methods and
techniques, molecular genetics, ELISA immunologic techniques, laboratory techniques,
virus infectivity neutralization test bioassay techniques, laboratory
techniques, gene mutations, methodology, viral genetics, viral neutralization,
mechanisms, analysis.
Imai, M., A. Takada, K. Okazaki, and H. Kida (1999). Antigenic
and genetic analyses of H5 influenza viruses isolated from ducks in Asia. Japanese
Journal of Veterinary Research 46(4): 171-7. ISSN: 0047-1917.
NAL
Call Number: 41.8 V6446
Abstract: The hemagglutinin (HA) of six H5 influenza
virus strains isolated from ducks in Japan and China in 1976 to 1996 were
analyzed antigenically and genetically. Antigenic analysis using a panel of
monoclonal antibodies revealed that the HA of H5 influenza viruses isolated
from ducks are antigenically closely related to each other. Phylogenetic
analysis indicates that the isolates from ducks in Hokkaido were derived from
an ancestor common with the highly pathogenic isolates from chickens and humans
in Hong Kong in 1997.
Descriptors: ducks virology, hemagglutinin glycoproteins,
influenza virus genetics, influenza A virus avian classification, avian
genetics, phylogeny, antibodies, monoclonal, antigens, viral genetics, viral
immunology, chickens virology, China, genes viral, hemagglutinin glycoproteins,
influenza virus immunology, Hong Kong, avian isolation and purification, Japan,
RNA viral genetics, viral isolation and purification.
Indulen, M.K. and R.L. Feldblum (1982). Obtaining
of a virazole-resistant fowl plague virus mutant. Acta Virologica
26(1-2): 109. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: influenza A virus avian genetics, human
genetics, mutation, ribavirin pharmacology, ribonucleosides pharmacology, drug
resistance, fowl plague microbiology, influenza microbiology, phenotype.
Indulen, M.K. and V.A. Kalninya (1973). Study on
the mechanism of inhibiting action of aminoadamantane on the reproduction of
fowl plague virus. Acta Virologica 17(4): 273-80. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: amantadine pharmacology, influenza A virus
avian metabolism, RNA viral biosynthesis, autoradiography, carbon
radioisotopes, cultured cells, chick embryo, dactinomycin pharmacology, avian
drug effects, avian growth and development, plaque assay, tissue culture,
tritium, uridine metabolism, virus replication drug effects.
Indulen, M.K., V.A. Kalnynia, N.V. Gorodkova, and
F.L. Fel'dblium (1986). Molekuliarno-biologicheskii analiz mutantov i
rekombinantov virusov grippa, rezistentnykh k remantidinu. [Molecular biology
analysis of influenza virus mutants and recombinants resistant to remantadine].
Voprosy Virusologii 31(5): 609-13.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: adamantane analogs and derivatives, influenza
A virus avian drug effects, human drug effects, mutation, recombination,
genetic drug effects, rimantadine antagonists and inhibitors, antigens, viral
analysis, chick embryo, drug resistance, microbial genetics, genes viral drug
effects, avian genetics, avian immunology, human genetics, human immunology,
plaque assay.
Inglis, S.C. and J.W. Almond (1980). An influenza
virus gene encoding two different proteins. Philosophical Transactions
of the Royal Society of London. Series B Biological Sciences 288(1029):
375-81. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Abstract: Evidence is presented which confirms that the
influenza virus genome specifies a polypeptide of molecular mass 11 000, in
addition to the eight previously recognized gene products. A summary is
included of results that show that this polypeptide is encoded by the smallest
genome segment of the virus (segment 8) which also encodes a polypeptide of
molecular mass 23 000 (NS1). The implications of these findings are considered.
Descriptors: genes viral, influenza A virus avian
genetics, viral proteins genetics, cultured cells, chickens, genes, structural,
molecular weight, species specificity.
Inglis, S.C. and C.M. Brown (1984). Differences in
the control of virus mRNA splicing during permissive or abortive infection with
influenza A (fowl plague) virus. Journal of General Virology 65(Pt.
1): 153-64. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Spliced transcripts of influenza A (fowl
plague) virus (FPV) RNA (vRNA) segments 7 and 8 accumulate to a much greater
extent during non-productive infection of mouse L cells, than they do during
productive infection in primary chick embryo fibroblasts (CEF). Virus-specific
protein synthesis, or a consequent event in virus replication appears necessary
to promote splicing of vRNA segment 8-encoded mRNAs in both cell types, and of
vRNA segment 7-encoded mRNAs in CEF. In L cells, however, splicing of the
segment 7-encoded mRNAs seems to be independent of such virus-specific control.
This observation is discussed in relation to the defect in expression of vRNA 7
which has been observed previously in FPV-infected L cells, and which is
thought to account for the failure of virus replication.
Descriptors: fowl plague microbiology, influenza A virus
avian genetics, RNA splicing, RNA viral genetics, chick embryo, DNA genetics,
viral genetics, gene expression regulation, l cells cell line microbiology,
mice, nucleic acid hybridization, peptides genetics, viral proteins
biosynthesis, virus cultivation, virus replication.
Inglis, S.C. and C.M. Brown (1981). Spliced and
unspliced RNAs encoded by virion RNA segment 7 of influenza virus. Nucleic
Acids Research 9(12): 2727-40. ISSN:
0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: Cells infected with the avian influenza virus
fowl plague virus, contains three species of polyadenylated RNA which are
complementary to virion RNA segment 7. The largest is virtually a complete
transcript of vRNA 7, and is the messenger RNA for the matrix protein, but the
coding function of the two smaller species, which are approximately 320 and 285
nucleotides long (excluding poly(A)), is unknown. It is likely however that at
least one of the small RNAs encodes a new virus polypeptide which has been
predicted from the nucleotides sequence of vRNA 7. The major part of each RNA
maps within about 300 nucleotides from the 5'-terminus of vRNA 7, but the
larger species also contains additional sequences derived from the 3' terminus.
Production of the two small RNAs may involve alternative patterns of splicing
of the matrix protein mRNA.
Descriptors: DNA, viral genetics, influenza A virus avian
genetics, poly A genetics, RNA genetics, chick embryo, cloning, molecular, DNA
restriction enzymes, fibroblasts, RNA, messenger genetics, transcription,
genetic, translation, genetic, viral proteins genetics.
Inglis, S.C., A.R. Carroll, R.A. Lamb, and B.W. Mahy
(1976). Polypeptides specified by the influenza virus genome I. Evidence for
eight distinct gene products specified by fowl plague virus. Virology
74(2): 489-503. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism,
translation, genetic, viral proteins biosynthesis, cultured cells,
hemagglutinins viral, influenza A virus avian enzymology, molecular weight,
neuraminidase biosynthesis, nucleoproteins biosynthesis, peptide synthesis,
peptides analysis, RNA replicase, viral proteins analysis.
Inglis, S.C., M.J. Gething, and C.M. Brown (1980). Relationship
between the messenger RNAs transcribed from two overlapping genes of influenza
virus. Nucleic Acids Research 8(16): 3575-89. ISSN: 0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: The relationship of the mRNAs encoding the
NS1 and NS2 polypeptides of influenza virus has been investigated through
synthesis and characterisation of complementary DNA copies of the mRNAs.
Previous work had shown that both mRNAs are encoded by virion RNA segment 8,
and that the sequences comprising the smaller of the two mRNAs (the NS2 mRNA)
were also present on the NS1 mRNA. Our results indicate that the mRNA encoding
the NS2 polypeptide of the avian influenza, fowl plague virus, is approximately
400 ntds long, and that its sequences correspond largely with the 3'-terminal
region of the NS1 mRNA.
Descriptors: DNA, viral metabolism, genes, structural,
orthomyxoviridae metabolism, RNA, messenger biosynthesis, transcription,
genetic, nucleic acid hybridization, peptide synthesis, translation, genetic,
viral proteins biosynthesis.
Inglis, S.C. and B.W. Mahy (1979). Polypeptides
specified by the influenza virus genome. 3. Control of synthesis in infected
cells. Virology 95(1): 154-64.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, RNA,
messenger biosynthesis, viral biosynthesis, viral proteins biosynthesis, cell
line, cycloheximide pharmacology, genes viral, avian genetics, transcription,
genetic, translation, genetic.
Inglis, S.C., D.J. McGeoch, and B.W. Mahy (1977). Polypeptides
specified by the influenza virus genoma. 2. Assignement of protein coding
functions to individual genome segments by in vitro translation. Virology
78(2): 522-36. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, peptide
synthesis, RNA, messenger metabolism, RNA viral metabolism, translation,
genetic, viral proteins biosynthesis, cell free system, genetic code,
glycoproteins biosynthesis, hemagglutinins viral, triticum.
Inkster, M.D., V.S. Hinshaw, and I.T. Schulze (1993).
The hemagglutinins of duck and human H1 influenza viruses differ in sequence
conservation and in glycosylation. Journal of Virology 67(12):
7436-43. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: We determined the deduced amino acid
sequences of two H1 duck influenza A virus hemagglutinins (HAs) and found that
the consensus sequence of the HA, determined directly from virus recovered from
the intestinal tract, remains unchanged through many generations of growth in
MDCK cells and chicken embryos. These two duck viruses differ from each other
by 5 amino acids and from A/Dk/Alberta/35/1976 (F. J. Austin, Y. Kawaoka, and
R. G. Webster, J. Gen. Virol. 71:2471-2474, 1990) by 9 and 12 amino acids, most
of which are in the HA1 subunit. They are antigenically similar to each other
but different from the Alberta virus. We compared these H1 duck HAs with the
HAs of human isolates to identify structural properties of this viral
glycoprotein that are associated with host range. By comparison to the human H1
HAs, the duck virus HA sequences are highly conserved as judged by the small
fraction of nucleotide differences between strains which result in amino acid
substitutions. However, the most striking difference between these duck and
human HAs is in the number and distribution of glycosylation sites. Whereas
duck and swine viruses have four and five conserved glycosylation sites per HA1
subunit, none of which are on the tip of the HA, all human viruses have at least
four additional sites, two or more of which are on the tip of the HA. These
findings stress the role of glycosylation in the control of host range and
suggest that oligosaccharides on the tip of the HA are important to the
survival of H1 viruses in humans but not in ducks or swine.
Descriptors: consensus sequence genetics, ducks
microbiology, hemagglutinins viral genetics, influenza A virus avian genetics,
human genetics, amino acid sequence, antigens, viral genetics, antigens, viral
immunology, cultured cells, consensus sequence immunology, feces microbiology,
glycosylation, hemagglutinin glycoproteins, influenza virus, hemagglutinins
viral immunology, avian immunology, human immunology, models, molecular,
molecular sequence data, protein processing, post translational, regulatory
sequences, nucleic acid genetics, selection genetics, sequence homology, amino
acid, variation genetics.
Inpanbutr, N. and R.D. Slemons (1993). Immunocytochemical
localization of type A influenza virus nucleoprotein in chicken kidney, using
freeze substitution technique for tissue fixation. American Journal of
Veterinary Research 54(3): 425-8.
ISSN: 0002-9645.
NAL
Call Number: 41.8 Am3A
Abstract: Kidney tissues were removed from euthanatized
mature White Leghorn chickens 4 days after IV inoculation with type A influenza
virus. The kidney tissues were then fixed at -70 C, using a freeze substitution
technique. Type A influenza virus nucleoprotein was readily detected in the
nuclei and cytoplasm of the proximal and distal tubular epithelial cells by
immunocytochemistry, and the sharpness of the immunomarker in the cells
indicated minimal antigen migration during fixation and tissue section preparation.
This tissue fixation technique also resulted in good preservation of cellular
morphology. The freeze substitution technique of tissue fixation is an
excellent alternative to cryostat-cut acetone-fixed tissue sections or
conventional chemical fixation of paraffin-embedded tissues for in situ
immunocytochemical localization of type A influenza virus nucleoprotein
antigen.
Descriptors: influenza A virus avian isolation and
purification, kidney microbiology, nucleoproteins analysis, chick embryo, chickens,
epithelium microbiology, freezing, immunohistochemistry, kidney tubules
microbiology.
Isachenko, V.A., S.S. Iamnikova, L.I.a.
Zakstel'skaia, T.A. Grigor'eva, and O.N. Berezina (1980). Vyiavlenie
determinant gemaggliutinina H3 virusov grippa metodom radioimmunologicheskogo
analiza. [Detection of the determinants of influenza virus H3 hemagglutinin by
the technic of radioimmunologic analysis]. Voprosy Virusologii (1):
49-53. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The interrelations between H3/73
hemagglutinin of human influenza virus and the other 16 mammalian and avian
hemagglutinin subtypes (a total of 50 strains) were studied by the method of
radioimmunologic analysis (RIA). The antigenic relations of H3, Hav7 and Heq2
were confirmed, certain common determinants were also found in H3/73
hemagglutinin and avian viral Hav6 and Hav9 hemagglutinins. No interrelations
were revealed with previously circulating human influenza viruses H0, H1, H2 as
well as with swine influenza virus and avian viruses Hav1-Hav5, Hav8. It has
been shown that the H3/73 determinant in some avian viruses evolves similarly
to drift-variants of human influenza virus. The method can be recommended for
fine analysis of influenza virus antigenic structure as it allows detecting
small antigenic quantities.
Descriptors: hemagglutinins viral immunology, influenza A
virus immunology, ducks microbiology, avian immunology, human immunology,
porcine immunology, species specificity, turkeys microbiology, radioimmunologic
analysis.
Isaeva, E.I., T.S. Belkina, Z.I. Rovnova, P.N.
Kosiakov, and I.A.M. Selivanov (1982). Antigennye determinanty virusov
grippa cheloveka v sostave grippoznykh virusov, vydelennykh ot zhivotnykh.
[Antigenic determinants of human influenza viruses among the influenza viruses
isolated from animals]. Voprosy Virusologii 27(6): 681-6. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Comparative studies of the antigenic
properties of hemagglutinin (HA) of animal and human viruses revealed both similarities
between them and complete differences in the composition of antigenic
determinants. Avian influenza viruses A/chicken/Kamchatka/12/71,
A/pintail/Primorie/730/76, and A/bat/Alma-Ata/73/77 were completely identical
with human strains of influenza virus. Influenza A/horse/Miami/63 contains one
antigenic determinant H3.1.HA of A/tern/Turkmenia/18/73 (Hav7) viruses has a
peculiar set of antigens. Apart from two antigenic determinants H3.1 and H3.3
inherent in human virus strains, HA of A/tern/Turkmenia/18/73 virus contains an
antigenic determinant the population of antibodies to which shows no relation
to HA of subtypes Hav2-Hav9.
Descriptors: epitopes isolation and purification,
influenza A virus human immunology, orthomyxoviridae immunology, complement
fixation tests, epitopes analysis, hemagglutination inhibition tests,
hemagglutinins viral analysis, hemagglutinins viral isolation and purification,
immunoelectrophoresis, orthomyxoviridae isolation and purification.
Israel, A. (1980). Genotypic and phenotypic
characterization of a mammalian cell-adapted mutant of fowl plague virus (FPV).
Journal of General Virology 51(Pt. 1): 33-44. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: A mammalian cell-adapted mutant of the Dobson
strain of fowl plague virus (FPV-B) was characterized. Genetic analyses of
recombinants between a ts mutant of this virus and either the non-adapted
Dobson strain or the Rostock strain of FPV showed that the gene coding for the
P3 protein of the adapted Dobson strain was sufficient to enable any
recombinant to grow in L cells. The abortive cycle of wild-type Dobson strain
(FPV+) was compared to the productive cycle of the mutant. By using 100
p.f.u./cell, no quantitative difference could be detected in infected L cells between
polypeptides and cRNAs induced by FPV+ and FPV-B. However, the maturation of
virions at the plasma membrane did not proceed correctly. At a lower m.o.i. the
amounts of virus polypeptides decreased with the m.o.i. This decrease was not
the same for all polypeptides and cRNA segments: HA, M and NA and their mRNAs
decreased to a greater extent than the others. These results are discussed in
relation to a possible biological activity of polypeptide P3.
Descriptors: genes viral, influenza A virus avian
genetics, virus replication, avian growth and development, avian metabolism, L
cells cell line, mice, mutation, RNA viral biosynthesis, recombination,
genetic, viral proteins biosynthesis.
Israel, A. (1979). Preliminary characterization of
the particles from productive and abortive infections of L cells by fowl plague
virus. Annales De Microbiologie 130b(1): 85-100. ISSN: 0300-5410.
NAL
Call Number: 448.3 An75
Abstract: Particles produced during the abortive
infection of L cells by fowl plague virus (Dobson strain) have been
characterized and compared to the infectious particles produced by a mutant of
this virus adapted to mammalian cells. The former are of apparently normal
morphology but most of them are non-infectious. They have the same RNA/protein
ratio as the infectious particles and the same polypeptide composition. They
contain also the same RNA segments as those found in infectious particles.
Possible reasons for the defectiveness of these particles are discussed.
Descriptors: influenza A virus avian analysis, l cells
cell line microbiology, virion analysis, electrophoresis, polyacrylamide gel,
hemagglutinins analysis, avian ultrastructure, peptides analysis, RNA viral
analysis, viral proteins analysis, virion ultrastructure.
Israel, A. (1980). Productive and abortive
infection of L cells by fowl plague virus (FPV): comparison of in vivo and in
vitro translation products of the virus mRNAs. Journal of General
Virology 47(2): 473-83. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The abortive infection of L cells by the
Dobson strain of fowl plague virus (FPV) and the productive infection by a
mammalian cell-adapted mutant have been compared. The mRNA population during
the abortive cycle is characterized by a lower production compared to the
productive system of mRNA 7 (which codes for the M polypeptide) early in the
cycle, and a lower production of mRNAs 4, 6 and 7 (which code for HA, NA and M)
late in the cycle. Differences in the amounts of the corresponding polypeptides
can also be detected when these mRNA populations are used to programme a wheat
germ cell-free system. However, analysis of the polypeptides synthesized in
vivo by the two viruses show that equivalent amounts of all virus polypeptides
are synthesized during the productive and the abortive cycles. Possible reasons
for differences between in vivo and in vitro translation of the virus mRNAs
during the abortive cycle are discussed.
Descriptors: influenza A virus avian metabolism, RNA,
messenger biosynthesis, RNA viral biosynthesis, viral proteins biosynthesis,
avian growth and development, L cells cell line, mice, RNA, messenger genetics,
viral genetics, translation, genetic, viral proteins analysis.
Israel, A. (1980). A temperature-dependent host
range mutant of fowl plague virus (FPV). Virology 105(1): 1-12. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian genetics, l cells
cell line microbiology, chick embryo, dactinomycin pharmacology,
electrophoresis, polyacrylamide gel, fluorouracil pharmacology, avian growth
and development, mice, mutation, nucleic acid hybridization, peptide synthesis,
plaque assay, RNA viral biosynthesis, temperature, viral proteins biosynthesis,
virus cultivation, virus replication.
Israel, A., A. Niveleau, G. Quash, and M.H. Richard
(1979). Latex fetuin spheres as probes for influenza virus neuraminidase in
productively and abortively infected cells. Archives of Virology
61(3): 183-99. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Fetuin bound latex spheres do not adhere to
the membranes of non-infected cells but adhere to those of cells productively
infected by fowl plague virus (FPV Dobson strain). In contrast, asialo fetuin
spheres do not attach to the membranes of productively infected cells. Moreover
latex fetuin spheres incubated with extracts of productively infected cells and
extensively washed are specifically enriched in neuraminidase activity without
any trace of haemagglutinin. These observations suggest that viral
neuraminidase in the membrane is the site of attachment of the sialic acid
moieties of fetuin spheres. These neuraminidase sites are detectable when L
cells are productively infected by a mammalian cell adapted mutant of the
Dobson strain (FPV-B) but are not detectable on L cells abortively infected by
wild type (FPV+). However, even in the abortive system, neuraminidase is
synthesised de novo as shown by its labelling with 14C-glucosamine and by its
isolation from labelled extracts of infected cells by latex fetuin spheres.
These results show that misintegration of viral neuraminidase in the plasma
membrane of L cells is a feature of abortive infection of these cells by the
Dobson strain of FPV. However the relationship (if any) of this misintegration
to abortive infection remains to be established.
Descriptors: cell membrane enzymology, influenza A virus
avian enzymology, microbiological techniques, neuraminidase analysis, cell
line, avian growth and development, l cells cell line, latex, microscopy,
electron, scanning, microspheres, neuraminidase biosynthesis, alpha
fetoproteins.
Israel, A., M. Semmel, and J. Huppert (1975). Host-range
mutant of fowl plague virus (FPV): comparison of the genome and virus proteins.
Virology 68(2): 503-9. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian growth and
development, mutation, RNA viral analysis, viral proteins analysis, cell line,
chickens, glycoproteins analysis, hamsters, avian analysis, mice, molecular
weight, nucleic acid conformation, peptides analysis, virus replication.
Itamura, S. (2000). Development of influenza
vaccines against newly emerging A/H5N1 virus. Nippon Rinsho Japanese
Journal of Clinical Medicine 58(1): 255-64.
ISSN: 0047-1852.
Abstract: Emergence of highly virulent influenza A/H5N1
viruses in Hong Kong in 1997 posed a threat of pandemic and brought an urgent
need to develop a suitable seed virus for vaccine production. The virulence of
the H5N1 viruses to chicken embryos should hamper the efficient production of
the vaccine. In addition, potential virulence to humans raised safety issue in
manufacturing vaccine. Toward vaccine development, one approach is to use an
avirulent avian influenza virus antigenically similar to the virulent ones as a
surrogate vaccine strain. The other approach is based on the attenuation of
pathogenicity of virulent H5N1 virus by genetic engineering of the
hemagglutinin gene and selection of a gene constellation. The reverse genetics
technique can make the latter approach possible. Candidate strains suitable for
vaccine production could be prepared by using either approach.
Descriptors: influenza transmission, influenza A virus
human genetics, human immunology, influenza vaccine, chick embryo, genes viral,
genetic engineering, hemagglutinins chemistry, hemagglutinins genetics,
vaccines, attenuated, virulence.
Itkin, Z.B. and Z.F. Bogautdinov (1973). Kharakteristika
belkov virusa grippa ptits. [Characteristics of proteins of avian influenza
virus]. Sbornik Nauchnykh Trudov, Moskovskaya Veterinarnaya Akademiya
70: 125-130.
Descriptors: proteins, avian influenza virus,
electrophoresis.
Ito, T., H. Kida, and R. Yanagawa (1985). Antigenic
analysis of H4 influenza virus isolates using monoclonal antibodies to defined
antigenic sites on the hemagglutinin of A/Budgerigar/Hokkaido/1/77 strain. Archives
of Virology 84(3-4): 251-9. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Three non-overlapping antigenic sites were
defined on the hemagglutinin of avian influenza virus
A/budgerigar/Hokkaido/1/77 (H4N6) by competitive binding assay of monoclonal
antibodies to the virus and comparative antigenic analysis of variants selected
with monoclonal antibodies. Antigenic relationship among 25 H4 influenza
viruses of different bird origin was examined by ELISA with the monoclonal
antibodies to each of defined antigenic sites. Two of the three antigenic sites
contained epitopes specific to the H4 influenza viruses of budgerigar and mynah
origin, and the remaining site contained an epitope which was cross-reactive
with almost all of the H4 influenza viruses.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, antibodies, monoclonal, antibodies, viral, birds
microbiology, chickens microbiology, cross reactions, ducks microbiology,
enzyme linked immunosorbent assay, epitopes immunology, species specificity.
Ito, T., Y. Kobayashi, T. Morita, T. Horimoto, and Y.
Kawaoka (2002). Virulent influenza A viruses induce apoptosis in chickens.
Virus Research 84(1-2): 27-35.
ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Virulent avian influenza A viruses produce
lethal disease in chickens. Since cell death can be caused by either necrosis
or apoptosis, we investigated the types of cell death that occur in natural
hosts, chickens, infected with virulent avian viruses. Using biochemical
methods, we demonstrate that virulent avian influenza viruses induce apoptosis
of vascular endothelial cells in liver, kidney, and brain. Viral antigens were
also detected in these organs, suggesting that viral replication induces
apoptosis in infected chickens. These results indicate that apoptosis does
occur in virulent avian influenza virus infection in a natural host, and may
contribute to the lethality of the virus.
Descriptors: apoptosis, influenza A virus avian
pathogenicity, antigens, viral physiology, chickens, virulence.
Ito, T., Y. Suzuki, L. Mitnaul, A. Vines, H. Kida,
and Y. Kawaoka (1997). Receptor specificity of influenza A viruses
correlates with the agglutination of erythrocytes from different animal
species. Virology 227(2): 493-9.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Despite their uniform ability to bind to
oligosaccharide-containing terminal sialic acids, influenza A viruses show
differences in receptor specificity. To test whether agglutination of
erythrocytes from different animal species could be used to assess the receptor
specificity of influenza A viruses, we determined the agglutinating activities
of a range of virus strains, including those with known receptor specificities,
using erythrocytes from seven animal species. All equine and avian viruses,
including those known to recognize N-acetyl and N-glycolyl sialic acid linked
to galactose by the alpha2,3 linkage (NeuAc alpha2,3Gal and NeuGc alpha2,3Gal),
agglutinated erythrocytes from all of the animal species tested (chickens,
ducks, guinea pigs, humans, sheep, horses, and cows). The human viruses,
including those known to preferentially recognize NeuAc alpha2,6Gal,
agglutinated all but the horse and cow erythrocytes. Fluorescence-activated
cell sorting analysis of erythrocytes using linkage-specific lectins [Sambucus
nigra agglutinin for sialic acid (SA) alpha2,6Gal and Maackia amurensis
agglutinin for SA alpha2,3Gal] showed that both cow and horse erythrocytes
contain a large amount of SA alpha2,3Gal-, but virtually no SA2,6Gal-specific
lectin-reactive oligosaccharides on the cell surface, while human and chicken
erythrocytes contained both types of oligosaccharides. Considering that the
majority (>93%) of sialic acid in horse and cow erythrocytes is of the
N-glycolyl type, our results suggest that viruses able to agglutinate these
erythrocytes (i.e., avian and equine viruses) recognize NeuGc alpha2,3Gal.
These findings also show that agglutinating assays with erythrocytes from
different animal species would be useful in characterizing the receptor
specificity of influenza A viruses.
Descriptors: erythrocytes physiology, erythrocytes
virology, hemagglutination, influenza A virus physiology, receptors, virus
physiology, carbohydrate sequence,
cattle, chick embryo, chickens, guinea pigs, horses, influenza A virus avian
physiology, human physiology, porcine, lectins, molecular sequence data,
species specificity, substrate specificity, swine.
Ito, T., Y. Suzuki, T. Suzuki, A. Takada, T.
Horimoto, K. Wells, H. Kida, K. Otsuki, M. Kiso, H. Ishida, and Y. Kawaoka
(2000). Recognition of N-glycolylneuraminic acid linked to galactose by the
alpha2,3 linkage is associated with intestinal replication of influenza A virus
in ducks. Journal of Virology 74(19): 9300-5. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The hemagglutinin (HA) of H3 human influenza
viruses does not support viral replication in duck intestine despite its avian
origin. A Leu-to-Gln mutation at position 226 and a Ser-to-Gly mutation at
position 228 in the HA of human A/Udorn/307/72 (H3N2) permit a reassortant virus
[human Udorn HA, with all other genes from A/mallard/New York/6750/78 (H2N2)]
to replicate in ducks. To understand the molecular basis of this change in host
range restriction, we investigated the receptor specificity of duck influenza
viruses as well as of human-duck virus reassortants. The results indicate that
the recognition of a glycoconjugate moiety possessing N-glycolneuramic acid
(NeuGc) linked to galactose by the alpha2,3 linkage (NeuGcalpha2,3Gal) is
associated with viral replication in duck intestine. Immunofluorescence assays
with NeuGcalpha2,3Gal-specific antiserum detected this moiety primarily on the
crypt epithelial cells of duck colon. Such recognition, together with
biochemical evidence of NeuGc in crypt cells, correlated exactly with the ability
of the virus to replicate in duck colon. These results suggest that recognition
of the NeuGcalpha2,3-Gal moiety plays an important role in the enterotropism of
avian influenza viruses.
Descriptors: ducks virology, hemagglutinins viral
physiology, influenza virology, influenza A virus physiology, neuraminic
acids, galactose, virus replication.
Ito, T., H. Goto, E. Yamamoto, H. Tanaka, M.
Takeuchi, M. Kuwayama, Y. Kawaoka, and K. Otsuki (2001). Generation of a
highly pathogenic avian influenza A virus from an avirulent field isolate by
passaging in chickens. Journal of Virology 75(9): 4439-4443. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Highly virulent avian influenza viruses can
arise from avirulent strains maintained in poultry, but evidence to support
their generation from viruses in wild birds is lacking. The most likely
mechanism for the acquisition of virulence by benign avian viruses is the
introduction of mutations by error-prone RNA polymerase, followed by the
selection of virulent viruses. To investigate whether this mechanism could
apply to wild waterfowl, we studied an avirulent wild-swan virus that
replicates poorly in chickens. After 24 consecutive passages by air sac
inoculation, followed by five passages in chicken brain, the avirulent virus
became highly pathogenic in chickens, producing a 100% mortality rate. Sequence
analysis at the hemmaglutinin cleavage site of the original isolate revealed a
typical avirulence type of sequence, R-E-T-R, which progressed incrementally to
a typical virulence type of sequence, R-R-K-K-R, during repeated passages in
chickens. These results demonstrate that avirulent viruses maintained in wild
waterfowl in nature and bearing the consensus avirulence type sequence R-E-T-R
have the potential to become highly pathogenic while circulating in chickens.
Descriptors: molecular genetics, infection, veterinary
medicine.
Ito, T., H. Ito, M. Kojima, and Y. Kawaoka (2004). Amino
acids associated with intestinal replication of influenza A virus in ducks:
relationship to low pH stability of neuraminidase. International
Congress Series 1263: 205-208.
Abstract: In order to determine the role of
neuraminidase (NA) in host range restriction, we studied a reassortant virus
that replicated with poor efficiency in ducks. The reassortant virus, in which
NA of an avian virus, A/duck/Hong Kong/278/78 (H2N9), was replaced with that
from a human virus, A/England/12/62 (H2N2), was rectally inoculated into ducks.
The viruses recovered were then orally inoculated into new ducks and a variant
that replicated efficiently in the intestinal tract was isolated. Sequence
analysis showed that the variant virus NA contained two amino acid
substitutions at positions 165 (Val to Ile) and 431 (Gln to Pro). Differences
in low pH resistance of the NAs were also assessed to identify differences in
the NAs possibly related to the restriction of viral growth in ducks. The NA
activity of the parental reassortant virus almost disappeared after low pH
treatment (pH 3.0), while that of the variant was conserved under the same
conditions. These results indicate that the amino acids, at positions 165
and/or 431 on the NA molecule, correlate with the ability to support viral
growth in ducks, contributing to the low pH stability of NA activity.
Descriptors: avian influenza, intestinal replication, low
pH, neuraminidase, ducks, amino acids, influenza A virus.
Ivanova, V., R. Rouseva, M. Kolarova, J. Serkedjieva,
R. Rachev, and N. Manolova (1994). Isolation of a polysaccharide with
antiviral effect from Ulva lactuca. Preparative Biochemistry
(USA) 24(2): 83-97. ISSN: 0032-7484.
NAL
Call Number: QD415.A1P7
Abstract: A polysaccharide from the green marine algae Ulva
lactuca has been isolated. The substance has been investigated after acid hydrolysis
by thin-layer and gas chromatography. The following carbohydrate components
have been found: arabinose-xylose-rhamnose-galactose-mannose-glucose in ratio
1:1:9:5:2.5:16 respectively. One unidentified sugar has been demonstrated too.
The polysaccharide has been studied for antiviral activity in vitro against a
number of human and avian influenza viruses. A considerable inhibition of the
viral reproduction was found. The effect was dose-dependent, strain-specific
and selective.
Descriptors: algae, chemical composition, polysaccharides,
purification, monosaccharides, arabinose, xylose, rhamnose, galactose, mannose,
glucose, aldoses, carbohydrates, monosaccharides, processing, reducing sugars,
sugars, carbohydrate composition, composition.
Ivanova, V.T., H. Hermann, L.Y.A. Zakstelskaya, L.
Dohner, R.Y.A. Podchernyaeva, and V.K. Blinova (1983). Differentiation of
influenza A virus nucleoproteins in enzyme-linked immunosorbent assay. Acta
Virologica 27(1): 71-4. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The serum antibody titre to the nucleoprotein
(NP) of the influenza virus recombinant MRC-11 was determined in virus strains
A/USSA/5/80 (H3N2), A/Hong Kong/8/64 (H3N2), A/duck/Ukraine/63 (Hav7Neq2) and
in a recombinant strain between A/tern/Frunse/334/78(Hav4Nav1) and
A/PR/8/34(H0N1) using the enzyme-linked immunosorbent assay (ELISA).
Significant differences between the NP of these strains were found proving the
usefulness for ELISA for such investigations.
Descriptors: antigens, viral analysis, influenza A virus
avian analysis, human analysis, nucleoproteins immunology, viral proteins
immunology, enzyme linked immunosorbent assay, avian immunology, human
genetics, human immunology, recombination, genetic.
Ivanova, V.T., V.A. Isachenko, L.I.A. Zaktstel'skaia,
and V.M. Zhdanov (1979). Sravnitel'noe izuchenie elektroforeticheskoi
podvizhnosti polipeptidov virusov grippa roda a ptitis. [Comparative study of
the electrophoretic mobility of the polypeptides from avian influenza viruses
type A]. Voprosy Virusologii (5): 505-10. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A comparative study of the electrophoretic
mobility of polypeptides of avian influenza viruses was carried out; molecular
weights of polypeptides and their percent content were determined. Strains
isolated from one host and possessing different hemagglutinin serotypes were
found to have different electrophoregrams due to differences in the position of
the light or heavy chain of hemagglutinin. Hemagglutinins (Hav7, Heq2, H3) and
(Hav1, Heq1) in virions isolated from different hosts had similar
electrophoretic mobilities of the heavy and particulary light chain. No
significant variations in the molecular weights of NP and M proteins of all the
viruses under study were found. No identity in the electrophoretic mobility and
content of P1--P3 proteins in different strains of avian influenza virus was
found.
Descriptors: influenza A virus avian analysis, peptides
analysis, birds microbiology, chick embryo, electrophoresis, polyacrylamide
gel, hemagglutinins viral analysis, molecular weight.
Iwasaki, T., S. Itamura, H. Nishimura, Y. Sato, M.
Tashiro, T. Hashikawa, and T. Kurata (2004). Productive infection in the
murine central nervous system with avian influenza virus A (H5N1) after
intranasal inoculation. Acta Neuropathologica 108(6): 485-92. ISSN: 0001-6322.
Abstract: The H5N1 type of influenza A virus isolated
from human patients in 1997 has a characteristic hemagglutinin and was
considered to be directly transmitted from birds. Although neuropathogenicity
of this virus was not demonstrated in human autopsy cases, some experimental
studies using mice have disclosed that this virus infects the central nervous
system (CNS) after intranasal inoculation. In this study we focused on the
topographical localization of virus-infected cells in the murine CNS after
intranasal inoculation. We immunohistochemically examined virus-infected cells
in mouse tissues using a rabbit antiserum recognizing the nucleoprotein of influenza
A virus. The virus-infected cells appeared initially in the respiratory tract.
Thereafter, the virus antigen-positive cells appeared in the olfactory system
and the cranial nerve nuclei innervating the facial region. This suggests that
this virus is principally transmitted from the nasal cavity to CNS through the
cranial nerves. Neurons were frequently infected and glial and ependymal cells
were also infected. Transneuronal transmission of the virus might play the
important role of viral spread within the CNS.
Descriptors: central nervous system pathology, central
nervous system virology, influenza A virus, avian influenza pathogenicity,
nasal cavity virology, administration, intranasal, birds, immunohistochemistry,
mice, neurons pathology.
Iwatsuki Horimoto, K., R. Kanazawa, S. Sugii, Y.
Kawaoka, and T. Horimoto (2004). The index influenza A virus subtype H5N1
isolated from a human in 1997 differs in its receptor-binding properties from a
virulent avian influenza virus. Journal of General Virology 85(Pt.
4): 1001-5. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: To gain insight into the events that occur
when avian influenza viruses are transmitted to humans, the receptor-binding
properties of the index H5N1 influenza virus isolated from a human in 1997 and
the A/turkey/Ontario/7732/66 (H5N9) virus were compared, by using a
haemadsorption assay. Cells expressing the haemagglutinin (HA) of the human
isolate were adsorbed by both chicken red blood cells (RBCs) and human RBCs;
those expressing the avian virus HA were only adsorbed by chicken RBCs. These
results indicate that human and avian influenza virus H5 HAs differ in their
recognition of sialyloligosaccharides on the RBCs of different animal species.
Mutational analyses indicated that differences in both the oligosaccharide
chains and in the amino acid sequences around the HA receptor-binding site were
responsible for this difference in receptor binding. These data further support
the concept that alteration in receptor recognition is important for
replication of avian viruses in humans.
Descriptors: influenza A virus, avian physiology, human
physiology, chickens, hemagglutinins, viral chemistry, viral genetics,
hemagglutinins, viral physiology, avian pathogenicity, human genetics, human
isolation and purification, human pathogenicity, models, molecular,
mutagenesis, site directed, protein conformation, receptors, virus physiology,
virulence, virus replication.
Jackson, D.C., L.E. Brown, and D.O. White (1981). Antigenic
determinants of influenza virus haemagglutinin. VI. Antigenic characterization
of the oligosaccharide sidechains form HA1 of influenza virus haemagglutinins.
Journal of General Virology 52(Pt. 1): 163-8. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The oligosaccharide sidechains attached to
the major polypeptide, HA1 of the haemagglutinin of influenza virus were
examined for antigenic activity using a solid-phase radioimmunoassay.
Cross-reactivity between the HA1 of the different human subtypes was clearly demonstrable
with IgG raised against purified virus but was abrogated if anti-carbohydrate
antibodies were first removed by passage of the IgG through an immunoadsorbent
column containing haemagglutinin (HA) from an unrelated avian influenza strain.
Antibodies eluted from the column were found to cross-react with the HA1 of all
subtypes tested. 'Host antigen' extracted from chick chorioallantoic membrane
and coupled to Sepharose was also able to remove cross-reactive antibodies from
antiviral sera, while antibodies raised against host antigen bound to the HA1
isolated from each subtype tested. It is concluded that, although there are
qualitative and quantitative differences between the oligosaccharide sidechains
of influenza haemagglutinins, the antigenically active sidechains are
cross-reactive.
Descriptors: hemagglutinins viral immunology, influenza A
virus immunology, oligosaccharides immunology, cross reactions, epitopes,
influenza A virus classification, radioimmunoassay.
Jackson, D.C., X.L. Tang, K.G. Murti, R.G. Webster,
G.W. Tregear, and W.J. Bean (1991). Electron microscopic evidence for the
association of M2 protein with the influenza virion. Archives of
Virology 118(3-4): 199-207. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Immunogold electron microscopy revealed that
site-specific antibodies elicited by a synthetic peptide representing the
N-terminal sequence (residues 2-10) of influenza virus M2 protein were capable
of binding to the surface of virions. Antibody binding was observed with two
human influenza virus strains but not with an avian virus strain which has
amino acid substitutions in the appropriate sequence of M2. These results
provide direct evidence for the presence of M2 in the influenza virion.
Descriptors: orthomyxoviridae metabolism, viral matrix
proteins metabolism, virion metabolism, amino acid sequence, influenza A virus
avian metabolism, avian ultrastructure, human metabolism, human ultrastructure,
influenza B virus metabolism, influenza B virus ultrastructure, influenza virus
C metabolism, influenza virus C ultrastructure, microscopy, immunoelectron,
molecular sequence data, orthomyxoviridae immunology, orthomyxoviridae
ultrastructure, peptides chemical synthesis, peptides immunology, viral matrix
proteins ultrastructure, virion ultrastructure.
Jameson, J., J. Cruz, M. Terajima, and F.A. Ennis
(1999). Human CD8+ and CD4+ T lymphocyte memory to influenza A viruses of
swine and avian species. Journal of Immunology 162(12):
7578-83. ISSN: 0022-1767.
NAL
Call Number: 448.8 J8232
Abstract: Recently, an avian influenza A virus (A/Hong
Kong/156/97, H5N1) was isolated from a young child who had a fatal influenza
illness. All eight RNA segments were of avian origin. The H5 hemagglutinin is
not recognized by neutralizing Abs present in humans as a result of infection
with the human H1, H2, or H3 subtypes of influenza A viruses. Subsequently,
five other deaths and several more human infections in Hong Kong were
associated with this avian-derived virus. We investigated whether influenza
A-specific human CD8+ and CD4+ T lymphocytes would recognize epitopes on
influenza A virus strains derived from swine or avian species, including the
1997 H5N1 Hong Kong virus strains. Our results demonstrate that adults living
in an urban area of the U.S. possess influenza A cross-serotype reactive CD8+
and CD4+ CTL that recognize multiple epitopes on influenza A viruses of other
species. Bulk culture cytotoxicity was demonstrated against avian and human
influenza A viruses. Enzyme-linked immunospot assays detected precursor CTL
specific for both human CTL epitopes and the corresponding A/HK/97 viral
sequences. We hypothesize that these cross-reactive CTL might provide partial
protection to humans against novel influenza A virus strains introduced into
humans from other species.
Descriptors: cd4 positive T lymphocytes immunology, CD4
positive T lymphocytes virology, CD8 positive T lymphocytes immunology, CD8
positive T lymphocytes virology, influenza A virus avian immunology, porcine
immunology, cell line, chickens, cytotoxicity, immunologic genetics, ducks,
enzyme linked immunosorbent assay, avian genetics, porcine genetics,
leukocytes, mononuclear immunology, leukocytes, mononuclear virology, peptides
genetics, peptides immunology, point mutation, stem cells immunology, stem
cells virology, swine.
Ji DeJun, Peng DaXin, Liu HongQi, Chen SuJuan, Wu
YanTao, Gao Song, and Liu XiuFan (2003). Genetic stability of a recombinant
fowlpox virus with an avian influenza virus H9 hemaglutinin (HA) gene insert.
Chinese Journal of Veterinary Science 23(4): 347-349. ISSN: 1005-4545.
NAL
Call Number: SF604.C58
Descriptors: antibodies, genetic stability,
hemagglutinins, immunity, avian influenza virus, fowl pox virus, chickens.
Jia LiJun, Liu XiuFan, Zhang YanMei, Peng DaXin, and
Zhang RuKuan (2004). Effect of rFPV-IFN- gamma as immunopotentiator on
active immunization induced by H5 subtype avian influenza vaccines in chickens.
Journal of Agricultural Biotechnology
12(4): 427-430. ISSN: 1006-1304.
NAL
Call Number: S494.5.B563N86
Descriptors: immunity, immunization, inactivated vaccines,
recombinant vaccines, interferon, maternal antibodies, potency, avian influenza
virus, fowl pox virus, chickens.
Jia LiJun, Zhang YanMei, Peng DaXin, Liu HongQi,
Cheng Jian, Zhang RuKuan, and Liu XiuFan (2004). Influence of dosage and
maternal antibody on responses of chickens to recombinant fowl pox virus
vaccine against H5 subtype avian influenza. Chinese Journal of
Veterinary Science 24(2): 150-152.
ISSN: 1005-4545.
NAL
Call Number: SF604.C58
Descriptors: chicks, immune response, immunization,
dosage, maternal antibodies, mortality, recombinant vaccines, avian influenza,
fowl pox virus.
Johansson, B.E. and E.D. Kilbourne (1993). Dissociation
of influenza virus hemagglutinin and neuraminidase eliminates their
intravirionic antigenic competition. Journal of Virology 67(10):
5721-3. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: When presented together on the intact
influenza virus particle, the external hemagglutinin (HA) and neuraminidase
(NA) antigens are competitive, with HA dominant over NA in both T- and B-cell
priming (B. E. Johansson, T. M. Moran, and E. D. Kilbourne, Proc. Natl. Acad.
Sci. USA 84:6869-6873, 1987). Dissociation and purification of HA and NA from
virus and their injection separately or in combination into BALB/c mice
eliminates their antigenic competition as measured by antibody response,
confirming that it is their structural association that leads to what we have
termed intravirionic antigenic competition. We discuss this phenomenon with
respect to previously described intermolecular antigenic competition and with
regard to its probable mechanism. Our findings are relevant to contemporary
interest in viral vaccine vectors and multicomponent vaccines.
Descriptors: hemagglutinins viral immunology, influenza
immunology, influenza A virus avian immunology, human immunology, neuraminidase
immunology, antibodies, viral blood, antibody formation, enzyme linked
immunosorbent assay, hemagglutination inhibition tests, hemagglutinin
glycoproteins, influenza blood, avian pathogenicity, human pathogenicity, lung
microbiology, mice, neutralization tests, viral envelope proteins immunology.
Joss, A., A.J. Hay, J.J. Skehel, and D.C. Burke
(1968). Protein components of fowl-plague virus. Biochemical Journal
110(3): 40-41. ISSN: 0264-6021.
NAL
Call Number: QP501,B64
Descriptors: antigens analysis, influenza A virus avian
analysis, proteins analysis, centrifugation, density gradient, electrophoresis,
hemagglutinins viral analysis, tritium.
Jou, W.M., M. Verhoeyen, R. Devos, E. Saman, R. Fang,
D. Huylebroeck, W. Fiers, G. Threlfall, C. Barber, N. Carey, and S. Emtage
(1980). Complete structure of the hemagglutinin gene from the human
influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA. Cell
19(3): 683-96. ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Abstract: The complete sequence of a hemagglutinin (HA)
gene of a recent human influenza A strain, A/Victoria/3/75, is 1768 nucleotides
long and contains the information for 567 amino acids. It codes for a signal
peptide of 16 amino acids, the HA1 chain of the mature hemagglutinin of 329
amino acids, a connecting region between HA1 and HA2 consisting of a single
arginine residue and the HA2 portion of 221 amiino acids. The sequence is
compared with the hemagglutinin of two members of other subtypes, the human H2
strain A/Jap/305/57 and the avian Hav1 strain A/FPV/Rostock/34, and with one of
the same H3 subtype, A/Memphis/3/72. To align the HA1 chain of different major
subtypes several deletions/insertions of single amino acids must be invoked,
but two more extensive differences are found at both ends, one leading to an
extension of the amino terminal sequence of HA1 and the other (four residues)
occurring in the region processed away between HA1 and HA2. Comparison of the
HA1 of two H3 strains suggests that drift probably depends on single base
mutations, some of which change antigenic determinants. The HA2 region, which
apparently is not involved in the immune response, is highly conserved even
between different subtypes, and single base substitutions account for all the
observed diversity. A hydrophobic segment of 24 residues is present in the same
position close to the carboxyl terminus of HA2 in both Victoria and FPV, and
presumably functions in implantation into the lipid bilayer. The many conserved
features not only in HA2 but also in HA1 suggest a rather rigid architecture
for the whole hemagglutinin molecule.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus human genetics, RNA viral genetics, amino acid sequence, base
sequence, carbohydrates analysis, cloning, molecular, codon, DNA, viral
genetics, epitopes, hemagglutinins viral analysis, avian genetics.
Justewicz, D.M., M.J. Morin, H.L. Robinson, and R.G.
Webster (1995). Antibody-forming cell response to virus challenge in mice
immunized with DNA encoding the influenza virus hemagglutinin. Journal
of Virology 69(12): 7712-7. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Immunization of mice with DNA encoding the
influenza virus hemagglutinin (HA) affords complete protection against lethal
influenza virus infection and the means to investigate the mechanisms of B-cell
responsiveness to virus challenge. Using a single-cell enzyme-linked immunospot
assay, we sought to determine the localization of HA-specific antibody-forming
cells (AFCs) during the development of humoral immunity in mice given HA DNA
vaccine by gene gun. At 33 days postvaccination, populations of AFCs were
maintained in the spleen and bone marrow. In response to lethal challenge with
influenza virus, the AFCs became localized at the site of antigenic challenge,
i.e., within the draining lymph nodes of the lung compartment. Immunoglobulin G
(IgG)- and IgA-producing AFCs were detected in lymph nodes of the upper and
lower respiratory tracts, underscoring their importance in clearing virus from
the lungs. Response to challenge required competent CD4+ T cells, without which
no AFCs were generated, even those producing IgM. By contrast, in mice
vaccinated with an HA-containing subunit vaccine, fewer AFCs were generated in
response to challenge, and these animals were less capable of resisting
infection. Our findings demonstrate the comparable localization of AFCs in
response to challenge in mice vaccinated with either HA DNA or live virus.
Moreover, the former strategy generates both IgG- and IgA-producing plasma
cells.
Descriptors: B lymphocytes immunology, DNA, viral
immunology, hemagglutinins viral genetics, influenza A virus avian immunology,
influenza vaccine toxicity, T lymphocytes, helper inducer immunology, antibody
formation, bone marrow immunology, CD4 positive T lymphocytes, viral
metabolism, viral toxicity, hemagglutinin glycoproteins, influenza virus, viral
biosynthesis, hemagglutinins viral immunology, immunization, secondary,
immunologic memory, lethal dose 50, lymph nodes immunology, lymphocyte
depletion, mice, spleen immunology, time factors.
Kaleta, E.F. and A. Honicke (2005). A
retrospective description of a highly pathogenic avian influenza A virus
(H7N1/Carduelis/Germany/72) in a free-living siskin (Carduelis spinus Linnaeus,
1758) and its accidental transmission to yellow canaries (Serinus canaria
Linnaeus, 1758). DTW Deutsche Tierarztliche Wochenschrift 112(1):
17-9. ISSN: 0341-6593.
NAL
Call Number: 41.8 D482
Abstract: A haemagglutinating virus was isolated in
summer 1972 from a single free-living siskin (Carduelis spinus Linnaeus,
1758) in embryonated chicken eggs. Additional cases of morbidity or mortality
were not observed in the area were the sick siskin was found. The virus was
characterized as an avian influenza A virus of the subtype H7N1 and designated
H7N1/Carduelis/Germany/72. The virus induced following experimental inoculation
of chicken embryos a high rate mortality (mean death time approximately 24
hours), formed plaques in chicken embryo fibroblast cultures without addition
of trypsin and has an intracerebral pathogenicity index (ICPI) of 1.80.
Therefore, this virus is considered as a highly pathogenic avian influenza A
virus. Canaries (Serinus canarius Linnaeus, 1758), that were housed in
the same room with the siskin were accidentially exposed by contact to the sick
siskin which resulted in virus transmission followed by conjunctivitis, apathy,
anorexia and a high rate mortality.
Descriptors: canaries virology, disease transmission,
horizontal veterinary, influenza A virus, avian pathogenicity, influenza, avian
transmission, Passeriformes virology, retrospective studies.
Kaleta, E.F. and A. Honicke (2004). Review of the
literature on avian influenza A viruses in pigeons and experimental studies on
the susceptibility of domestic pigeons to influenza A viruses of the
haemagglutinin subtype H7. DTW Deutsche Tierarztliche Wochenschrift
111(12): 467-72. ISSN: 0341-6593.
NAL
Call Number: 41.8 D482
Abstract: The scientific literature of the past century
is reviewed on fowl plague (presently termed highly pathogenic avian influenza,
HPAI) in pigeons. HPAI viruses cause epidemic disease outbreaks with high rates
of losses in many avian species, particularily in chickens and turkeys. Also
susceptible to disease are quails, guinea fowl, ducks, geese, ostriches,
passerine birds, and birds of prey whereas conflicting reports on the
susceptibility of the domestic pigeon exist. Based on literature reports and on
own experiments, and applying as criteria for judgements clinically overt forms
of disease, virus multiplication plus shedding and seroconversion, it is
concluded that domestic pigeons are only partially susceptible to influenza A
viruses of the haemagglutinin subtype H7. Infection of pigeons with H7 viruses
results only in some of them in signs, virus shedding and seroconversion. Using
the same criteria, pigeons appear to be even less susceptible to infection with
influenza A viruses of the H5 subtype. Only one of five publications describe
in 1/19 pigeons exposed to H5 influenza A virus depression one day before
death, and only 2/19 multiplied and excreted virus, and 1/19 developed
circulating antibodies. Consequently, pigeons play only a minor role in the
epidemiology of H5 influenza viruses. In contrast, following infection with
influenza A virus of the subtype H7 clinical signs in pigeons consist of
conjunctivitis, tremor, paresis of wings and legs, and wet droppings.
H7-infected pigeons multiply and excrete H7 viruses and develop circulating
antibodies. Albeit of the status of infection, free-flying domestic pigeons can
act as mechanical vectors and vehicles for long-distance transmission of any
influenza A virus if plumage or feet were contaminated.
Descriptors: Columbidae virology, influenza A virus, avian
pathogenicity, avian influenza virology, chick embryo, chickens, disease
susceptibility veterinary, ducks, avian classification, avian influenza
pathology, avian influenza transmission, species specificity, virus shedding.
Kalninya, V.A. and M.K. Indulen (1976). Effect of
adamantane derivatives on the activity of orthomyxovirus RNA-dependent RNA
polymerase. Acta Virologica 20(4): 343-6. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The effect of several adamantane derivatives
on the activity of virion-associated RNA-dependent RNA polymerase of fowl
plague virus (FPV) and influenza B virus was studied in vitro. Some of the
derivatives inhibited the activity of the polymerase by 60 per cent. A
correlation was established between the previously demonstrated capacity of
these inhibitors to suppress orthomyxovirus reproduction in vivo and their
ability to reduce the activity of virion-associated RNA-dependent RNA
polymerase in vitro.
Descriptors: adamantane pharmacology, bridged compounds
pharmacology, influenza A virus avian enzymology, orthomyxoviridae enzymology,
RNA nucleotidyltransferases metabolism, RNA replicase metabolism, adamantane
analogs and derivatives, avian growth and development, orthomyxoviridae growth
and development, virus replication drug effects.
Kaluza, G. (1976). Early synthesis of Semliki
Forest virus-specific proteins in infected chicken cells. Journal of
Virology 19(1): 1-12. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Cells preinfected with fowl plague virus
followed by treatment with actinomycin D are a suitable system for studying
early protein synthesis in cells infected with Semliki forest virus. One and
one-half hours after superinfection, three new nonstructural proteins (NVP)
were detected: NVP 145, NVP, 112, and NVP 65. They appeared in parallel with a
low incorporation of mannose at the beginning of the infectious cycle. Behavior
on chasing suggested a precursor relationship of NVP 112 to the envelope
glycoproteins. Two kinds of NVP 65 are described, both of which are varieties
of NVP 68 with an incomplete mannose content. One type, detected early after
infection, was converted into NVP 68 by supplementary glycosylation. The
second, late type was stable. It contains fucose and resembles the NVP 65
observed after impairment of glycosylation. The mechanism of NVP 68
glycosylation is discussed. The presence of the complete carbohydrate moiety is
crucial for the cleavage of NVP 68 into the envelope proteins E2 and E3 and, thus,
for virus maturation. Only the complete form of NVP 68 was precipitated by
envelope-specific antisera. A large production of NVP 78 is a further feature
of the early events in infected cells. It is not related to the structural
proteins.
Descriptors: Semliki Forest virus metabolism, viral
proteins biosynthesis, chick embryo, dactinomycin pharmacology, epitopes,
glycoproteins biosynthesis, glycoproteins immunology, influenza A virus avian
growth and development, mannose metabolism, molecular weight, peptide
synthesis, protein precursors biosynthesis, Semliki Forest virus immunology,
tissue culture, viral proteins immunology.
Kaluza, G., A.A. Kraus, and R. Rott (1975). Inhibition
of cellular protein synthesis by simultaneous pretreatment of host cells with
fowl plague virus and actinomycin D: a method for studying early protein
synthesis of several RNA viruses. Journal of Virology 17(1):
1-9. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: A method is described for analysis of viral
protein synthesis early after infection when minute amounts of viral proteins
are effectively concealed by large amounts of produced host-specific proteins.
The method is superior to a radioimmune assay, since all virus-induced proteins
can be measured independent of their immunological reactivity. Host-specific
protein synthesis can be suppressed by infection with fowl plague virus.
Addition of actinomycin C 1.25 h postinfection does not prevent this
suppression, but it does block effectively the formation of fowl plague
virus-specific proteins. Such cells synthesize only small amounts of cellular
proteins, as revealed by polyacrylamide electrophoresis. They can be
superinfected with several different enveloped viruses, however, without
significant diminution of virus yeilds. In pretreated cells the eclipse is
shortened for Semliki Forest virus, Sindbis virus, and vesicular stomatitis
virus, but prolonged for Newcastle disease virus. The onset of protein
synthesis, specific for the superinfecting virus, could be clearly demonstrated
within 1 h after superinfection. At this time, in cells superinfected with
Semliki Forest virus, great amounts of NSP 75 (nonstructural protein; molecular
weight, 75 X 10(3)) and reduced amounts of the core protein C could be
deomonstrated. The precursor glycoprotein NSP 68 is followed by a new
polypeptide, NSP 65: three proteins with molecular weights exceeding 100 X
10(3) were observed which are missing later in the infectious cycle. Similar
results were obtained after superinfection with Sindbis virus. The formation of
a new polypeptide with a molecular weight of about 80 X 10(3) was detected.
After superinfection with vesicular stomatis virus or Newcastle disease virus
the formation of new proteins, characteristic for the early stage of infeciton,
was not observed.
Descriptors: dactinomycin pharmacology, influenza A virus
avian growth and development, proteins metabolism, RNA viruses metabolism,
viral proteins biosynthesis, cell line, glycoproteins biosynthesis, molecular
weight, Newcastle disease virus growth and development, Newcastle disease virus
metabolism, peptide synthesis, protein precursors biosynthesis, Semliki Forest
virus growth and development, Semliki Forest virus metabolism, sindbis virus
growth and development, sindbis virus metabolism, tissue culture, vesicular
stomatitis Indiana virus growth and development, vesicular stomatitis Indiana
virus metabolism, virus replication drug effects.
Kaluza, G., C. Scholtissek, and R. Rott (1972). Inhibition
of the multiplication of enveloped RNA-viruses by glucosamine and
2-deoxy-D-glucose. Journal of General Virology 14(3): 251-9. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: glucosamine pharmacology, hexoses
pharmacology, RNA viruses growth and development, virus inhibitors
pharmacology, virus replication drug effects, agglutination tests, antigens,
viral analysis, cell line, cultured cells microbiology, concanavalin a
pharmacology, fluorescent antibody technique, HeLa cells, hemagglutinins viral
analysis, influenza A virus avian drug effects, Newcastle disease virus drug
effects, polioviruses drug effects, RNA nucleotidyltransferases biosynthesis,
RNA viruses drug effects, RNA viruses enzymology, RNA viruses immunology, RNA
viruses metabolism, RNA viral biosynthesis, Semliki Forest virus drug effects,
sindbis virus drug effects, viral proteins biosynthesis.
Kanegae, Y., S. Sugita, K.F. Shortridge, Y. Yoshioka,
and K. Nerome (1994). Origin and evolutionary pathways of the H1
hemagglutinin gene of avian, swine and human influenza viruses: cocirculation
of two distinct lineages of swine virus. Archives of Virology
134(1-2): 17-28. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The nucleotide sequences of the HA1 domain of
the H1 hemagglutinin genes of A/duck/Hong Kong/36/76, A/duck/Hong Kong/196/77,
A/sw/North Ireland/38, A/sw/Cambridge/39 and A/Yamagata/120/86 viruses were
determined, and their evolutionary relationships were compared with those of
previously sequenced hemagglutinin (H1) genes from avian, swine and human
influenza viruses. A pairwise comparison of the nucleotide sequences revealed
that the genes can be segregated into three groups, the avian, swine and human
virus groups. With the exception of two swine strains isolated in the 1930s, a
high degree of nucleotide sequence homology exists within the group. Two
phylogenetic trees constructed from the substitutions at the synonymous site
and the third codon position showed that the H1 hemagglutinin genes can be
divided into three host-specific lineages. Examination of 21 hemagglutinin
genes from the human and swine viruses revealed that two distinct lineages are
present in the swine population. The swine strains, sw/North Ireland/38 and
sw/Cambridge/39, are clearly on the human lineage, suggesting that they
originate from a human A/WSN/33-like variant. However, the classic swine
strain, sw/Iowa/15/30, and the contemporary human viruses are not direct
descendants of the 1918 human pandemic strain, but did diverge from a common
ancestral virus around 1905. Furthermore, previous to this the above mammalian
viruses diverged from the lineage containing the avian viruses at about 1880.
Descriptors: evolution, hemagglutinins viral genetics,
influenza A virus avian genetics, human genetics, porcine genetics, amino acid
sequence, chick embryo, genes viral, hemagglutinin glycoproteins, influenza
virus, avian classification, human classification, porcine classification,
molecular sequence data, phylogeny, sequence homology, amino acid.
Kantorovich, E.N., N.V. Kaverin, O.N. Berezina, S.A.
Moisiadi, and T.A. Bektemirov (1973). Izuchenie autointerferiruiushchikh
svoistv populiatsii virusa grippa, soderzhashchei defktnye virusnye chastitsy.
[The autointerfering properties of a population of influenza viruses containing
defective virus particles]. Voprosy Virusologii 18(5): 548-52. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: defective viruses, influenza A virus avian,
orthomyxoviridae, viral interference, chick embryo, cytopathogenic effect,
viral, fetal membranes, fibroblasts, tissue culture, virus cultivation.
Karako, N.I., E.I. Boreko, V.A. Kirillov, and V.I.
Votiakov (1989). Izmenenie virusa grippa pri razmnozhenii v prisutstvii
vysokikh kontsentratsii remantadine. [Change in the influenza virus upon
multiplication in the presence of high concentrations of remantadine]. Voprosy
Virusologii 34(1): 43-6. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: It was established that classical fowl plague
virus Rostock (H7N1) propagated in culture to which 10-25 micrograms/ml of
remantadine had been added differed from the original FPV and its
remantadine-resistant variant by markedly reduced infectious and
hemagglutinating activity and, to a lesser extent, neuraminidase activity,
lower amounts of M protein and hemagglutinin, incomplete cleavage of
hemagglutinin, and significant loss of spikes on the virion surface.
Descriptors: adamantane analogs and derivatives, influenza
A virus avian drug effects, rimantadine pharmacology, drug resistance,
microbial, electrophoresis, polyacrylamide gel, hemagglutination, viral drug
effects, hemagglutinins viral analysis, influenza A virus avian physiology,
influenza A virus avian ultrastructure, viral matrix proteins analysis, viral
proteins analysis, virus replication drug effects.
Karasin, A.I., M.M. Schutten, L.A. Cooper, C.B.
Smith, K. Subbarao, G.A. Anderson, S. Carman, and C.W. Olsen (2000). Genetic
characterization of H3N2 influenza viruses isolated from pigs in North America,
1977-1999: evidence for wholly human and reassortant virus genotypes. Virus
Research 68(1): 71-85. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: Since 1998, H3N2 viruses have caused
epizootics of respiratory disease in pigs throughout the major swine production
regions of the U.S. These outbreaks are remarkable because swine influenza in
North America had previously been caused almost exclusively by H1N1 viruses. We
sequenced the full-length protein coding regions of all eight RNA segments from
four H3N2 viruses that we isolated from pigs in the Midwestern U.S. between
March 1998 and March 1999, as well as from H3N2 viruses recovered from a piglet
in Canada in January 1997 and from a pig in Colorado in 1977. Phylogenetic
analyses demonstrated that the 1977 Colorado and 1997 Ontario isolates are
wholly human influenza viruses. However, the viruses isolated since 1998 from
pigs in the Midwestern U.S. are reassortant viruses containing hemagglutinin,
neuraminidase and PB1 polymerase genes from human influenza viruses, matrix,
non-structural and nucleoprotein genes from classical swine viruses, and PA and
PB2 polymerase genes from avian viruses. The HA proteins of the Midwestern
reassortant swine viruses can be differentiated from those of the 1995 lineage
of human H3 viruses by 12 amino acid mutations in HA1. In contrast, the
Sw/ONT/97 virus, which did not spread from pig-to-pig, lacks 11 of these
changes.
Descriptors: influenza A virus avian genetics, human
genetics, porcine classification, porcine genetics, reassortant viruses
genetics, genotype, influenza veterinary, influenza virology, molecular
sequence data, North America, phylogeny, swine, swine diseases virology.
Karelin, V., P.N. Kosiakov, and I.u.P. Gofman (1970).
Antigeny kletok khoziaina v ochishchennykh suspenziiakh virusa klassicheskoi
chumy ptits. [Host cell antigens in purified suspensions of classical fowl
plague virus]. Voprosy Virusologii 15(4): 399-404. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antigens analysis, influenza A virus avian
immunology, centrifugation, density gradient, chick embryo, chromatography,
complement fixation tests, avian isolation and purification, microscopy, electron,
virus cultivation.
Kato, N. and H.J. Eggers (1969). Inhibition of
uncoating of fowl plague virus by l-adamantanamine hydrochloride. Virology
37(4): 632-41. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, virus replication drug effects, amantadine toxicity, chick
embryo, cytopathogenic effect, viral, light, tissue culture.
Katz, J.M., J. Plowden, M. Renshaw Hoelscher, X. Lu,
T.M. Tumpey, and S. Sambhara (2004). Immunity to influenza: the challenges
of protecting an aging population. Immunologic Research 29(1-3):
113-24. ISSN: 0257-277X.
NAL
Call Number: QR180.S88
Abstract: Influenza viruses cause annual epidemics and
occasional pandemics of acute respiratory disease. Improved vaccines that can
overcome the decline in immune function with aging and/or can induce broader
immunity to novel pandemic strains are a high priority. To design improved
vaccines for the elderly, we need to better understand the effects of age on both
innate and adaptive immunity. In a murine model, we have determined that
defects in antigen-presenting cell (APC) expression of pattern-recognition
molecules, co-stimulatory molecules, and cytokine production may play an
important role in the reduced clonal expansion of T cells in aging. The use of
immunomodulators such as adjuvants may overcome some of the defects of aging
immunity and may also be useful in the development of improved vaccines for
avian influenza A subtypes that pose a pandemic threat. Several novel
strategies including the use of ISCOM-formulated vaccines, mucosal delivery, or
DNA vaccination provided cross-subtype protection that could provide an
important component of immunity in the event of a pandemic.
Descriptors: aging immunology, disease outbreaks
prevention and control, influenza prevention and control, influenza vaccines
immunology, adjuvants, immunologic pharmacology, aged, immunity, active
immunology, immunity, natural, influenza epidemiology, influenza immunology,
influenza A virus, avian immunology, avian pathogenicity, membrane
glycoproteins genetics, membrane glycoproteins metabolism, mice,
orthomyxoviridae immunology, orthomyxoviridae pathogenicity, receptors, cell
surface genetics, receptors, cell surface metabolism.
Kaverin, N.V. and H.D. Klenk (1999). Strain-specific
differences in the effect of influenza A virus neuraminidase on
vector-expressed hemagglutinin. Archives of Virology 144(4):
781-6. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: In order to evaluate the efficiency of the
removal of sialic acid residues from the influenza virus hemagglutinin by the
viral neuraminidase in the course of the virus replication cycle, CV-1 cells
expressing the hemagglutinin of H7 subtype from an SV40-based vector were
superinfected with influenza virus strain A/Duck/Ukraine/63 (H3N8) or
A/USSR/90/77 (H1N1). Vector-expressed hemagglutinin was immunoprecipitated from
cell lysates and analyzed by polyacrylamide gel electrophoresis. The data
indicate that the removal of sialic acid residues from the vector-expressed H7
hemagglutinin by N1 neuraminidase of A/USSR/90/77 virus in the course of the
virus replication cycle is incomplete. The results are discussed in connection
with previously published data showing that the low activity of NA in wild-type
influenza virus results in incomplete removal of sialic acid residues from
virion components.
Descriptors: hn protein genetics, influenza A virus avian
physiology, neuraminidase metabolism, virus replication, cell line, Cecopithecus
aethiops, ducks, genetic vectors, hn protein biosynthesis, avian
enzymology, avian genetics, simian virus 40, species specificity.
Kaverin, N.V., M. Ohuchi, R. Ohuchi, and H.D. Klenk
(1996). Phenotypic mixing with recombinant haemagglutinin of high
cleavability mediates multi-cycle replication of human influenza virus in cell
culture. Journal of General Virology 77(Pt. 1): 119-22. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: When CV-1 cells expressing haemagglutinin
(HA) of fowl plague virus A/FPV/34/Rostock(H7) (FPV) from an SV40-based
recombinant vector were superinfected with the human influenza virus
A/FM/1/47(H1N1)(FM1), phenotypically mixed progeny virus was observed. It
contained cleaved FPV HA and uncleaved FM1 HA, was infectious without trypsin
treatment and its infectivity was neutralizable by anti-FPV serum. When
superinfection of H7 HA-expressing CV-1 cells was performed at a low
multiplicity of infection, multi-cycle replication occurred. Control cells
preinfected with an SV40-based recombinant not expressing FPV HA did not allow
multi-cycle replication. Multi-cycle replication of FM1 virus was also observed
when cells were preinfected with a vector expressing a highly cleavable mutant
of influenza virus A/Port Chalmers/1/73(H3) HA carrying an insert of four
arginine residues at the cleavage site. This was not the case when cells
expressing uncleaved wild-type H3 HA were used. The results show that by
phenotypic mixing with recombinant HA of high cleavability, a human influenza
virus can be obtained in infectious form from cells lacking a suitable protease
to activate this virus.
Descriptors: hemagglutinins viral physiology, influenza A
virus avian physiology, human physiology, reassortant viruses physiology, cell
line, hemagglutinin glycoproteins, influenza virus, hemagglutinins viral
genetics, avian genetics, human genetics, phenotype, reassortant viruses
genetics, trypsin, virus replication.
Kaverin, N.V., I.A. Rudneva, N.A. Ilyushina, N.L.
Varich, A.S. Lipatov, Y.A. Smirnov, E.A. Govorkova, A.K. Gitelman, D.K. Lvov,
and R.G. Webster (2002). Structure of antigenic sites on the haemagglutinin
molecule of H5 avian influenza virus and phenotypic variation of escape
mutants. Journal of General Virology 83(Pt. 10): 2497-505. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: To elucidate the structure of the antigenic
sites of avian H5 influenza virus haemagglutinin (HA) we analysed escape
mutants of a mouse-adapted variant of the H5N2 strain
A/Mallard/Pennsylvania/10218/84. A panel of five anti-H5 monoclonal antibodies
(mAbs) was used to select 16 escape mutants. The mutants were tested by ELISA
and haemagglutination inhibition with this panel of anti-H5 mAbs and the HA
genes of the mutants were sequenced. The sequencing demonstrated that the amino
acid changes were grouped in two antigenic sites. One corresponded to site A in
the H3 HA. The other contained areas that are separated in the amino acid
sequence but are topographically close in the three-dimensional structure and
partially overlap in the reactions with mAbs. This site corresponds in part to
site B in the H3 structure; it also includes a region not involved in site B
that partially overlaps site Sa in the H1 HA and an antigenic area in H2 HA.
Mutants with the amino acid change K152N, as well as those with the change
D126N, showed reduced lethality in mice. The substitution D126N, creating a new
glycosylation site, was accompanied by an increase in the sensitivity of the
mutants to normal mouse serum inhibitors. Several amino acid changes in the H5
escape mutants occurred at the positions of reported changes in H2 drift
variants. This coincidence suggests that the antigenic sites described and
analysed here may be important for drift variation if H5 influenza virus ever
appears as a pathogen circulating in humans.
Descriptors: antigenic variation genetics, antigens, viral
genetics, epitopes, B lymphocyte genetics, hemagglutinin glycoproteins,
influenza virus genetics, influenza A virus avian genetics, antigens, viral
chemistry, antigens, viral immunology, base sequence, binding sites, birds,
DNA, viral, enzyme linked immunosorbent assay methods, epitope mapping,
epitopes, B lymphocyte chemistry, epitopes, B lymphocyte immunology,
hemagglutination inhibition tests, hemagglutinin glycoproteins, influenza virus
chemistry, hemagglutinin glycoproteins, influenza virus immunology, avian
immunology, avian pathogenicity, mice, molecular sequence data, mutagenesis,
phenotype, protein structure, tertiary, sequence analysis, DNA, virulence.
Kaverin, N.V., I.A. Rudneva, Y.A. Smirnov, and N.N.
Finskaya (1988). Human-avian influenza virus reassortants: effect of
reassortment pattern on multi-cycle reproduction in MDCK cells. Archives
of Virology 103(1-2): 117-26. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Human-avian influenza reassortants possessing
the HA gene of the avian parent virus were tested for their ability to
replicate in MDCK cells at 37 degrees C and 31 degrees C. Both avian parent
viruses, A/Duck/Ukraine/1/63 (H3N8) and A/Duck/Hoshimin/014/78 (H5N3) induced
an efficient multi-cycle infection at 37 degrees C, but replicated poorly at 31
degrees C, whereas the human parent virus, MDCK-adapted variant of A/USSR/90/77
(H1N1) strain, replicated efficiently at both temperatures. The reassortant
clone possessing the HA gene of A/Duck/Ukraine/1/63 virus and the other 7 genes
of A/USSR/90/77 virus replicated at both temperatures almost as efficiently as
the human parent virus. Among the reassortants between A/Duck/Hoshimin/014/78
and A/USSR/90/77, the clones possessing the HA and NA genes of the avian
strain, or the HA, NA, NP, and NS genes of the avian strain, and the other
genes of the human parent virus, replicated poorly at both temperatures,
especially at 31 degrees C, whereas the reassortant possessing the HA, NA, and
M genes of the avian virus replicated at both temperatures fairly efficiently.
The results are discussed in connection with the limitations imposed by
different genes upon avian influenza viruses' ability to replicate in mammalian
cells.
Descriptors: genes viral, hemagglutinins viral physiology,
influenza A virus avian pathogenicity, human pathogenicity, virus replication,
birds microbiology, chick embryo, hemagglutinins viral biosynthesis,
hemagglutinins viral genetics, avian genetics, human genetics, RNA viral
analysis, temperature, transfection, viral proteins biosynthesis.
Kaverin, N.V., Y.A. Smirnov, E.A. Govorkova, I.A.
Rudneva, A.K. Gitelman, A.S. Lipatov, N.L. Varich, S.S. Yamnikova, N.V.
Makarova, R.G. Webster, and D.K. Lvov (2000). Cross-protection and
reassortment studies with avian H2 influenza viruses. Archives of
Virology 145(6): 1059-66. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: In order to assess the degree of immune
cross-protection among avian H2 influenza virus strains, mice were immunised
with beta-propiolactone-inactivated virus preparations and infected
intranasally with mouse-adapted variant of A/Black Duck/New Jersey/1580/78
(H2N3) strain. The experiments with 11 avian H2 strains revealed that both
Eurasian and American H2 avian influenza viruses exhibit either high or
moderate degree of cross-protection. The grouping of the strains in accordance
with their cross-protection efficiency does not coincide with H2 phylogenetic
branches. Several reassortant clones were obtained with the use of A/Pintail
Duck/Primorie/695/76 (H2N3) strain and high-yield X-67 reassortant as parent
viruses, among them a high-yield H2N3 reassortant. Taking into account the data
on cross-protection among avian H2 strains, the high-yield H2N3 reassortant may
be regarded as a prototype strain to be used for the preparation of killed
vaccines in the case of a new appearance of avian H2 haemagglutinin in
circulation in humans.
Descriptors: influenza prevention and control, influenza A
virus avian genetics, avian immunology, influenza vaccine immunology,
reassortant viruses immunology, chick embryo, cross reactions, immunization,
influenza immunology, avian pathogenicity, mice, reassortant viruses genetics,
vaccines, attenuated immunology.
Kawakami, K., A. Ishihama, and M. Hamaguchi (1981). RNA
polymerase of influenza virus. I. Comparison of the virion-associated RNA
polymerase activity of various strains of influenza virus. Journal of Biochemistry
89(6): 1751-7. ISSN: 0021-924X.
NAL
Call Number: 385 J822
Abstract: A systematic and comparative study was
performed on the polypeptide composition and the RNA polymerase activity
associated with virions of various strains of influenza A virus, including four
human and two avian viruses. Significant differences were found in the
molecular weights of not only hemagglutinin (HA) but also both nucleoprotein
(NP) and membrane protein (M), as determined by polyacrylamide gel
electrophoresis under denaturing conditions. The results indicate that, among
viruses sharing the same serotype determined by the surface proteins HA and NA
(neuraminidase), considerable variations exist in the structure of viral
proteins, including inner proteins. The relative contents of viral proteins
also varied among these strains grown under similar conditions. The total
content of three P proteins, the putative RNA polymerase subunits, was within
the range between 1.1 and 2.2% of total viral proteins and roughly paralleled
the virion-associated RNA polymerase activity. The virion-associated RNA
polymerase of all the strains tested were stimulated by the same dinucleotide
primers, ApG or GpG, indicating that the specificity of transcription
initiation is conserved among wide varieties of influenza virus.
Descriptors: DNA directed RNA polymerases metabolism,
dinucleoside phosphates, influenza A virus avian enzymology, human enzymology,
5' guanylic acid analogs and derivatives, 5' guanylic acid pharmacology,
adenosine monophosphate analogs and derivatives, adenosine monophosphate
pharmacology, chemistry, guanosine analogs and derivatives, guanosine
pharmacology, macromolecular systems, molecular weight, peptides, species
specificity, virion enzymology.
Kawano, J., R. Yanagawa, and H. Kida (1979). Site
of replication of influenza virus A/budgerigar/Hokkaido/1/77 (Hav 4 Nav 1) in
budgerigars. Zentralblatt Fur Bakteriologie, Parasitenkunde,
Infektionskrankheiten Und Hygiene. Erste Abteilung Originale. Reihe A
Medizinische Mikrobiologie Und Parasitologie 245(1-2): 1-7. ISSN: 0300-9688.
NAL
Call Number: 448.3 C33 (1)
Descriptors: influenza A virus avian growth and
development, parrots microbiology, Psittacines microbiology, virus replication,
hemagglutination inhibition tests, avian isolation and purification, organ
specificity, respiratory system microbiology.
Kawaoka, Y. (1991). Difference in replication and
pathogenicity of influenza A viruses in chickens and mice. Journal of
Veterinary Medical Science the Japanese Society of Veterinary Science
53(1): 125-6. ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Descriptors: chickens microbiology, influenza A virus
avian physiology, porcine physiology, influenza A virus physiology, mice
microbiology, cloaca microbiology, avian pathogenicity, porcine pathogenicity,
influenza A virus pathogenicity, orthomyxoviridae infections microbiology,
orthomyxoviridae infections veterinary, poultry diseases microbiology, rodent
diseases microbiology, trachea microbiology, virus replication.
Kawaoka, Y. (1991). Structural features
influencing hemagglutinin cleavability in a human influenza A virus. Journal
of Virology 65(3): 1195-201. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: The cleavability of the hemagglutinin (HA)
molecule is related to the virulence of avian influenza A viruses, but its
influence on human influenza virus strains is unknown. Two structural features
are involved in the cleavage of avian influenza A virus HAs: a series of basic
amino acids at the cleavage site and an oligosaccharide side chain in the near
vicinity. The importance of these properties in the cleavability of a human
influenza A virus (A/Aichi/2/68) HA was investigated by using mutants that contained
or lacked an oligosaccharide side chain and had either four or six basic amino
acids. All mutants except the one that contains a single mutation at the
glycosylation site were cleaved, although not completely, demonstrating that a
series of basic amino acids confers susceptibility to cellular cleavage enzymes
among human influenza virus HAs. The mutants containing six basic amino acids
at the cleavage site showed limited polykaryon formation upon exposure to low
pH, indicating that cleavage was adequate to impart fusion activity to the HA.
Deletion of the potential glycosylation site had no effect on the cleavability
of these mutants; hence, the oligosaccharide side chain appears to have no role
in human influenza virus HA cleavage. The inability to induce high cleavability
in a human influenza A virus HA by insertion of a series of basic amino acids
at the cleavage site indicates that other, as yet unidentified structural
features are needed to enhance the susceptibility of these HAs to cellular proteases.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus human genetics, amino acid sequence, arginine, cell line,
chick embryo, cloning, molecular, glycosylation, hemagglutinin glycoproteins,
influenza virus, hydrolysis, human immunology, human ultrastructure, lysine,
molecular sequence data, mutagenesis,
site directed, recombination, genetic, simian virus 40 genetics, simian virus
40 ultrastructure, transfection, viral envelope proteins genetics.
Kawaoka, Y., C.W. Naeve, and R.G. Webster (1984). Is
virulence of H5N2 influenza viruses in chickens associated with loss of
carbohydrate from the hemagglutinin? Virology 139(2): 303-16. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The A/Chick/Penn/83 (H5N2) influenza virus
that appeared in chickens in Pennsylvania in April 1983 and subsequently became
virulent in October 1983, was examined for plaque-forming ability and
cleavability of the hemagglutinin (HA) molecule. The avirulent virus produced
plaques and cleaved the HA only in the presence of trypsin. In contrast, the
virulent virus produced plaques and cleaved the HA precursor into HA1 and HA2
in the presence or absence of trypsin. The apparent molecular weight of the HA1
from the avirulent virus was higher than that from the virulent virus, but when
the viruses were grown in the presence of tunicamycin, the molecular weights of
HA were indistinguishable. Two of nine monoclonal antibodies to the HA of the
avirulent virus indicate that there is at least one epitope on the HA that is
different between the virulent and avirulent viruses. The amino acid sequences
of the HAs from the two viruses were compared by sequencing their respective HA
gene. The nucleotide sequence coding for the processed HA polypeptide contained
1641 nucleotides specifying a protein of 547 amino acids. The amino acid
sequences of the virulent and avirulent viruses were indistinguishable through
the connecting peptide region, indicating that the difference in cleavability
of the H5 HA is not directly attributed to the amino acid sequence of the
connecting peptide. Four of seven nucleotide changes resulted in amino acid
changes at residues 13, 69, and 123 of HA1 and at residue 501 of the HA2
polypeptide. Since there were no deletions or insertions in the amino acid
sequence of the virulent or avirulent viruses, the possibility exists that the
difference in molecular weight is due to loss of a carbohydrate side chain in
the virulent strain. The amino acid change in the virulent strain at residue 13
is the only mutation that could affect a glycosylation site and this is in the
vicinity of the connecting peptide. It is postulated that the loss of this
carbohydrate may permit access of an enzyme that recognizes the basic amino
acid sequences and results in cleavage activation of the HA in the virulent
virus.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian pathogenicity, amino acid sequence, antibodies, monoclonal, base
sequence, carbohydrates analysis, chick
embryo, chickens, DNA, viral genetics, hemagglutinins viral isolation and
purification, avian genetics, plaque assay, RNA viral isolation and
purification, serotyping, species specificity, virulence.
Kawaoka, Y., A. Nestorowicz, D.J. Alexander, and R.G.
Webster (1987). Molecular analyses of the hemagglutinin genes of H5
influenza viruses: origin of a virulent turkey strain. Virology
158(1): 218-27. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Comparative sequence analysis of the hemagglutinin
(HA) genes of a highly virulent H5N8 virus isolated from turkeys in Ireland in
1983 and a virus of the same subtype detected simultaneously in healthy ducks
showed only four amino acid differences between these strains. Partial
sequencing of six of the other genes and antigenic similarity of the
neuraminidases established the overall genetic similarity of these two viruses.
Comparison of the complete sequence of two H5 gene sequences and partial
sequences of other virulent and avirulent H5 viruses provides evidence for at
least two different lineages of H5 influenza virus in the world, one in Europe
and the other in North America, with virulent and avirulent members in each
group. In vivo studies in domestic ducks showed that all of the H5 viruses that
are virulent in chickens and turkeys replicate in the internal organs of ducks
but did not produce any disease signs. Additionally, both viruses isolated from
turkeys and ducks in Ireland were detected in the blood. These studies provide
the first conclusive evidence for the possibility that fully virulent influenza
viruses in domestic poultry can arise directly from viruses in wild aquatic
birds. Studies on the cleavability of the HA of virulent and avirulent H5
viruses showed that the principles established for H7 viruses (F. X. Bosch, M.
Orlich, H. D. Klenk, and R. Rott, 1979, Virology 95, 197-207; F. X. Bosch, W.
Garten, H. D. Klenk, and R. Rott, 1981, Virology 113, 725-735) also apply to
the H5 subtype. These are (1) only the HAs of virulent influenza viruses were
cleaved in tissue culture in the absence of trypsin and (2) virulent H5
influenza viruses contain a series of basic amino acids at the cleavage site of
the HA, whereas avirulent strains contain only a single arginine with the
exception of the avirulent Chicken/Pennsylvania virus. Thus, a series of basic
amino acids at the cleavage site probably forms a recognition site for the
enzyme(s) responsible for cleavage.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian genetics, amino acid sequence, base sequence, chickens
microbiology, ducks microbiology, fowl plague microbiology, avian
pathogenicity, avian physiology, turkeys microbiology, virulence, virus
replication.
Kawaoka, Y. and R.G. Webster (1985). Evolution of
the A/Chicken/Pennsylvania/83 (H5N2) influenza virus. Virology
146(1): 130-7. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The epidemiological features of the H5N2
outbreak of influenza in poultry were studied by sequencing the HA genes of
several viruses isolated during the epidemic. Comparison of the nucleotide
sequences of the HA genes indicated there was a single introduction of virulent
virus. The variation rate (silent mutations) in the HA gene of the virulent
Ck/Penn virus was 9.0 or 14.4% per 10 years depending on the viruses compared
and was similar to that in H3 HA gene of human influenza A virus. The virulent
and avirulent viruses isolated after October 1983 were derived from a common
ancestoral virus and the virulent virus did not supersede the avirulent virus,
instead, the virulent and avirulent viruses coexisted and evolved separately
during the course of the epidemic. The evolutionary changes in the HA of H5N2
viruses that occurred during the epidemic permitted us to establish that a
virus (A/Chick/Washington/84) that was isolated 8 months after the last H5N2
virus had been isolated from poultry in Pennsylvania belonged to the family of
potentially dangerous H5N2 viruses and was a direct descendent of the virus
that spread to Maryland and Virginia. All of the virulent Ck/Penn viruses
retained the amino acid changes at residues 13 and 69 in the HA.
Descriptors: fowl plague microbiology, hemagglutinins
viral genetics, influenza A virus avian genetics, amino acid sequence, base
sequence, disease outbreaks veterinary,
District of Columbia, evolution, fowl plague epidemiology, genes viral,
hemagglutinins viral analysis, avian isolation and purification, avian
pathogenicity, Maryland, mutation, Pennsylvania, poultry, virulence.
Kawaoka, Y. and R.G. Webster (1989). Interplay
between carbohydrate in the stalk and the length of the connecting peptide
determines the cleavability of influenza virus hemagglutinin. Journal of
Virology 63(8): 3296-300. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: The ability of many viruses to replicate in
host cells depends on cleavage of certain viral glycoproteins, including
hemagglutinin (HA). By generating site-specific mutant HAs of two highly
virulent influenza viruses, we established that the relationship between
carbohydrate in the stalk and the length of the connecting peptide is a
critical determinant of cleavability. HAs that lacked an oligosaccharide side
chain in the stalk were cleaved regardless of the number of basic amino acids
at the cleavage site, whereas those with the oligosaccharide side chain
resisted cleavage unless additional basic amino acids were inserted. This
finding suggests that the oligosaccharide side chain interferes with HA
cleavage if the number of basic amino acids at the cleavage site is not
adequate to nullify this effect. Similar interplay could influence cleavage of
other viral glycoproteins, such as those of human and simian immunodeficiency
viruses and paramyxoviruses.
Descriptors: carbohydrates metabolism, hemagglutinins
viral metabolism, influenza A virus avian metabolism, oligosaccharides
metabolism, amino acid sequence, amino acids, glycosylation, hemagglutinins
viral genetics, avian genetics, molecular sequence data, mutation.
Kawaoka, Y. and R.G. Webster (1988). Molecular
mechanism of acquisition of virulence in influenza virus in nature. Microbial
Pathogenesis 5(5): 311-8. ISSN:
0882-4010.
NAL
Call Number: QR175.M53
Descriptors: influenza A virus avian pathogenicity,
chickens, influenza epidemiology, influenza microbiology, avian genetics,
orthomyxoviridae pathogenicity, virulence.
Kawaoka, Y. and R.G. Webster (1988). Sequence
requirements for cleavage activation of influenza virus hemagglutinin expressed
in mammalian cells. Proceedings of the National Academy of Sciences of
the United States of America 85(2): 324-8.
ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Cleavage of the hemagglutinin (HA) in tissue
culture systems has been correlated with virulence of avian influenza viruses.
To examine the structural requirements for cleavage of the HA, the HA gene from
a virulent H5 influenza virus was expressed in mammalian cells (CV-1), and the
cleavage site of the HA was explored by using site-specific mutagenesis. The
expressed HA protein exhibited normal cleavage, transport to the cell membrane,
and ability to adsorb and to fuse erythrocytes at pH 5. Site-specific
mutagenesis of the HA directly established that (i) most of the basic amino
acids at this site are critical for cleavage activation; (ii) besides the
connecting peptide sequence, at least one other structural feature of the HA is
required for enzyme recognition; and (iii) the length of the connecting peptide
can abrogate the structural feature(s).
Descriptors: hemagglutinins viral genetics, influenza A
virus human genetics, amino acid sequence, cell line, cloning, molecular, DNA
restriction enzymes, hemadsorption, hemagglutinin glycoproteins, influenza
virus, hemagglutinins viral immunology, human immunology, human pathogenicity,
plasmids, simian virus 40 genetics, species specificity, transfection,
virulence.
Keawcharoen, J., K. Oraveerakul, T. Kuiken, R.A.
Fouchier, A. Amonsin, S. Payungporn, S. Noppornpanth, S. Wattanodorn, A.
Theambooniers, R. Tantilertcharoen, R. Pattanarangsan, N. Arya, P. Ratanakorn,
D.M. Osterhaus, and Y. Poovorawan (2004). Avian influenza H5N1 in tigers and
leopards. Emerging Infectious Diseases 10(12): 2189-91. ISSN: 1080-6040.
NAL
Call Number: RA648.5.E46
Abstract: Influenza virus is not known to affect wild
felids. We demonstrate that avian influenza A (H5N1) virus caused severe
pneumonia in tigers and leopards that fed on infected poultry carcasses. This
finding extends the host range of influenza virus and has implications for
influenza virus epidemiology and wildlife conservation.
Descriptors: zoo animals virology, influenza veterinary,
influenza A virus, avian pathogenicity, Panthera virology, chickens virology,
food microbiology, influenza virology, avian genetics, lung virology, meat
virology, phylogeny, tigers virology, variation genetics.
Keil, W., R. Geyer, J. Dabrowski, U. Dabrowski, H.
Niemann, S. Stirm, and H.D. Klenk (1985). Carbohydrates of influenza virus.
Structural elucidation of the individual glycans of the FPV hemagglutinin by
two-dimensional 1H n.m.r. and methylation analysis. EMBO Journal
4(10): 2711-20. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: The structures of the oligosaccharides of the
hemagglutinin of fowl plague virus [influenza A/FPV/Rostock/34 (H7N1)] have
been elucidated by one- and two-dimensional 1H n.m.r. spectroscopy at 500 MHz
and by microscale methylation analysis. N-Glycosidic oligosaccharides of the
oligomannosidic (OM) and of the N-acetyllactosaminic type have been found, the
latter type comprising biantennary structures, without (A) or with (E)
bisecting N-acetylglucosamine, and triantennary (C) structures. Analysis of the
tryptic and thermolytic glycopeptides of the hemagglutinin allowed the
allocation of these oligosaccharides to the individual glycosylation sites.
Each attachment site contained a unique set of oligosaccharides. Asn12 contains
predominantly structures C and E which are highly fucosylated. Asn28 contains
OM and A structures that lack fucose and sulfate. Asn123 shows A that has
incomplete antennae but is highly fucosylated and sulfated. Asn149 has
fucosylated A and E. Asn231 shows fucosylated A and E with incomplete antennae.
Asn406 has OM oligosaccharides. Asn478 has A and E with little fucose.
Localization of the oligosaccharides on the three-dimensional structure of the
hemagglutinin revealed that the oligomannosidic glycans are attached to
glycosylation sites at which the enzymes responsible for carbohydrate
processing do not have proper access. These observations demonstrate that an
important structural determinant for the oligosaccharide side chains is the
structure of the glycoprotein itself. In addition, evidence was obtained that
the rate of glycoprotein synthesis also has an influence on carbohydrate
structure.
Descriptors: glycoproteins, hemagglutinins viral,
influenza A virus avian, glycopeptides analysis, magnetic resonance
spectroscopy, methylation, oligosaccharides analysis, protein processing, post
translational.
Keil, W., H.D. Klenk, and R.T. Schwarz (1979). Carbohydrates
of influenza virus. III. Nature of oligosaccharide-protein linkage in viral
glycoproteins. Journal of Virology 31(1): 253-6. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Four different glycopeptides can be
distinguished after pronase digestion of influenza A virus glycoproteins: Ia
and Ib, containing N-acetylglucosamine, mannose, galactose, and fucose, and IIa
and IIb, containing mannose and N-acetylglucosamine. All glycopeptides yielded
N-acetylglucosaminyl-asparagine after mild acid hydrolysis. There was no
evidence for O-glycosidic bonds. Thus, the carbohydrate complement is linked to
the polypeptide exclusively by N-glycosidic linkages between N-acetylglucosamine
and asparagine.
Descriptors: glycoproteins analysis, influenza A virus
analysis, viral proteins analysis, acetylglucosamine analysis, asparagine
analysis, carbohydrate conformation, glycopeptides analysis, influenza A virus
avian analysis, molecular weight, oligosaccharides analysis, protein
conformation.
Keil, W., H. Niemann, R.T. Schwarz, and H.D. Klenk
(1984). Carbohydrates of influenza virus. V. Oligosaccharides attached to
individual glycosylation sites of the hemagglutinin of fowl plague virus. Virology
133(1): 77-91. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The carbohydrate side chains of the
hemagglutinin of fowl plague virus (A/FPV/Rostock/34 (H7N1] have been localized
by a procedure involving fragmentation of the polypeptide with cyanogen bromide
and various proteases. The positions of the fragments were determined by
radioactive labeling of the sugars and of specific amino acids. Side chains of
the complex type I are attached to asparagine residues 12, 28, 123, 149, and
478. A mannose-rich (type II) side chain is linked to asparagine 406.
Asparagine 231 is not glycosylated. The side chains attached to asparagine
residues 12, 123, 149, and 478 contain sulfate. Glycopeptides derived by
Pronase digestion from the individual attachment sites have been analyzed by
their affinity to concanavalin A and Lens culinaris agglutinin. The results
indicate that each glycosylation site has a typical set of heterogeneous
oligosaccharides. Comparison of the glycosylation patterns of the
hemagglutinins of FPV and other influenza A viruses reveals that the
glycosylation sites at asparagine residues 12, 28, and 478, which are located
at the base of the spike, are highly conserved. Mannose-rich side chains appear
to be located preferentially at interfaces between the three monomers of a
spike or between the globular and fibrous domains of a monomer.
Descriptors: hemagglutinins viral isolation and
purification, influenza A virus avian immunology, oligosaccharides analysis,
serine endopeptidases, acetylglucosaminidase, amino acid sequence,
chromatography, affinity, cyanogen bromide, endopeptidases, glycopeptides
analysis, hemagglutinins viral genetics, mannosyl glycoprotein endo beta
N-acetylglucosaminidase, pronase,
trypsin.
Kelly, D.C., R.J. Avery, and N.J. Dimmock (1974). Failure
of an influenza virus to initiate infection in enucleate BHK cells. Journal
of Virology 13(6): 1155-61. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Descriptors: cell nucleus physiology, orthomyxoviridae growth
and development, virus replication, antigens, viral analysis, cell line,
electrophoresis, polyacrylamide gel, fluorescent antibody technique, hamsters,
influenza A virus avian growth and development, kidney, methionine, Newcastle
disease virus growth and development, nucleic acid hybridization, peptides
analysis, sulfur radioisotopes, tritium, uridine, vaccinia virus growth and
development.
Kelly, D.C. and N.J. Dimmock (1974). Fowl plaque
virus replication in mammalian cell-avian erythrocyte heterokaryons: studies
concerning the actinomycin D and ultra-violet light sensitive phase in
influenza virus replication. Virology 61(1): 210-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cell nucleus microbiology, dactinomycin
pharmacology, influenza A virus avian growth and development, ultraviolet rays,
virus replication drug effects, virus replication radiation effects, antigens,
viral analysis, autoradiography, cell fusion, cell line, cell nucleus
immunology, cultured cells cytology, chick embryo, chickens, erythrocytes
cytology, fluorescent antibody technique, hamsters, hemagglutinins viral, avian
immunology, avian metabolism, kidney, l cells cell line, mice, neuraminidase
biosynthesis, nucleoproteins biosynthesis, radiation effects, viral proteins
biosynthesis.
Kendal, A.P. and H.D. Klenk (1991). Amantadine
inhibits an early, M2 protein-dependent event in the replication cycle of avian
influenza (H7) viruses. Archives of Virology 119(3-4): 265-73. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Analysis of the effects of amantadine during
a single cycle of replication of A/FPV/Rostock virus in vitro showed that, as
with other influenza A viruses, an M2 protein-dependent step early in infection
was inhibited. No effect was observed on later steps in replication under the
conditions used.
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, viral matrix proteins biosynthesis, viral matrix proteins
drug effects, viral matrix proteins genetics, base sequence, avian genetics,
avian physiology, molecular sequence data, mutation, viral proteins
biosynthesis, virus replication drug effects.
Khadzhiev, G. (1974). Vurkhu adsorbtsiiata na
khemaglutininite na virusi na psevdochumata na mozuchni kletki in vitro [Absorption
of hemagglutinins from the pseudopest virus by brain cells in vitro]. Veterinarnomeditsinski Nauki 11(5):
93-7. ISSN: 0324-1068.
NAL
Call Number: 41.8 V6468
Descriptors: brain metabolism, hemagglutinins viral
metabolism, influenza A virus avian immunology, brain cytology, cultured cells,
chick embryo, tissue culture metabolism.
Kharitonenko, I.G., I.U.A. Zakomyrdin, A.K.
Gitel'man, and A.G. Bukrinskaia (1980). Izuchenie struktury lipidnoi
obolochki virionov grippa, vyrashchennykh v raznykh khoziaevakh. [Structural
study of the lipid envelope of influenza virions grown in different hosts].
Voprosy Virusologii (6): 708-12.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian analysis, lipids
analysis, virion analysis, carcinoma, Ehrlich tumor microbiology, chick embryo,
electron spin resonance spectroscopy methods, spin labels, virus cultivation.
Kharitonenkov, I.G., V.P. Ginzburg, A.I. Klimov, and
A.N. Tikhonov (1982). Vzaimodeistvie remantadina s lipidnoi membranoi
chuvstvitel'nykh i rezistentnykh k preparatu variantov virusa grippa.
[Interaction of rimantadine with the lipid membrane of influenza virus variants
sensitive to the drug]. Voprosy Virusologii 27(5): 52-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: adamantane analogs and derivatives,
orthomyxoviridae drug effects, rimantadine pharmacology, drug resistance,
microbial, influenza A virus avian drug effects, influenza A virus drug
effects, variation genetics.
Khatchikian, D., M. Orlich, and R. Rott (1989). Increased
viral pathogenicity after insertion of a 28S ribosomal RNA sequence into the
haemagglutinin gene of an influenza virus. Nature 340(6229): 156-7. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Abstract: The haemagglutinin glycoprotein HA of
influenza viruses is responsible for the attachment of the virus to neuraminic
acid-containing receptors at the cell surface and subsequent penetration by
triggering fusion of the viral envelope with cellular membranes. To express
full activity of the newly synthesized precursor, HA has to be modified by
post-translational proteolytic cleavage into the polypeptides HA1 and HA2 by
cellular enzymes. If proteases suitable for cleavage are not present in the
host cell, the resulting virus particles are non-infectious. During adaptation
of the apathogenic influenza virus A/turkey/Oregon/71 to chicken embryo cells,
which are not permissive for HA cleavage, we obtained an infectious virus
variant with increased pathogenicity. Sequence analysis revealed that during
adaptation 54 nucleotides were inserted into the HA gene; their sequence
corresponds to a region of the 28S ribosomal RNA. This insertion is probably
responsible for increased cleavability of HA, as well as for infectivity and
pathogenicity of the adapted virus.
Descriptors: DNA transposable elements, hemagglutinins
viral genetics, influenza A virus avian pathogenicity, RNA, ribosomal genetics,
ribosomal, 28S genetics, base sequence, cloning, molecular, hemagglutinin
glycoproteins, influenza virus, avian genetics, molecular sequence data,
recombinant fusion proteins genetics, turkeys, viral fusion proteins
metabolism, virulence.
Kida, H., L.E. Brown, and R.G. Webster (1982). Biological
activity of monoclonal antibodies to operationally defined antigenic regions on
the hemagglutinin molecule of A/Seal/Massachusetts/1/80 (H7N7) influenza virus.
Virology 122(1): 38-47. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, antibodies, monoclonal, antibodies, viral, antibody
specificity, antigen antibody reactions, epitopes.
Kida, H., R. Yanagawa, and Y. Matsuoka (1980). Duck
influenza lacking evidence of disease signs and immune response. Infection
and Immunity 30(2): 547-53. ISSN:
0019-9567.
NAL
Call Number: QR1.I57
Abstract: Influenza viruses A/duck/Hokkaido/5/77
(Hav7N2), A/budgerigar/Hokkaido/1/77 (Hav4Nav1), A/Kumamoto/22/76 (H3N2),
A/Aichi/2/68 (H3N2), and A/New Jersey/8/76 (Hsw1N1) were experimentally
inoculated into Pekin ducks. Of these, the influenza viruses of duck and
budgerigar origin replicated in the intestinal tract of the ducks. The infected
ducks shed the virus in the feces to high titers, but did not show clinical
signs of disease and scarcely produced detectable serum antibodies. Using
immunofluorescent staining, we demonstrated that the target cells of the duck
virus in ducks were the simple columnar epithelial cells which form crypts in
the large intestines, especially in the colon. After primary infection, the
birds resisted reinfection with the duck virus at least for 28 days, but from
46 days onward they were susceptible to reinfection. These infections were
quickly restricted by a brisk secondary immune response, reflected in the rapid
appearance of high titers of antibody after reinoculation. In contrat to the
avian influenza viruses, the remaining three influenza viruses of human origin
did not replicate in the intestinal tract but did cause a serum antibody
response.
Descriptors: ducks microbiology, influenza veterinary,
influenza A virus avian growth and development, antibody formation, digestive
system microbiology, feces microbiology, influenza immunology, human growth and
development, parakeets microbiology, virus replication.
King, A.P. and K.F. Shortridge (1982). Multiple
avain influenza infection: selection of a non-avid virus by a heterologous
avain host. Research in Veterinary Science 33(1): 127-9. ISSN: 0034-5288.
NAL
Call Number: 41.8 R312
Abstract: Experimental infection of domestic fowl,
ducks and geese with an influenza A virus (H7N2) isolated from a domestic duck
showed that this virus was apathogenic for these poultry. A second virus
(H6N2), also apathogenic and more 'non-avid' than any such isolates previously
recognised in surveillance of domestic poultry in Hong Kong, was isolated from
one goose after H7N2 shedding had ceased. This goose, in effect, acted as a
selective isolation system for the H6N2 virus whose presence in the field
isolate could not be detected in spite of multiple passage in embryonated eggs.
Descriptors: chickens microbiology, ducks microbiology,
fowl plague microbiology, geese microbiology,
influenza A virus avian pathogenicity, poultry diseases microbiology.
Kishida, N., Y. Sakoda, M. Eto, Y. Sunaga, and H.
Kida (2004). Co-infection of Staphylococcus aureus or Haemophilus
paragallinarum exacerbates H9N2 influenza A virus infection in chickens.
Archives of Virology 149(11): 2095-104.
ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: H9N2 influenza viruses are frequently
isolated from chicken meat and bone marrow imported from China to Japan since
2001. These isolates were experimentally inoculated into specific pathogen-free
chickens intranasally. Viruses were recovered from the meat and bone marrow of
birds showing no overt signs. On the other hand, chickens co-infected with H9N2
virus and either Staphylococcus aureus or Haemophilus paragallinarum
showed clinical signs severer than those shown by birds infected only with the
virus alone or each of the bacteria alone. In addition, H9N2 viruses were more
efficiently recovered from the chickens co-infected with S. aureus or H.
paragallinarum than those from the birds infected with only the virus. The
present results indicate that co-infection of H9N2 influenza virus with S.
aureus or H. paragallinarum enhances the replication of the virus in
chickens, resulting in exacerbation of the H9N2 virus infection.
Descriptors: chickens virology, haemophilus infections
veterinary, Haemophilus paragallinarum, influenza A virus, avian,
influenza, avian virology, poultry diseases virology, staphylococcal infections
veterinary, chickens microbiology, haemophilus infections complications,
poultry diseases microbiology, specific pathogen free organisms, staphylococcal
infections complications, virus replication.
Kistner, O., K. Muller, and C. Scholtissek (1989). Differential
phosphorylation of the nucleoprotein of influenza A viruses. Journal of
General Virology 70(Pt. 9): 2421-31.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: An analysis of the nucleoprotein (NP) of 29
different influenza A viruses by phosphopeptide fingerprinting revealed three
prototype patterns. The first, which was a complex pattern consisting of six to
seven phosphopeptides, another which was relatively simple consisted of two or
three phosphopeptides, and a third one which was complex but was missing the
main phosphopeptide shared by the two other patterns. Phosphoserine was the
only labelled phosphamino acid detected. A tentative deduction of two of the
phosphate attachment sites (serine residues at positions 3 and 473) could be
made by comparison of the known amino acid sequences of the NPs of 25 strains.
No correlation was found between species specificity or subtype or year of
isolation of the strains. During the infectious cycle the fingerprint underwent
significant changes, indicating subtle phosphorylation and dephosphorylation of
the NP at various stages during viral multiplication. Most of the
phosphopeptides were metabolically stable; however one major phosphopeptide,
which was not found in the NP of mature virions, exhibited a high turnover
(presumably serine at position 3). The phosphopeptide fingerprint could be
significantly influenced in vivo by the specific stimulation of cellular
protein kinase C by the phorbol ester 12-O-tetradecanoylphorbol 13-acetate or
by its inhibition with the isoquinoline sulphonamide H7.H7 specifically inhibited
the replication of influenza A viruses by deregulation of viral protein
synthesis without interfering with the multiplication of a parainfluenza virus
(Newcastle disease virus), an alphavirus (Semliki Forest virus) or a flavivirus
(West Nile). Therefore the correct phosphorylation of the NP of influenza
viruses appears to be essential for influenza virus replication.
Descriptors: influenza A virus analysis, nucleoproteins
isolation and purification, phosphoproteins isolation and purification, 1 5
isoquinolinesulfonyl 2 methylpiperazine, amino acids analysis, chick embryo,
influenza A virus avian analysis, influenza A virus avian physiology, influenza
A virus human analysis, influenza A virus, porcine analysis, influenza A virus metabolism, isoquinolines pharmacology,
nucleoproteins metabolism, peptide mapping, phosphopeptides isolation and
purification, phosphoproteins biosynthesis, phosphorylation, piperazines
pharmacology, protein kinase c metabolism, species specificity,
tetradecanoylphorbol acetate pharmacology, virus replication.
Kiyotani, K., N. Takei, M. Senoo, S. Takao, K.
Otsuki, M. Tsubokura, and T. Yoshida (1987). Enzymological characteristics
of avian influenza A virus neuraminidase. Microbiology and Immunology
31(11): 1131-5. ISSN: 0385-5600.
NAL
Call Number: 448.8 J273
Abstract: Neuraminidases of 18 strains of avian
influenza A virus were examined by both colorimetric and fluorometric assays
using fetuin and 4-methylumbelliferyl-N-Ac-alpha-D-neuraminide as substrates,
respectively, to compare them with those of human influenza A and B viruses.
The ratios of the neuraminidase activity of avian influenza virus measured by
the colorimetric assay method to that measured by the fluorometric assay were
distributed in the range of 2.4-20.3. The enzyme of avian influenza virus
showed calcium-ion dependence in both assay methods. These results suggest that
neuraminidase of avian influenza A virus is varies greatly from one strain to
another in substrate specificity as compared with those of human influenza A
and B viruses, and that some strains of avian influenza A virus have a
neuraminidase with unique enzymological characteristics different from that of
human influenza A virus as well as that of influenza B virus.
Descriptors: influenza A virus avian enzymology,
neuraminidase metabolism, colorimetry, edetic acid pharmacology, epitopes,
fluorometry, species specificity, substrate specificity.
Kleineidam, R.G., K. Furuhata, H. Ogura, and R.
Schauer (1990). 4-Methylumbelliferyl-alpha-glycosides of partially
O-acetylated N-acetylneuraminic acids as substrates of bacterial and viral
sialidases. Biological Chemistry Hoppe Seyler 371(8): 715-9. ISSN: 0177-3593.
NAL
Call Number: 384 Z38
Abstract: 4-O-Acetylated, 7-O-acetylated, and
9-O-acetylated 4-methylumbelliferyl-alpha-N-acetyl-neuraminic acids
(Neu4,5Ac2-MU, Neu5,7Ac2-MU, Neu5,9Ac2-MU) were tested as substrates of
sialidases of Vibrio cholerae and of Clostridium perfringens.
Both sialidases were unable to hydrolyse Neu4,5Ac2-MU. This compound at 1 mM
concentration did not inhibit significantly the cleavage of Neu5Ac-MU, the best
substrate tested. The 4-O-acetylated sialic acid glycoside is hydrolysed slowly
by the sialidase from fowl plague virus. The relative substrate specificity,
reflected in V/Km of the Vibrio cholerae sialidase is Neu5Ac-MU much
greater than Neu5,7Ac2-MU approximately Neu5,9Ac2-MU and of the clostridial
enzyme it is Neu5Ac-MU greater than Neu5,9Ac2-MU greater than Neu5,7Ac2-MU. The
affinities of both enzymes for the side-chain O-acetylated sialic acid
derivatives are higher than for Neu5Ac-MU. The artificial, well-defined
substrates, described here, provide the opportunity to quantify the influence
of sialic acid O-acetylation on the hydrolysis of sialoglycoconjugates without the
side effects introduced by other parts of more complex glycans.
Descriptors: glycosides metabolism, hymecromone analogs
and derivatives, neuraminidase metabolism, sialic acids metabolism,
acetylation, Clostridium perfringens enzymology, hymecromone metabolism,
influenza A virus avian enzymology, kinetics, species specificity, substrate
specificity, Vibrio cholerae
enzymology.
Klenk, H.D. (1983). Biosynthesis of myxovirus
glycoproteins with special emphasis on mutants defective in glycoprotein
processing. Methods in Enzymology 96: 434-43. ISSN: 0076-6879.
NAL
Call Number: QP601.M49
Descriptors: glycoproteins genetics, influenza A virus
avian genetics, mutation, viral proteins genetics, cell line, cell membrane
metabolism, cell transformation, viral, cultured cells, chick embryo, dogs,
glycoproteins isolation and purification, hamsters, kidney, Newcastle disease
virus genetics, Newcastle disease virus isolation and purification,
parainfluenza virus 1, human genetics, parainfluenza virus 1, human isolation
and purification, viral proteins isolation and purification.
Klenk, H.D., H. Becht, and R. Rott (1974). Reaction
of viruses and virus-infected cells with heterophile agglutinins. Annals
of the New York Academy of Sciences 234(0): 355-68. ISSN: 0077-8923.
NAL
Call Number: 500 N484
Descriptors: antigen antibody reactions, antigens, viral,
cultured cells immunology, influenza A virus avian immunology, lectins, cell
line, chick embryo, concanavalin A, fibroblasts, glycoproteins immunology,
hamsters, HeLa cells, hemadsorption, hemadsorption inhibition tests, avian
ultrastructure, kidney, l cells cell line, mice, viral proteins biosynthesis,
viral proteins immunology, virus replication.
Klenk, H.D., W. Garten, and R. Rott (1984). Inhibition
of proteolytic cleavage of the hemagglutinin of influenza virus by the
calcium-specific ionophore A23187. EMBO Journal 3(12): 2911-5. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: At calcium-specific ionophore A23187
concentrations of approximately 0.25 microM [which still allow assembly and
release of fowl plague virus (FPV) particles] post-translational proteolytic
cleavage of the viral hemagglutinin precursor HA into the fragments HA1 and HA2
is inhibited. The resulting virus particles with uncleaved hemagglutinin, that
cannot be obtained under normal conditions, provide a suitable substrate for in
vitro assays of the protease sensitivity of the FPV hemagglutinin. Proteolytic
activation is accomplished with trypsin. Treatment with cathepsin B at low pH yields
aberrant cleavage products suggesting that the cellular cleavage enzyme is not
of lysosomal origin. A protease that cleaves the FPV hemagglutinin in the
correct place can be detected in lysates of MDBK cells. This enzyme is calcium
dependent and has a neutral pH optimum.
Descriptors: calcimycin pharmacology, influenza A virus
avian genetics, thermolysin metabolism, viral envelope proteins analysis, viral
matrix proteins, cattle, cell line, hamsters, hemagglutination tests, avian
drug effects, kidney, plaque assay, virus replication drug effects.
Klenk, H.D., W. Keil, H. Niemann, R. Geyer, and R.T.
Schwarz (1983). The characterization of influenza A viruses by carbohydrate
analysis. Current Topics in Microbiology and Immunology 104:
247-57. ISSN: 0070-217X.
NAL
Call Number: QR1.C8
Descriptors: carbohydrates analysis, hemagglutinins viral
analysis, influenza A virus avian analysis, influenza A virus analysis,
chemistry, glycopeptides analysis, avian immunology, human analysis, porcine
analysis, influenza A virus classification, influenza A virus immunology,
serotyping, species specificity.
Klenk, H.D., K. Kuroda, E. Kretzschmar, R. Geyer, A.
Groner, and W. Doerfler (1991). Processing of influenza virus hemagglutinin
in insect cells. Behring Institute Mitteilungen (89): 27-34. ISSN: 0301-0457.
NAL
Call Number: QR180.B4
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, influenza A virus genetics, baculoviridae genetics,
carbohydrate conformation, cell line, genetic vectors, hemadsorption,
hemagglutinin glycoproteins, influenza virus, avian physiology, influenza A
virus physiology, insects, larva, moths, oligosaccharides analysis, viral
envelope proteins genetics.
Klenk, H.D. and R. Rott (1973). Formation of
influenza virus proteins. Journal of Virology 11(6): 823-31. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Descriptors: influenza A virus avian metabolism, viral
proteins biosynthesis, amino acids metabolism, carbon isotopes, chick embryo,
electrophoresis, polyacrylamide gel, fibroblasts, fluorine, glucosamine
metabolism, glycoproteins biosynthesis, glycoproteins metabolism, hemagglutination
tests, hemagglutinins viral, influenza A virus avian growth and development,
isoflurophate pharmacology, peptide synthesis, phenylalanine pharmacology,
plaque assay, protein precursors biosynthesis, temperature, tissue culture,
tritium, viral proteins metabolism,
virus replication.
Klenk, H.D., R. Rott, and H. Becht (1972). On the
structure of the influenza virus envelope. Virology 47(3):
579-91. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: carbohydrates analysis, influenza A virus
avian analysis, lipids analysis, viral proteins analysis, agglutination tests,
antigens, viral analysis, bromelains, carbon isotopes, centrifugation, density
gradient, chick embryo, concanavalin a, electrophoresis, disc, erythrocytes
immunology, fibroblasts, glycoproteins
analysis, avian immunology, microscopy, electron, molecular weight, peptides
analysis, sucrose, tissue culture, tritium, virus cultivation.
Klenk, H.D., R. Rott, and M. Orlich (1977). Further
studies on the activation of influenza virus by proteolytic cleavage of the
haemagglutinin. Journal of General Virology 36(1): 151-61. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: glycoproteins metabolism, hemagglutinins
viral, influenza A virus avian growth and development, influenza A virus growth
and development, viral proteins metabolism, chick embryo, glycosaminoglycans
metabolism, avian metabolism, influenza A virus metabolism, peptide hydrolases
metabolism, tissue culture, trypsin metabolism, virus replication.
Klenk, H.D., R. Rott, M. Orlich, and J. Blodorn
(1975). Activation of influenza A viruses by trypsin treatment. Virology
68(2): 426-39. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: orthomyxoviridae pathogenicity, trypsin
pharmacology, adsorption, arteritis virus, equine analysis, arteritis virus,
equine growth and development, arteritis virus, equine pathogenicity, chick
embryo, fetal membranes, glycoproteins analysis, hemagglutinins viral analysis,
influenza A virus avian analysis, avian growth and development, avian
pathogenicity, human analysis, human growth and development, human
pathogenicity, porcine analysis, porcine growth and development, porcine
pathogenicity, peptides analysis, tissue culture, viral proteins analysis,
virulence, virus replication.
Klenk, H.D., C. Scholtissek, and R. Rott (1972). Inhibition
of glycoprotein biosynthesis of influenza virus by D-glucosamine and
2-deoxy-D-glucose. Virology 49(3): 723-34. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: glucosamine pharmacology, glucose
pharmacology, glycoproteins biosynthesis, influenza A virus avian metabolism,
viral proteins biosynthesis, amino acids metabolism, carbon isotopes, cultured
cells metabolism, cultured cells microbiology, chick embryo, chromatography, electrophoresis,
polyacrylamide gel, fibroblasts microbiology, fucose metabolism, galactose
metabolism, hemagglutinins viral biosynthesis, avian enzymology, avian growth
and development, molecular weight, neuraminidase biosynthesis, peptide
synthesis, stereoisomerism, tritium,
uridine metabolism.
Klenk, H.D., W. Wollert, R. Rott, and C. Scholtissek
(1974). Association of influenza virus proteins with cytoplasmic fractions.
Virology 57(1): 28-41. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cultured cells metabolism, glycoproteins
metabolism, influenza A virus avian metabolism, viral proteins metabolism,
carbon radioisotopes, cell fractionation, cell line, chick embryo, DNA directed
RNA polymerases metabolism, electrophoresis, polyacrylamide gel, fibroblasts,
glucosamine pharmacology, glucose pharmacology, glycoproteins analysis, avian
analysis, avian enzymology, avian growth and development, microscopy, electron,
neuraminidase metabolism, nucleoproteins analysis, peptides analysis, subcellular
fractions analysis, subcellular fractions metabolism, tritium, viral proteins analysis.
Klimov, A., Y. Ghendon, H. Zavadova, J. Broucek, and
T. Medvedeva (1983). High reproduction capacity of recombinants between H3N2
human influenza and fowl plague viruses is due to the gene coding for M
proteins. Acta Virologica 27(5): 434-8. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Recombinants between H3N2 human influenza
viruses (A/Victoria/3/75 and A/Bangkok/1/79, low-yielding parents in chick embryos)
and fowl plague virus (FPV, a high-yielding parent in chick embryos) have been
obtained. The high reproductive capacity of recombinants in chick embryos has
been shown to be due to the gene coding for M proteins.
Descriptors: genes viral, influenza A virus avian
genetics, human genetics, recombination, genetic, viral proteins genetics,
virus replication, chick embryo, avian physiology, human physiology, viral
matrix proteins.
Klimov, A., S. Prosch, J. Schafer, and D. Bucher (1992).
Subtype H7 influenza viruses: comparative antigenic and molecular analysis
of the HA-, M-, and NS-genes. Archives of Virology 122(1-2):
143-61. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Antigenic analysis of the haemagglutinin and matrix
protein with corresponding sets of monoclonal antibodies as well as sequence
analysis of HA-, M-, and NS-genes were carried out to establish antigenic and
genetic relationships between four fowl plague virus (FPV) strains of H7
subtype. The data obtained revealed close genetic relatedness between the
oldest known influenza A virus, A/chicken/Brescia/1902 (H7N7), and two FPV
strains, A/FPV/Dobson (H7N7) and A/FPV/Weybridge (H7N7). These three strains
apparently differ in all genes investigated from the A/FPV/Rostock isolate.
Descriptors: capsid genetics, genes viral, hemagglutinins
viral genetics, influenza A virus avian genetics, viral core proteins genetics,
viral matrix proteins genetics, amino acid sequence, base sequence, capsid
immunology, DNA, viral, deoxyribonucleotides, hemagglutinin glycoproteins,
influenza virus, hemagglutinins viral immunology, avian immunology, molecular
sequence data, sequence homology, nucleic acid, species specificity, viral core
proteins immunology, viral matrix proteins immunology, viral nonstructural
proteins.
Klimov, A.I. and Y.Z. Ghendon (1975). The effect
of the isolation procedure on the transcriptase activity of fowl plaque virus
ribonucleoprotein. Acta Virologica 19(1): 91. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: centrifugation, density gradient methods, DNA
directed RNA polymerases metabolism, influenza A virus avian enzymology,
nucleoproteins isolation and purification, viral proteins isolation and
purification, cell free system, deoxycholic acid, mercaptoethanol, sucrose,
tritium, uracil nucleotides metabolism, urea.
Klimov, A.I. and Y.Z. Ghendon (1976). Investigation
on the biological activity of fowl plague virus ribonucleoprotein. Acta
Virologica 20(4): 273-82. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Fowl plague virus (FPV) ribonucleoprotein
(RNP) bands in sucrose density gradient in a heterogeneous peak with
sedimentation coefficients from 45 to 70 S, whereas in cesium chloride gradient
it has a homogeneous density of 1.33-1.34 g/cm3. FPV RNP contains 7.4-8% RNA.
Upon inoculation of chick embryo cell cultures. FPV RNP shows no infectivity,
does not induce virus-specific protein synthesis and does not participate in
complementation or recombination interactions with ts mutants of FPV. The
biological activity of FPV RNP demonstrable under certain experimental
conditions is due to admixture of undestroyed virions and is completely
eliminated by treatment of the preparation with gamma-globulin fraction of
antiserum to FPV haemagglutinin, but not with antiserum to RNP proteins.
Descriptors: influenza A virus avian analysis, influenza A
virus avian metabolism, RNA viral analysis, viral proteins analysis, viral
proteins biosynthesis, centrifugation, density gradient, genetic
complementation test, immune sera, peptides analysis, recombination, genetic,
ribonucleases.
Klimov, A.I., S.G. Markushin, S. Prosch, V.P.
Ginzburg, H. Heider, A.M. Heider, C. Schroeder, and R.G. Webster (1992). Relation
between drug resistance and antigenicity among norakin-resistant mutants of
influenza A (fowl plague) virus. Archives of Virology 124(1-2):
147-55. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Norakin-resistant (NR) mutants of fowl plague
virus (A/FPV/Weybridge, H7N7) have 1 to 2 (in one instance 3) amino acid
substitutions in different positions of the heavy (HA 1) and/or light (HA 2)
subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using
the haemagglutination inhibition test with monoclonal antibodies (MAb) to the
HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR
1) differs antigenically from the wild-type fowl plague virus: its
haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast,
MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus
under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These
findings suggest a possibility of correlation between alteration of influenza
virus antigenicity and change of its sensitivity to drugs whose target is the
haemagglutinin. This potential effect should be taken into account when
antiviral substances directed to surface influenza virus antigens are being
developed for use as antiviral drugs.
Descriptors: drug resistance, microbial genetics, fowl
plague genetics, hemagglutinins viral genetics, influenza A virus avian
genetics, piperidines pharmacology, amino acid sequence, antibodies, monoclonal immunology, chick
embryo, epitopes immunology, fowl plague immunology, hemagglutinin
glycoproteins, influenza virus, influenza A virus avian drug effects, influenza
A virus avian immunology, molecular sequence data, mutation genetics.
Klimov, A.I., R.I.A. Podcherniaeva, G.A. Danlybaeva,
V.V. Iaros, and K.V. Lisovskaia (1992). Reproduktsiia reassortantov virusov
grippa A i B s izvestnym sostavom genoma v razlichnykh kletochnykh sistemakh.
[The reproduction of reassortant influenza A and B viruses with a known genome
composition in different cell systems]. Voprosy Virusologii 37(1):
31-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Reproduction of parental strains and
reassortants (with known genome composition) of influenza A and B viruses was
studied in chick embryos (CE) and in different cell lines (SPEV, MDCK, BHK-21,
M22, etc.). The results agree with the concept that the yield of influenza A
virus in CE depends on its M-gene. At the same time, the experimental results
suggest that reproduction of influenza B virus in the same system is not
determined by M-gene. Reproduction (hr-phenotype) of influenza A and B viruses
in cell cultures was shown to be determined not only by the gene coding for
hemagglutinin but also by other virus genes, the reproduction level being
dependent on different genes in different cell systems.
Descriptors: genome, viral, influenza A virus avian
physiology, influenza B virus physiology, reassortant viruses physiology, virus
replication physiology, cell line, influenza A virus avian genetics, influenza
B virus genetics, reassortant viruses genetics, virus cultivation, virus
replication genetics.
Kobasa, D., K. Wells, and Y. Kawaoka (2001). Amino
acids responsible for the absolute sialidase activity of the influenza A virus
neuraminidase: relationship to growth in the duck intestine. Journal of Virology
75(23): 11773-80. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The 1957 human pandemic strain of influenza A
virus contained an avian virus hemagglutinin (HA) and neuraminidase (NA), both
of which acquired specificity for the human receptor, N-acetylneuraminic acid
linked to galactose of cellular glycoconjugates via an alpha2-6 bond
(NeuAcalpha2-6Gal). Although the NA retained considerable specificity for
NeuAcalpha2-3Gal, its original substrate in ducks, it lost the ability to support
viral growth in the duck intestine, suggesting a growth-restrictive change
other than a shift in substrate specificity. To test this possibility, we
generated a panel of reassortant viruses that expressed the NA genes of human
H2N2 viruses isolated from 1957 to 1968 with all other genes from the avian
virus A/duck/Hong Kong/278/78 (H9N2). Only the NA of A/Singapore/1/57 supported
efficient viral growth in the intestines of orally inoculated ducks. The
growth-supporting capacity of the NA correlated with a high level of enzymatic
activity, comparable to that found to be associated with avian virus NAs. The
specific activities of the A/Ann Arbor/6/60 and A/England/12/62 NAs, which
showed greatly restricted abilities to support viral growth in ducks, were only
8 and 5%, respectively, of the NA specific activity for A/Singapore/1/57. Using
chimeric constructs based on A/Singapore/1/57 and A/England/12/62 NAs, we
localized the determinants of high specific NA activity to a region containing
six amino acid substitutions in A/England/12/62: Ser331-->Arg,
Asp339-->Asn, Asn367-->Ser, Ser370-->Leu, Asn400-->Ser, and
Pro431-->Glu. Five of these six residues (excluding Asn400) were required
and sufficient for the full specific activity of the A/Singapore/1/57 NA. Thus,
in addition to a change in substrate specificity, a reduction in high specific
activity may be required for the adaptation of avian virus NAs to growth in
humans. This change is likely needed to maintain an optimal balance between NA
activity and the lower affinity shown by human virus HAs for their cellular
receptor.
Descriptors: influenza A virus avian enzymology,
intestines virology, neuraminidase metabolism, virus replication, amino acid
substitution, base sequence, DNA
primers, ducks, avian growth and development, avian physiology, models,
molecular, mutagenesis, site directed, neuraminidase chemistry, neuraminidase
genetics, reassortant viruses enzymology, reassortant viruses genetics,
reassortant viruses growth and development, reassortant viruses physiology.
Kobasa, D., M.E. Rodgers, K. Wells, and Y. Kawaoka
(1997). Neuraminidase hemadsorption activity, conserved in avian influenza A
viruses, does not influence viral replication in ducks. Journal of
Virology 71(9): 6706-6713. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: The N1 and N9 neuraminidase (NA) subtypes of
influenza A viruses exhibit significant hemadsorption activity that localizes
to a site distinct from that of the enzymatic active site. To determine the
conservation of hemadsorption activity among different NAs, we have examined
most of the NA subtypes from avian, swine, equine, and human virus isolates.
All subtypes of avian virus NAs examined and one equine virus N8 NA possessed
high levels of hemadsorption activity. A swine virus N1 NA exhibited only weak
hemadsorption activity, while in human virus N1 and N2 NAs, the activity was
detected at a much lower level than in avian virus NAs. NAs which possessed
hemadsorption activity for chicken erythrocytes (RBCs) were similarly able to
adsorb human RBCs. However, none of the hemadsorption-positive NAs could bind
equine, swine, or bovine RBCs, suggesting that RBCs from these species lack
molecules, recognized by the NA hemadsorption site, present on human and
chicken RBCs. Mutagenesis of the putative hemadsorption site of A/duck/Hong
Kong/7/75 N2 NA abolished the high level of hemadsorption activity exhibited by
the wild-type protein but also resulted in a 50% reduction of the NA enzymatic
activity. A transfectant virus, generated by reverse genetics, containing this
mutated NA replicated 10-fold less efficiently in chicken embryo fibroblast
cultures than did a transfectant virus expressing the wild-type NA. However,
both viruses replicated equally well in Peking ducks. Although conservation of
NA hemadsorption activity among avian virus NAs suggests the maintenance of a
required function of NA, loss of the activity does not preclude the replication
of the virus in an avian host.
Descriptors: biochemistry and molecular biophysics, blood
and lymphatics, cell biology, enzymology, genetics, infection, microbiology,
skeletal system, A, duck, Hong Kong, 7, 75, blood and lymphatics enzymology,
erythrocyte fibroblasts, hemadsorption activity, host infection, influenza A
viruses, N1 neuraminidase, N9 neuraminidase, Peking duck, viral replication,
viral surface, glycoprotein.
Kocan, A.A., G.A. Daubney, and K.M. Kocan (1978). Structural
changes associated with type-A influenza in Mallard duck tracheal organ
culture. Avian Diseases 22(3): 535-41. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Mallard duck tracheal organ cultures were
used to study structural changes associated with infection with type-A
influenza (A/Turkey/WIS/68) (H9N2) at the light-microscope and electron-microscope
levels. Light-microscope changes in infected organ culture were cytoplasmic
vacuolization, nuclear swelling, reduction in ciliated epithelium, and
sloughing of epithelial cells. Ultrastructural changes included the loss of
cilia and microvilli, distortion and swelling of cellular organelles, breakdown
of intercellular junction, and apparent phagocytosis of the ciliated
epithelium. Numerous budding virions were noted at the plasmalemma. Virus was
detected by egg inoculation from all experimental cultures throughout the
192-hour experiment.
Descriptors: influenza A virus, avian growth and
development, trachea ultrastructure, organ culture, trachea microbiology.
Kodihalli, S., J.R. Haynes, H.L. Robinson, and R.G.
Webster (1997). Cross-protection among lethal H5N2 influenza viruses induced
by DNA vaccine to the hemagglutinin. Journal of Virology 71(5): 3391-6. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Inoculation of mice with hemagglutinin
(HA)-expressing DNA affords reliable protection against lethal influenza virus
infection, while in chickens the same strategy has yielded variable results.
Here we show that gene gun delivery of DNA encoding an H5 HA protein confers
complete immune protection to chickens challenged with lethal H5 viruses. In
tests of the influence of promoter selection on vaccine efficacy, close
correlations were obtained between immune responses and the dose of DNA
administered, whether a cytomegalovirus (CMV) immediate-early promoter or a
chicken beta-actin promoter was used. Perhaps most important, the HA-DNA
vaccine conferred 95% cross-protection against challenge with lethal antigenic
variants that differed from the primary antigen by 11 to 13% (HA1 amino acid
sequence homology). Overall, the high levels of protection seen with gene gun
delivery of HA-DNA were as good as, if not better than, those achieved with a
conventional whole-virus vaccine, with fewer instances of morbidity and death.
The absence of detectable antibody titers after primary immunization, together
with the rapid appearance of high titers immediately after challenge,
implicates efficient B-cell priming as the principal mechanism of DNA-mediated
immune protection. Our results suggest that the efficacy of HA-DNA influenza
virus vaccine in mice extends to chickens and probably to other avian species
as well. Indeed, the H5 preparation we describe offers an attractive means to
protect the domestic poultry industry in the United States from lethal H5N2
viruses, which continue to circulate in Mexico.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian immunology, influenza vaccine immunology,
vaccines, DNA immunology, antibodies, viral blood, biolistics, chickens, dose
response relationship, immunologic, epitopes, fowl plague prevention and
control, hemagglutinin glycoproteins, influenza virus immunology, promoter
regions genetics, vaccination.
Kodihalli, S., V. Sivanandan, K.V. Nagaraja, D. Shaw,
and D.A. Halvorson (1994). Effect of avian influenza virus infection on the
phagocytic function of systemic phagocytes and pulmonary macrophages of
turkeys. Avian Diseases 38(1): 93-102. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The effects of avian influenza virus (AIV)
infection on systemic phagocytes and pulmonary macrophages of turkeys were
studied. There was a significant increase (P < 0.0001) in oxidative burst in
systemic phagocytes of AIV-inoculated turkeys on 2, 4, 6, and 8 days
postinoculation (PI), as measured by chemiluminescence. There was also a
significant increase (P < 0.02) in oxidative burst in pulmonary macrophages
on day 4 PI. The chemiluminescence response was depressed on 6, 8, and 10 days
PI in AIV-inoculated turkeys compared with controls. The increase in oxidative
response in both systemic phagocytes and pulmonary macrophages correlated with
the peak virus titer in the lungs and trachea of AIV-inoculated turkeys.
Bacterial killing by pulmonary macrophages from AIV-inoculated turkeys was
reduced on days 6 and 10 PI compared with uninoculated controls.
Histopathological changes in trachea were more pronounced on day 6 PI in
AIV-inoculated turkeys; no significant changes were detected in the lungs.
These data indicate that compromised functional capacity of pulmonary
macrophages predisposes turkeys to secondary bacterial infections.
Descriptors: turkeys, avian influenza virus, phagocytes,
macrophages, immune response, histopathology, lungs, trachea, antimicrobial properties,
animal morphology, antibiotic properties, birds, cells, Galliformes, immunity,
influenza virus, pathology, phagocytes, respiratory system, viruses, oxidative
burst, phagocytosis, immune competence, antibacterial properties.
Korbecki, M. (1973). Dzialanie
2-(N-D-glukozyloamino)-5-(3-pirydylo)-1,3,4-oksadiazolu na replikacje wirusa
pomoru drobiu w hodowli komorkowej. [Effect of
2-(N-D-glucosylamino)-5-(3-pyridilo)-1,3,4-oxadiazole on replication of fowl
plague virus in cell culture]. Medycyna Doswiadczalna i Mikrobiologia
25(4): 335-8. ISSN: 0025-8601.
Descriptors: influenza A virus avian drug effects,
oxadiazoles pharmacology, virus replication drug effects, cultured cells, chick
embryo, cytopathogenic effect, viral, fibroblasts.
Kornilaeva, G.V. and A.G. Bukrinskaia (1980). Deproteinizatsiia
virusa grippa zarazhaemymi kletkami pri 4 gradusa C. [Deproteinization of the
influenza virus by infected cells at 4 degrees C]. Voprosy Virusologii
(6): 701-5. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The process of influenza virus
deproteinization was compared in two systems: chick fibroblasts infected with
fowl plague virus (FPV) and MDCK cells infected with WSN virus. The cells were
infected with 3H-uridine-labeled viruses. Deproteinization of virus structures
was studied at 4 degrees C and after incubation of virus-infected cells at 37
degrees C. At 4 degrees C, the bulk of radioactivity of the original virus was
found in the perinuclear cytoplasm (the fraction obtained by treatment of
triton X-100-purified nuclei with 0.1 M citric acid) and much less
radioactivity was found in the nucleus. After incubation at 37 degrees C the
level of radioactivity in the nucleus increased and reached or even exceeded
that in the perinuclear cytoplasm. A biophysical analysis of the structures
showed the perinuclear cytoplasm to contain subviral particles (SVP) similar to
nucleoids as well as RNP with a buoyant density of 1.35 g/ml in cesium
chloride. The nuclear extract contained RNP with a buoyant density 1.39-1.41
m/ml. The experimental results indicate that the first stage of
deproteinization of virus particles to SVP occurs at 4 degrees C. The second
stage of deproteinization, to RNP with a buoyant density 1.35 g/ml, also occurs
at a low temperature.
Descriptors: orthomyxoviridae metabolism, temperature,
viral proteins metabolism, chick embryo, influenza A virus avian metabolism,
ribonucleoproteins metabolism, time factors, tritium, virus cultivation.
Kornilaeva, G.V., E.V. Molibog, and A.G. Bukrinskaia
(1983). pH-zavisimost' gemoliticheskoi i neiraminidaznoi aktivnosti
chuvstvitel'nykh i ustoichivykh k remantadinu variantov virusa grippa.
[pH-dependent hemolytic and neuraminidase activity of remantadine-sensitive and
-resistant variants of influenza virus]. Voprosy Virusologii 28(1):
30-2. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A comparative study of pH-dependence of
hemolytic and neuraminidase activities of four remantadin-sensitive influenza A
virus strains CAPV (classical avian plague virus) (H7N7), USSR/090/77 (H1N1),
Ann Arbor (H2N2), and Texas (H3N2) and their remantadin-resistant variants was
carried out. The original strains were shown to produce hemolysis in a narrow
pH range (5.0 and 5.5) and to have maximal neuraminidase activity at the same
pH values. In remantadin-resistant variants the optimal pH values for hemolytic
and neuraminidase activities were higher by 0.5-1.0 than for the sensitive
variants.
Descriptors: adamantane analogs and derivatives,
hemolysis, influenza A virus enzymology, neuraminidase metabolism, rimantadine
pharmacology, variation genetics drug effects, drug resistance, microbial,
hydrogen-ion concentration, influenza A virus avian drug effects, avian
enzymology, influenza A virus drug effects.
Kornilaeva, G.V., V.A. Slepushkin, and A.G.
Bukrinskaia (1986). Raznaia priroda kletochnykh retseptorov dlia virusov
grippa i paragrippa. [Varying nature of the cell receptors for influenza and
para-influenza viruses]. Voprosy Virusologii 31(1): 35-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A comparative study of receptors for
influenza virus, fowl plague virus, and human parainfluenza type 3 virus was
carried out. Natural receptors of guinea pig erythrocytes were destroyed with
neuraminidase, and individual gangliosides GM1, GD1a, and GT1b were inserted
into their membranes. The labeled virus was adsorbed on the erythrocytes
modified in this manner, and the degree of restoration of the receptor activity
of erythrocytes lost after neuraminidase treatment was determined. Two
gangliosides, GD1a and GT1b, were found to be capable of functioning as
specific receptors for influenza virus. Both gangliosides restored completely
the virus adsorption on erythrocytes. In contrast, none of the three gangliosides
used did not restore parainfluenza virus adsorption. It is concluded that the
nature of influenza and parainfluenza virus receptors is different.
Descriptors: influenza A virus avian metabolism,
orthomyxoviridae metabolism, parainfluenza virus 3, human metabolism,
receptors, virus metabolism, respirovirus metabolism, adsorption, cell line,
erythrocytes drug effects, erythrocytes metabolism, erythrocytes microbiology,
gangliosides metabolism, guinea pigs, neuraminidase pharmacology, receptors,
virus drug effects, virus cultivation.
Kortt, A.A., E. Nice, and L.C. Gruen (1999). Analysis
of the binding of the Fab fragment of monoclonal antibody NC10 to influenza
virus N9 neuraminidase from tern and whale using the BIAcore biosensor: effect
of immobilization level and flow rate on kinetic analysis. Analytical
Biochemistry 273(1): 133-41. ISSN:
0003-2697.
NAL
Call Number: 381 An13
Descriptors: antibodies, monoclonal metabolism, biosensing
techniques methods, immunoglobulin fragments immunology, immunoglobulins, fab
immunology, influenza A virus avian enzymology, neuraminidase immunology,
birds, avian immunology, kinetics, neuraminidase metabolism, protein binding,
whales.
Kosiakov, P.N., V.S. Pankratov, and Z.I. Rovnova
(1979). Antigeny gemaggliutininov virusov grippa, vydelennykh ot cheloveka i
ptits. [Hemagglutinin antigens of influenza viruses isolated from man and
birds]. Voprosy Virusologii (3): 242-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Immunological analysis has shown
hemagglutinins of avian viruses like hemagglutinins of human viruses to have a
complex antigenic composition. Three antigenic determinants were discovered in
hemagglutinin of A/Chicken/12/71 virus previously designated H3 and in
hemagglutinin of A/Tern/18/73 virus previously designated Hav7. The H3
determinant and the second determinant are identical in avian and A/Hong
Kong/1/68 human viruses. In addition, hemagglutinins of avian viruses have a
determinant specific for each virus which is lacking in human influenza virus
hemagglutinin.
Descriptors: antigens, viral isolation and purification,
birds microbiology, hemagglutinins viral isolation and purification, influenza
A virus avian immunology, human immunology, adsorption, chick embryo,
complement fixation tests, epitopes, hemagglutination inhibition tests.
Kraus, A.A. and C. Scholtissek (1974). Purification
and characterization of a ribonuclease inhibitor of chick-embryo cells. European
Journal of Biochemistry FEBS 48(2): 345-50.
ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Descriptors: DNA directed RNA polymerases antagonists and
inhibitors, DNA directed RNA polymerases blood, enzyme inhibitors isolation and
purification, ribonucleases antagonists and inhibitors, centrifugation, density
gradient, chick embryo, chromatography, affinity, cytoplasm enzymology,
cytosol, electrophoresis, polyacrylamide
gel, hydrogen-ion concentration, influenza A virus avian enzymology, kinetics,
molecular weight, orthomyxoviridae enzymology.
Kretzschmar, E., M. Veit, S. Brunschon, K. Kuroda,
and H.D. Klenk (1992). Secretion of fowl plague virus haemagglutinin from
insect cells requires elimination of both hydrophobic domains. Journal
of General Virology 73(Pt. 4): 839-48.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: In the present study we have investigated the
role of the hydrophobic domains of the fowl plague virus (FPV) haemagglutinin
(HA) on its intracellular transport and maturation in insect cells. To this end
processing of full-length HA (A+) has been compared to that of two truncated
forms lacking either the cytoplasmic domain and the transmembrane domain (A-)
or lacking the entire HA2 subunit, i.e. the transmembrane domain and the fusion
peptide (HA2-). All glycosylation sites present on A- and HA2- were
glycosylated, indicating that both truncated forms were completely translocated
in the endoplasmic reticulum. Unlike A+, A- and HA2- did not form trimers as
indicated by cross-linking, gradient centrifugation and studies employing
conformation-specific antibodies. Whereas HA2- was efficiently secreted, A- was
retained in the cells in an apparently membrane-bound form. The data show that
the carboxy-terminal transmembrane region is essential for the formation and
stability of the trimers of the FPV HA. These observations also indicate that,
under certain conditions, the fusion peptide of the FPV HA can serve as a
membrane anchor.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian metabolism, protein processing, post translational, viral envelope
proteins secretion, base sequence, biological transport, active, cell
fractionation, cultured cells, DNA mutational analysis, endopeptidases
metabolism, glycosylation, hemagglutinin glycoproteins, influenza virus, avian
genetics, insects, molecular sequence data, protein conformation, recombinant
proteins biosynthesis, structure activity relationship.
Kuiken, T., G. Rimmelzwaan, D. van Riel, G. van
Amerongen, M. Baars, R. Fouchier, and A. Osterhaus (2004). Avian H5N1
influenza in cats. Science 306(5694): 241. ISSN: 1095-9203.
NAL
Call Number: 470 Sci2
Abstract: During the 2003 to 2004 outbreak of avian
influenza A (H5N1) virus in Asia, there were anecdotal reports of fatal
infection in domestic cats, although this species is considered resistant to
influenza. We experimentally inoculated cats with H5N1 virus intratracheally
and by feeding them virus-infected chickens. The cats excreted virus, developed
severe diffuse alveolar damage, and transmitted virus to sentinel cats. These
results show that domestic cats are at risk of disease or death from H5N1
virus, can be infected by horizontal transmission, and may play a role in the
epidemiology of this virus.
Descriptors: cat diseases virology, influenza veterinary,
influenza A virus, avian pathogenicity, cat diseases pathology, cat diseases
transmission, cats, chickens virology, disease transmission, horizontal
veterinary, feeding behavior, influenza pathology, influenza transmission,
influenza virology, influenza A virus, avian isolation and purification, avian
influenza virology, pulmonary alveoli pathology, pulmonary alveoli virology.
Kul'kova, L.V. and V.Z. Soloukhin (1979). Reproduktsiia
virusa istinnoi chumy ptits v organizme komarov Aedes aegypti.
[Classical fowl plague virus reproduction in the body of Aedes aegypti
mosquitoes]. Voprosy Virusologii (6): 652-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The results of the studies on fowl plague
virus (FPV, Rostok strain) reproduction in Aedes aegypti mosquitoes are
presented. The virus-containing allantoic fluid was inoculated intrathoracally
in volumes of 0.1 and 0.2 microliter. The virus was isolated in chick embryos
and could be detected at 5--14 days after inoculation. After inoculation of 0.1
microliter of virus it could be detected in doses of 0.5, 2.0, 1.75 Ig2 ID50,
after inoculation of 0.2 microliter--in doses of 5, 1.5, and 0.5 Ig2 ID50.
Descriptors: Aedes microbiology, influenza A virus
avian physiology, time factors, virus replication.
Kurinenko, B.M., N.V. Kalacheva, and P.I.U. Muratov
(1995). Poluchenie i protivovirusnye svoistva ribonukleazy Bacillus
intermedius, modifitsirovannoi khlorangidridom adamantankarbonovoi kisloty.
[Preparation and antiviral properties of Bacillus intermedius
ribonuclease modified by chloranhydride of adamantanecarboxylic acid]. Antibiotiki
i Khimioterapiia Antibiotics and Chemoterapy [Sic] Ministerstvo Meditsinskoi i
Mikrobiologicheskoi Promyshlennosti SSSR 40(9): 17-9. ISSN: 0235-2990.
NAL
Call Number: RM265.A5125
Abstract: Bacillus intermedius ribonuclease
modified by the residue of adamantane carboxylic acid was prepared. When the
cells of chick embryo fibroblasts infected by the fowl plague virus were
exposed to the modified ribonuclease, the antiviral activity proved to be
higher by comparison to that of the native enzyme. The chemotherapeutic index
of the RNAse after the modification increased 4 times.
Descriptors: adamantane analogs and derivatives, antiviral
agents isolation and purification, Bacillus enzymology, ribonucleases isolation
and purification, adamantane chemistry, antiviral agents pharmacology, chick
embryo, fibroblasts drug effects, fowl plague drug therapy, influenza A virus
avian drug effects, molecular structure, ribonucleases chemistry,
ribonucleases pharmacology.
Kuroda, K., A. Groner, K. Frese, D. Drenckhahn, C.
Hauser, R. Rott, W. Doerfler, and H.D. Klenk (1989). Synthesis of
biologically active influenza virus hemagglutinin in insect larvae. Journal
of Virology 63(4): 1677-85. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The hemagglutinin of influenza (fowl plague)
virus was expressed in larvae of Heliothis virescens by using
recombinant Autographa californica nuclear polyhedrosis virus (AcNPV) as
a vector. Animals were infected with the recombinant virus either by parenteral
injection or by feeding. For oral uptake, recombinant virus occluded in
polyhedra obtained from cultured Spodoptera frugiperda cells after
coinfection with authentic AcNPV was used. Immunohistological analyses of
infected animals revealed that the hemagglutinin was expressed only in those
tissues that are also permissive for the replication of authentic AcNPV. These
tissues included hypodermis, fat body, and tracheal matrix. After oral infection,
hemagglutinin was also detected in individual gut cells. The amount of
hemagglutinin synthesized in larvae after parenteral infection was 0.3% of the
total protein, compared with 5% obtained in cultured insect cells. The
hemagglutinin was transported to the cell surface and expressed in polarized
cells only at the apical plasma membrane. It was processed by posttranslational
proteolysis into the cleavage products HA1 and HA2. Oligosaccharides were
attached by N-glycosidic linkages and were smaller than those found on
hemagglutinin obtained from vertebrate cells. Hemagglutinin from larvae
expressed receptor binding and cell fusion activities, but quantitation of the
hemolytic capacity revealed that it was only about half as active as
hemagglutinin from vertebrate or insect cell cultures. Chickens immunized with
larval tissues containing hemagglutinin were protected from infection with fowl
plague virus. These observations demonstrate that live insects are able to
produce a recombinant membrane protein of vertebrate origin in biologically
active form.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian immunology, insect viruses genetics, administration, oral,
blotting, western, cloning, molecular, DNA, recombinant, genetic vectors,
hemolysis, avian genetics, larva, Lepidoptera, membrane glycoproteins
genetics, recombinant proteins genetics.
Kuroda, K., M. Veit, and H.D. Klenk (1991). Retarded
processing of influenza virus hemagglutinin in insect cells. Virology
180(1): 159-65. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: When expressed in Spodoptera frugiperda
cells by a baculovirus vector, the hemagglutinin of fowl plague virus has been
found to contain palmitic acid in covalent hydroxylamine-sensitive linkage,
indicating that these cells have the capacity to acylate foreign proteins at
cysteine residues. Centrifugation on sucrose density gradients and immune
precipitation with conformation-specific antibodies were used to compare
trimerization of the hemagglutinin in insect cells and in fowl plague
virus-infected MDCK cells. Trimerization of the hemagglutinin was incomplete in
insect cells, and the kinetics of this reaction were about three times slower
than in vertebrate cells. Similarly, post-translational proteolytic cleavage
occurred in insect cells with a half-time of 90 min, and a substantial fraction
of the hemagglutinin persisted in uncleaved form. In contrast, hemagglutinin
was almost completely cleaved in MDCK cells, and the half-time of cleavage was
only 30 min. The data indicate that in insect cells trimerization and, as a
result, the subsequent processing steps of the hemagglutinin, are retarded and
less efficient. The possible roles of aberrant glycosylation, acidic milieu,
and lack of other influenza virus proteins in hemagglutinin trimerization are
discussed.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian metabolism, acylation, antibodies, monoclonal, biological
transport, cell line, centrifugation, density gradient, electrophoresis,
polyacrylamide gel, eukaryotic cells, fatty acids metabolism, avian growth and
development, kinetics, moths cytology, polymers, precipitin tests, protein
processing, post translational.
L'vov, D.K., R.I.A. Podcherniaeva, R. Webster, M.V.
Ronina, and T.V. Pysina (1979). Poluchenie rekombinantov, antigenno
identichynykh tsirkuliruiushchim v prirode shtammam virusa grippa. [Production
of recombinants antigenically identical to influenza virus strains circulating
in nature]. Voprosy Virusologii (5): 493-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Recombination of a human influenza virus with
an avian influenza virus produced a H2Nav2 recombinant with the antigenic
properties analogous to those of avian influenza virus (H2Nav2) isolated from
wild ducks in the Far East, USSR. Recombination of two avian influenza viruses
yielded a recombinant H2N2, an antigenic analogues of influenza
A/Singapore/1/57 (H2N2) virus which had started an epidemic of influenza in
1957.
Descriptors: antigens, viral genetics, influenza A virus
genetics, recombination, genetic, animals, wild, crosses, genetic, ducks
microbiology, hemagglutination inhibition tests, influenza A virus human
genetics, neuraminidase antagonists and inhibitors.
Lambkin, R. and N.J. Dimmock (1995). All rabbits
immunized with type A influenza virions have a serum haemagglutination-inhibition
antibody response biased to a single epitope in antigenic site B. Journal
of General Virology 76(Pt. 4): 889-97.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Nine rabbits were immunized with type A
influenza virions and the epitope specificities of the secondary serum
haemagglutination-inhibition (HI) antibody response were analysed with a panel
of neutralizing monoclonal (MAb) antibody double escape mutants. Each of the
latter was made by sequential selection using a MAb directed to an epitope of a
discrete antigenic site, site A, site B or site D, of the haemagglutinin (HA).
Thus the epitope reactivity of the escape mutants was represented as A+ B- D-,
A- B+ D- and A- B- D+. The HI antibody response of all antisera was biased to
the site B epitope. In 9/12 antisera, obtained from seven rabbits immunized
with whole virions, the site B epitope was predominant, representing 65-82% of
the total HI antibody. The restriction of HI antibody was unaffected by strain
of rabbit, route of inoculation (intravenous or subcutaneous), use of Freund's
adjuvant, and up to four immunizing injections. In 3/7 rabbits immunized with
whole virus, there was a HI antibody response to the HC2 (site A) or HC10 (site
D) epitope, but not both, of equal magnitude to the site B epitope. The HI
antibody response in one of the rabbits (#40) became more biased to the site B
epitope between the third and fourth immunizing doses. Two further rabbits were
immunized with virions which had been partially digested with bromelain and
then purified from free HA. Both of these made equal HI antibody responses to
the site B epitope and the site D epitope, possibly because their remaining HA
spikes were better exposed. Overall, these data demonstrate an unexpected
degree of restriction in the production of biologically relevant antibody, such
that some rabbits (e.g. #45) mount an HI antibody response which is essentially
epitope-specific. Implications for epitope specificity of HI antibody
stimulated by human influenza vaccines, and also for the generation of
antigenic drift variants are discussed. The reason for the non-responsiveness
of the immune system to the many other HI epitopes of the HA is not known.
Descriptors: antibodies, viral immunology, antibody
specificity immunology, antigens, viral immunology, epitopes immunology,
influenza A virus avian immunology, antibodies, viral blood, binding sites,
cell line, chick embryo, dogs, hemagglutination inhibition tests, immunization,
neutralization tests, rabbits, virion immunology.
Lambkin, R., L. McLain, S.E. Jones, S.L. Aldridge,
and N.J. Dimmock (1994). Neutralization escape mutants of type A influenza
virus are readily selected by antisera from mice immunized with whole virus: a
possible mechanism for antigenic drift. Journal of General Virology
75(Pt. 12): 3493-502. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: It is not fully understood how antigenic
drift of the haemagglutinin of type A influenza virus in man occurs in the
presence of the expected polyclonal antibody response to the five antigenic
sites, A to E. Here we show that 12% (11/92) of sera from mice which had
mounted a secondary immune response to inactivated influenza virus were able to
select escape mutants. No escape mutant was selected with serum from
nonimmunized mice (0/65). Selection required only a single passage, and escape
mutants were identified by their reaction with monoclonal antibodies (MAbs);
all but one had altered reactivity at site A. Most of the site A escape mutants
(7/10) were conventional in character and did not react in
haemagglutination-inhibition (HI) or neutralization assays with the identifying
MAb. The HA genes of three of these were part sequenced and had a predicted
single amino acid substitution (Gly-144-->Glu) in site A. The other escape
mutants (3/10) had a small (2-fold) reduction in HI and neutralization to the
site A MAb, but no amino acid substitution in site A. The final mutant was a
conventional site B escape mutant. To model antisera which selected escape
mutants, we constructed 'pseudo-immune sera' using mixtures of two neutralizing
MAbs in which the first MAb was held at a constant high concentration (1000
HIU/ml). Escape mutants could be selected to the first MAb when the titre of
the second MAb was reduced to a low but still inhibiting concentration (1 to 3
HIU/ml). Mixtures of three MAbs also selected escape mutants with similar
facility provided that the second and third MAbs were reduced to a similar low
concentration. Thus it is possible that the ability of an antiserum to select
escape mutants is due to the neutralizing antibody response being biased to an
epitope/cross-reacting epitopes within a single antigenic site. However, when
escape mutants were reacted in HI assay with their selecting antiserum, the maximum
difference from the titre with wt virus was 75%. The findings of this study may
be relevant to the understanding of antigenic drift in type A human influenza
virus, and to immune-driven antigenic variation in other virus infections.
Descriptors: antibodies, monoclonal immunology, antigenic
variation genetics, hemagglutinins viral genetics, immune sera, influenza A
virus avian immunology, point mutation, antibodies, viral blood, DNA mutational
analysis, epitopes analysis, gene frequency genetics, genes, structural, viral genetics,
hemagglutination inhibition tests, hemagglutinin glycoproteins, influenza
virus, hemagglutinins viral immunology, immunization, avian genetics, mice,
mice inbred BALB c, mice, inbred c3h, neutralization tests, selection genetics,
viral envelope proteins genetics, viral envelope proteins immunology.
Lau, S.C. and C. Scholtissek (1995). Abortive
infection of Vero cells by an influenza A virus (FPV). Virology
212(1): 225-31. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: We have discovered a new type of abortive
replication in Vero cells infected with fowl plague virus. In these cells there
is an enhanced splicing of the colinear mRNAs of segment 7 and presumably also
of segment 8, leading to an extreme overproduction of M2 and NS2 proteins. The
cleavage of the hemagglutinin (HA) into HA1 and HA2 and the processing of its
carbohydrate side chains are markedly retarded and incomplete. Although some of
the HA is incorporated into the plasma membrane, leading to a positive
hemadsorption, most of it accumulates in a discrete compartment close to the
nuclear membrane, representing presumably the reticuloendothel and/or the Golgi
network. Neuraminidase activity in Vero cells is extremely low. The
nucleoprotein is normally released from nuclei late in infection. Very little
infectious virus is released, and its spread is highly impeded.
Descriptors: gene expression regulation, viral, influenza
A virus avian growth and development, vero cells microbiology, cultured cells, Cercopithecus
aethiops, chick embryo, RNA, messenger metabolism, viral metabolism, time
factors, viral proteins metabolism, virus replication.
Laudert, E., D. Halvorson, V. Sivanandan, and D. Shaw
(1993). Comparative evaluation of tissue trophism characteristics in turkeys
and mallard ducks after intravenous inoculation of type A influenza viruses.
Avian Diseases 37(3): 773-80.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Ten avian type A influenza viruses consisting
of seven waterfowl-origin, one pheasant-origin, and two turkey-origin viruses
were evaluated for their pathogenicity potential after intravenous inoculation
into domestic turkeys and mallard ducks (Anas platyrhynchos). The
replicative abilities and tissue trophism properties of each virus isolate were
examined in both species. The overall virus-isolation rate and
histopathological lesion score were greater in the turkeys than in the ducks.
The waterfowl-origin viruses caused more tissue damage in turkeys than in ducks
but had a narrower tissue distribution range. The pheasant isolate was
extremely pathogenic in turkeys but had limited distribution and little effect
in ducks. The turkey isolates were more pathogenic in turkeys than in ducks.
The pancreas was the most severely affected organ in turkeys, followed by
kidney and liver. The spleen and bursa were the most commonly affected organs
in ducks.
Descriptors: ducks microbiology, fowl plague microbiology,
influenza A virus avian pathogenicity, turkeys microbiology, fowl plague pathology,
avian isolation and purification, avian physiology, injections, intravenous,
kidney microbiology, kidney pathology, organ specificity, pancreas
microbiology, pancreas pathology, species specificity, spleen microbiology,
spleen pathology, virus replication.
Laudert, E., V. Sivanandan, and D. Halvorson (1993). Effect
of an H5N1 avian influenza virus infection on the immune system of mallard
ducks. Avian Diseases 37(3): 845-53.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Avian influenza virus (AIV) of waterfowl
origin, A/Mallard/Ohio/184/86 (H5N1), was used to evaluate the effect of AIV
infection on the functional capabilities of the immune system in mallard ducks.
The three main arms of the immune system--humoral, cell-mediated, and cellular--were
evaluated. The integrity of the humoral immune system after AIV infection was
evaluated by measuring total immunoglobulin and IgG antibody production to
sheep erythrocytes and Brucella abortus antigen using hemagglutination
and microagglutination assays, respectively. Cell-mediated immunity was
evaluated using mitogen/antigen stimulation assays, and by measuring the
cutaneous basophilic hypersensitivity response to intradermal
phytohemagglutinin-P inoculation. The cellular component of the immune response
was evaluated using whole-blood chemiluminescence and bacterial clearance
assays. Results showed that infection with this AIV isolate suppressed T-cell
function and enhanced macrophage phagocytic activity.
Descriptors: bird diseases immunology, ducks, fowl plague
immunology, basophils immunology, Escherichia coli infections
complications, Escherichia coli infections immunology, Escherichia
coli infections veterinary, fowl plague complications, fowl plague
etiology, hypersensitivity, delayed, immunoglobulin g metabolism, immunoglobulins metabolism, influenza A virus
avian immunology, avian isolation and purification, avian pathogenicity,
lymphocyte activation, macrophages immunology, phagocytosis, T lymphocytes
immunology.
Laudert, E., V. Sivanandan, D. Halvorson, D. Shaw,
and R.G. Webster (1993). Biological and molecular characterization of H13N2
influenza type A viruses isolated from turkeys and surface water. Avian
Diseases 37(3): 793-9. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The pathogenicity potential of two H13N2
influenza viruses, one isolated from turkeys and the other isolated from
surface water, was evaluated in turkeys, chickens, and mallard ducks (Anas
platyrhynchos ) after intracranial and oculonasal inoculation. Both
isolates replicated in turkey poults, causing depressed weight gain, morbidity
and mortality; both also caused histopathological lesions, such as mild to
severe pancreatitis, hepatitis, and nephritis in turkeys. These isolates
replicated in mallard ducklings but not in chickens. There was depressed weight
gain in ducklings given the H13N2 isolate from water. Neither isolate caused
morbidity or mortality in ducklings or chicks after inoculation.
Descriptors: influenza A virus avian isolation and
purification, turkeys microbiology, water microbiology, antibodies, monoclonal,
chickens, cross reactions, ducks, fowl plague etiology, fowl plague pathology,
avian immunology, avian pathogenicity, species specificity, virulence.
Laver, W.G., P.M. Colman, R.G. Webster, V.S. Hinshaw,
and G.M. Air (1984). Influenza virus neuraminidase with hemagglutinin
activity. Virology 137(2): 314-23.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Isolated intact influenza virus neuraminidase
(NA) molecules of the N9 subtype have been found to possess hemagglutinin (HA)
activity which, at equivalent protein concentration, was fourfold higher than
that of isolated hemagglutinin molecules of the H3 subtype. The amino-terminal
sequence of the N9 NA is the same as in neuraminidases of the eight other
influenza A virus NA subtypes previously reported. Viruses possessing N9 NA
therefore have two different HA activities and antibody to either HA or NA
alone was incapable of inhibiting hemagglutination by the virus. However,
antibody to the HA of an H1N9 virus neutralized its infectivity as effectively
as it neutralized H1N1 or H1N2 viruses whose neuraminidases have no HA
activity. (Antibodies to N9 NA did not neutralize the infectivity of viruses
with N9 neuraminidase). 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid inhibited
N9 NA activity but had no effect on the HA activity of the isolated N9 NA. One
interpretation of this result would be that the HA and NA activities are
located in separate sites. Pronase-released N9 NA heads form crystals suitable
for X-ray diffraction studies and preliminary data to 2.9 A establish the space
group as cubic, I432 with cell dimension a = 184 A. Data extend to beyond 1.9 A
resolution, and these will be collected in the future.
Descriptors: hemagglutinins viral, influenza A virus avian
enzymology, neuraminidase isolation and purification, antibodies, monoclonal,
antigen antibody complex, birds, hemagglutination tests, neuraminidase
immunology, x-ray diffraction.
Laver, W.G. and R.G. Webster (1977). Hemagglutinin
molecules of Hong Kong, equine-2, and duck/Ukraine influenza viruses lack
N-terminal aspartic acid. Virology 81(2): 482-5. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: hemagglutinins viral analysis, influenza A
virus avian immunology, human immunology, influenza A virus immunology, RNA
viruses immunology, aspartic acid analysis, horses, recombination, genetic.
Lavrov, S.V., E.I. Eremkina, T.G. Orlova, G.A.
Galegov, V.D. Soloviev, and V.M. Zhdanov (1968). Combined inhibition of
influenza virus reproduction in cell culture using interferon and amantadine.
Nature 217(131): 856-7. ISSN:
0028-0836.
NAL
Call Number: 472 N21
Descriptors: amantadine pharmacology, interferons
pharmacology, orthomyxoviridae drug effects, chick embryo, cytopathogenic
effect, viral, ethionine pharmacology, fluorouracil pharmacology,
hemagglutination tests, influenza A virus avian drug effects, tissue culture,
virus cultivation, virus inhibitors.
Lavrov, S.V., N.L. Pushkarsakia, and G.A. Galegov
(1968). Ingibiruiushchee deistvie 1-adamantanamina na virus klassicheskoi
chumy kur. [Inhibiting effect of 1-adamantamine on the classical fowl plague
virus]. Voprosy Virusologii 13(3): 352-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, chickens, cytopathogenic effect, viral.
Lazymova, Z.A., T.A. Asadullaev, E.S.h. Mamedov, and
R.I.a. Akhverdieva (1988). Bis-(N,N'-uratsil-1-il)-selenoksometan: ingibitor
virusa grippa. Voprosy Virusologii 33(2): 163-5. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Experimental studies of the influence of
bis-(N,N'-uracil-1-yl)-selenoxomethane (I) and sodium selenite (II) on
influenza virus reproduction on pieces of chorioallantoic membrane, both alone
and in combination with remantadine and ribavirin, were carried out. The
antiviral effects of both preparations were found to be enhanced in combination
with effective and ineffective remantadine concentrations, whereas with
ribavirin the additive effect was observed only in combination of the former
preparation with ribavirin effective concentration. Combination of ribavirin
with sodium selenite did not enhance the antiviral effect of the latter even
when the effective concentration of nucleoside was used.
Descriptors: antimetabolites pharmacology, antiviral
agents pharmacology, influenza A virus avian drug effects, organometallic
compounds pharmacology, organoselenium compounds, uracil analogs and
derivatives, chick embryo, drug synergism, fluorouracil pharmacology, avian
physiology, ribavirin pharmacology, rimantadine pharmacology, selenious acid,
selenium pharmacology, uracil pharmacology, virus replication drug effects.
Lecomte, J. and J.S. Oxford (1981). Detection of
antigenic variation of influenza A matrix protein by a competitive
radioimmunoassay. Journal of General Virology 57(Pt. 2): 403-6. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Antigenic relationships among the matrix
proteins of influenza A viruses were analysed using a competitive
radioimmunoassay technique. There were at least two antigenic determinants on
the M protein of A/PR/8/34 virus. One antigenic determinant was shared by
several influenza A viruses of human, avian, swine or equine origin, while the
second determinant was not necessarily shared by all influenza viruses since it
was not detected on the M protein of A/chicken/Germany/N/49 virus. In addition,
the cross-reactive determinant(s) of the M protein of N virus was not equally
represented in other influenza A virus subtypes.
Descriptors: influenza A virus human immunology, influenza
A virus immunology, viral proteins immunology, cross reactions, epitopes, avian
immunology, porcine immunology, radioimmunoassay, viral matrix proteins.
Ledovskikh, N.B., L.V. Iurchenko, G.A. Nevinskii,
E.I. Frolova, E.M. Ivanova, A.A. Koshkin, N.A. Bulichev, V.F. Zarytova, and
V.V. Vlasova ( 1992). Podavlenie transkriptsii RNK virusa grippa
proizvodnymi oligonukleotidov. [Suppression of transcription of influenza virus
RNA by oligonucleotide derivatives]. Molekuliarnaia Biologiia 26(3):
635-44. ISSN: 0026-8984.
NAL
Call Number: QH506.A1M62
Abstract: The inhibitory effects of oligonucleotide
derivatives on the transcription of virus RNA in an in vitro system and
synthesis of virus proteins was studied. Oligonucleotide derivatives d(T)3,
d(T)4, d(T)8, d(T)10, d(CCAAACA), d(TCACCCTC), d(TTCCCATT), d(AATACTCT) and
d(TGACCCTCTTCCCATT), that bear residues of ethidium, deuteroporphyrin and its
complexes with Fe3+, hemin, cholesterol, deuterocholesterol, estrone and
naphthoquinone at the 5'-end phosphate and/or at the 3'-end phosphate were
studied. Unmodified oligonucleotides and their derivatives had a negligible
effect on the synthesis of cellular proteins, but did inhibit the synthesis of
influenza virus proteins. The majority of structural modifications increased
the inhibitory effect of oligonucleotides. It was shown that the oligonucleotide
derivatives carrying residues of porphyrin, quinone, ethidium, cholesterol,
deuterotestosterone and estrone at concentrations near 10 mM inhibit virus
development to 50-80%. A clear inhibitory effect (20-25%) of deuteroporphyrin,
cholesterol and ethidium derivatives was revealed even at concentration 0.1 mM.
The obtained results testified that the inhibition of influenza virus
development is dependent on the interaction of oligonucleotide derivatives with
the transcription complex proteins.
Descriptors: influenza A virus avian genetics,
oligonucleotides pharmacology, RNA viral genetics, transcription, genetic drug
effects, autoradiography, base sequence, cultured cells, chick embryo, genes
viral, molecular sequence data, oligonucleotides chemistry, viral drug effects,
viral proteins metabolism.
Lee, C.W., C.S. Song, Y.J. Lee, I.P. Mo, M. Garcia,
D.L. Suarez, and S.J. Kim (2000). Sequence analysis of the hemagglutinin
gene of H9N2 Korean avian influenza viruses and assessment of the pathogenic
potential of isolate MS96. Avian Diseases 44(3): 527-35. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Sequence analysis of the hemagglutinin (HA)
gene of five Korean H9N2 avian influenza virus (AIV) isolates showed that these
viruses were closely related and possibly came from the same source.
Phylogenetic analysis of the HA1 subunit of H9 subtype isolates revealed that
Korean AIV isolates were different from isolates from the poultry markets in
Hong Kong in 1997. None of the Korean AIVs had multiple basic amino acids at
the HA cleavage site that confer high pathogenicity to some H5 and H7 AIVs.
Phylogenetic analysis of the nucleoprotein and matrix gene demonstrated that
Korean isolates cluster with Eurasian origin AIVs. The pathogenic potential of
one of the isolates (MS96) was assessed after several passages in 14-day-old
embryonated chicken eggs (ECE). Fourteen-day-old ECE derivatives of MS96 showed
increased HA titer and embryo mortality in eggs; this was apparent after the
third passage in 14-day-old ECE. Sequence analysis of the cleavage site of MS96
after the third and tenth passages in 14-day-old ECE revealed no changes in the
amino acid sequence. The pathogenicity of MS96 after the tenth passage in
14-day-old eggs (MS96p10(ECE14)) was tested with 4-wk-old
specific-pathogen-free chickens. The 14-day-old derivative, MS96p10(ECE14),
showed wider tissue tropism and induced more severe clinical signs than the
parent virus. Furthermore, after intranasal inoculation of 86-wk-old broiler
breeders and 30-wk-old layers, the MS96p10(ECE14) derivative induced more
severe signs of depression than the parent virus as well as a transient drop in
egg production.
Descriptors: chick embryo virology, fowl plague
physiopathology, hemagglutinin glycoproteins, influenza virus genetics,
influenza A virus avian genetics, avian pathogenicity, amino acid sequence,
Asia, chickens, disease progression, genes, structural, viral, avian
classification, Korea, molecular sequence data, phylogeny, reverse
transcriptase polymerase chain reaction, sequence alignment, specific pathogen
free organisms, virulence genetics.
Lee, C.W. and D.L. Suarez (2004). Application of
real-time RT-PCR for the quantitation and competitive replication study of H5
and H7 subtype avian influenza virus. Journal of Virological Methods
119(2): 151-8. ISSN: 0166-0934.
NAL
Call Number: QR355.J6
Abstract: Avian influenza (AI) viruses are endemic in
wild birds and if transmitted to poultry can cause serious economic losses. In
the study of AI, the quantitation of virus shed from infected birds is valuable
in pathogenesis studies and to determine the effectiveness of vaccines, and is performed
routinely by cultivation of virus containing samples using embryonating chicken
eggs (ECE) and expressed by 50% egg infectious dose (EID(50)). Although, this
assay is accurate and is the standard test for infectious virus titration, the
method is laborious, requires a large number of ECE, and takes at least 7 days
to determine results. In this study, a one-tube hydrolysis fluorescent probe
based real-time RT-PCR (RRT-PCR) was applied for the quantitation of AI virus
and compared with conventional virus titration method. A strong positive
correlation was observed between the amount of RNA determined by quantitative
RRT-PCR and the EID(50)s determined by conventional methods. This RRT-PCR test
was further applied in the study of competitive replication of co-infected H5
and H7 subtype viruses in chickens. Using hemagglutinin subtype specific
probes, we were able to determine the amount of individual subtype virus, which
could not have easily been done with conventional methods. This RRT-PCR based
quantitation of AI virus, which is specific, sensitive, easy to perform, and
rapid, will be useful for virological, pathogenesis, and protection studies.
Descriptors: influenza A virus, avian physiology, avian
classification, avian genetics, avian isolation and purification, poultry,
sensitivity and specificity, poultry diseases virology, reverse transcriptase
polymerase chain reaction methods, virus replication, fluorescent dyes,
hemagglutinin glycoproteins, influenza virus analysis.
Leneva, I.A., S.I.A. Mel'nikov, A.V. Mikheeva, and
I.U.Z. Gendon (1985). Vzaimodeistvie belka M virusa chumy ptits dikogo tipa
i ts-mutanta s ribonukleoproteidom virusa chumy ptits in vitro. [Interaction of
the M protein of the wild-type fowl pest virus and its ts-mutant with the ribonucleoprotein
of the fowl pest virus in vitro]. Voprosy Virusologii 30(6):
711-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The extent of inhibition of transcription
realized in vitro by fowl plague virus (FPV) ribonucleoprotein (RNP) upon the
addition of M protein isolated from FPV virions does not depend on nonionic
detergent concentration in the reaction medium but does depend greatly on NaCl
concentration. The highest inhibition of transcription is observed at a low
ionic strength (0.02 M NaCl); inhibition is completely eliminated by increasing
NaCl concentration to 0.3 M. When M protein isolated from FPV virions with ts mutation
of M protein is added to RNP, addition to the system of 0.3 M NaCl decreases
transcription inhibition but does not eliminate it completely.
Descriptors: influenza A virus avian metabolism, mutation,
ribonucleoproteins metabolism, viral proteins metabolism, DNA directed RNA
polymerases metabolism, detergents pharmacology, dose response relationship, drug, drug
interactions, avian drug effects, polyethylene glycols pharmacology,
ribonucleoproteins antagonists and inhibitors, sodium chloride pharmacology,
transcription, genetic drug effects, viral matrix proteins.
Leneva, I.A., A.V. Mikhejeva, V.P. Kuznetsov, W.
Seidel, and Y.U.Z. Ghendon (1985). Studies of proteins soluble in acidic
chloroform-methanol isolated from crude human leukocyte interferon preparations.
Acta Virologica 29(6): 475-81.
ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Acidic chloroform-methanol soluble proteins
possessing hydrophobic properties and capable of inhibiting in vitro
transcriptase activity of influenza virus RNP were detected in native and
partially purified human leukocyte interferon (IFN) preparations. Purification
of IFN resulted in the removal of at least a portion of such proteins; however,
no proteins have been found in highly-purified IFN preparations.
Descriptors: interferon type I analysis, proteins
isolation and purification, chloroform, cytopathogenic effect, viral, DNA
directed RNA polymerases antagonists and inhibitors, hydrogen-ion
concentration, influenza A virus avian enzymology, interferon type I isolation
and purification, methanol, proteins analysis, proteins pharmacology,
ribonucleoproteins metabolism, solubility.
Lesnik, F. and O.J. Vrtiak (1973). Comparative
study of fowl plague virus infected and non-infected allantoic fluid of chick
embryos. Acta Veterinaria Academiae Scientiarum Hungaricae 23(2):
137-44. ISSN: 0001-7205.
Descriptors: body fluids analysis, influenza A virus avian
metabolism, viral proteins biosynthesis, body fluids metabolism, chick embryo,
viral proteins analysis.
Li, S., M.L. Perdue, and E. Patzer (2002). Seed
viruses containing novel avian HA and NA antigens for prevention against
potential influenza pandemic. Developments in Biologicals 110:
135-41. ISSN: 1424-6074.
NAL
Call Number: QR180.3.D4
Abstract: An influenza pandemic could arise
unexpectedly with rapid spread across the world. The efficiency of production
of a vaccine and the ability to administer it widely will be among the most
important factors in the ability to protect public health. The current process
for producing inactivated or live attenuated influenza vaccines requires six to
nine months. That reduces considerably the likelihood that the vaccine will be
available during the first wave of the pandemic. Therefore, a key element of
preparedness is to optimize the production process and to reduce the vaccine
development time. During the 1997 H5N1 outbreak in Hong Kong, seed viruses were
prepared for production of inactivated and live-attenuated vaccines. We used
the cold-adapted A/Ann Arbor/6/60 as the donor virus to generate live
attenuated vaccines containing genetically modified HA and NA genes from H5N1
influenza viruses. These reassortants were shown to be safe and protective in
animal models. This study indicates that production of live attenuated avian
influenza vaccines is feasible and that development of a library of
reassortants containing different subtype HA and NA genes may reduce the
vaccine preparation time for future influenza pandemics.
Descriptors: antigens, viral immunology, influenza
prevention and control, influenza A virus avian immunology, influenza
epidemiology, influenza vaccine administration and dosage.
Liao Ming, Luo KaiJian, Chen JuYi, Yao Xuan, Su
XiangWen, LiLin , and Xin ChaoAn (2004).
Dynamic changes on shedding virus of experimental infection of chickens with
avian influenza virus H5N1 subtype. Chinese Journal of Zoonoses
20(9): 751-753. ISSN: 1002-2694.
Descriptors: tissue distribution, brain, kidneys, liver,
muscles, pancreas, spleen, avian influenza virus, fowl plague virus,
experimental infection, virus shedding, chickens.
Lin, A.H. and P.M. Cannon (2002). Use of
pseudotyped retroviral vectors to analyze the receptor-binding pocket of
hemagglutinin from a pathogenic avian influenza A virus (H7 subtype). Virus
Research 83(1-2): 43-56. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: The hemagglutinin (HA) protein of influenza
virus binds to terminal sialic acid residues present on cell surface
glycoproteins and glycolipids. The specific amino acids involved in this
interaction have been identified for a H3 subtype HA from the human
non-pathogenic virus, A/Aichi/2/68, by both crystallographic and mutagenesis
studies. We were interested to examine the receptor-binding pocket of a H7
subtype protein from the avian pathogenic virus A/FPV/Rostock/34. Accordingly,
we made amino acid substitutions at six conserved residues (Y88, T126, H174,
E181, L185, and G219), suggested by comparison with the receptor-binding pocket
of the H3 protein, and analyzed the resulting proteins using pseudotyped
retroviral vectors. The use of these vectors enabled us to quantitate both the
ability of the mutant HA proteins to bind with receptor-expressing cells, and
also to promote virus-cell fusion by measuring vector titer. Using this system,
we identified a subset of mutants with impaired receptor-binding activity and a
corresponding decrease in titer, but which retained the ability to induce
syncytia in low pH cell-cell fusion assays. The most severely affected mutants
contained more than one substitution, with the triple mutant Y88F/E181Q/G219K
being the most defective. These observations highlight the importance of
multiple contact points for the interaction between sialic acid and HA.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian genetics, receptors, virus metabolism, 3T3
cells, amino acid sequence, amino acid substitution, binding sites, cell line,
transformed, cell membrane metabolism, gene expression, genetic vectors, giant
cells, hemagglutinin glycoproteins, influenza virus chemistry, hydrogen-ion
concentration, avian metabolism, avian pathogenicity, avian physiology,
membrane fusion, mice, molecular sequence data, mutagenesis, protein structure,
tertiary, receptors, virus chemistry, retroviridae, sequence homology, amino
acid, sialic acids chemistry, sialic acids metabolism, temperature.
Linitskaia, G.L., A.A. Iatsyna, N.L. Pushkarskaia,
and G.A. Galegov (1978). Vliianie ribovirina
(1-beta-D-ribofuranozil-1,2,4-triazol-3-karboksimida) na induktsiuu
RNK-zavisimoi RNK-polimerazy i obrazovanie virusspetsificheskikh polisom v
kul'ture kletok, infitsirovannykh virusom grippa A. [Effect of ribovirine
(1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboximide) on RNA-dependent
RNA-polymerase induction and virus-specific polysome formation in cell cultures
infected with influenza A virus]. Voprosy Meditsinskoi Khimii 24(5):
699-702. ISSN: 0042-8809.
Descriptors: antiviral agents pharmacology, influenza A
virus avian drug effects, polyribosomes drug effects, RNA
nucleotidyltransferases metabolism, RNA replicase metabolism, ribavirin
pharmacology, ribonucleosides pharmacology, virus replication drug effects,
cultured cells, chick embryo, depression, chemical, enzyme induction drug
effects, RNA viral biosynthesis, viral proteins biosynthesis.
Liozner, A.L., G.K. Vorkunova, N.A. Volynskaia, and
A.G. Bukrinskaia (1983). Antigennye kharakteristiki belka M virusa grippa.
Vyiavlenie metodom ELISA razlichii belkov M chuvstvitel'nogo i ustoichivogo k
remantadinu variantov virusa. [Antigenic characteristics of influenza virus
protein M. The ELISA detection of the differences in the M proteins of
remantadine-sensitive and -resistant variants of the virus]. Voprosy
Virusologii (3): 281-6. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Antigenic characteristics of influenza A
virus M protein were studied by ELISA using a monospecific antiserum to M
protein and monoclonal antibodies to the B4 and A7 antigenic determinants of M
protein. The design of the test systems for M protein detection was based on
the indirect and "sandwich" variants of ELISA as well as on the
previously developed principle of blocking the indirect reaction. The latter
variant of the test system had the highest specificity: 0.1--0.5 ng of specific
protein. The high specificity of the method allows subtle antigenic differences
of M protein within influenza A virus group to be detected. Comparative studies
of remantadine-sensitive and resistant variants of the classic fowl plague
virus showed the previously demonstrated significant differences in the
physico-chemical properties of M protein of these variants to correlate with a
marked antigenic divergence associated, in particular, with greater
antigenicity of B4 epitope in M protein of remantadine-sensitive strains. The
test system of ELISA blocking was found to be useful for M protein detection in
virus-containing materials not subjected to purification and concentration
(native allantoic fluids). The latter attests to the expedience of using ELISA
in clinical diagnostic studies of influenza.
Descriptors: adamantane analogs and derivatives, antigens,
viral analysis, glycoproteins analysis, influenza A virus analysis, rimantadine
pharmacology, viral proteins analysis, enzyme linked immunosorbent assay,
glycoproteins immunology, influenza A virus avian analysis, avian drug effects,
avian immunology, influenza A virus drug effects, influenza A virus immunology,
viral proteins immunology.
Lipatov, A.S., A.K. Gitel'man, E.A. Govorkova, and
I.U.A. Smirnov (1995). Izmeneniia biologicheskikh i fiziko-khimicheskikh
svoistv gemaggliutinina H2 ptich'ego virusa grippa A v protsesse adaptatsii k
novomu khozainu. [Changes in biological and physico-chemical properties of
avian influenza virus A hemagglutinin H2 during adaptation to a new host]. Voprosy
Virusologii 40(5): 208-11. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Avian influenza A virus with H2 hemagglutinin
has been adapted to mice for the first time. Alterations in the hemagglutinin
of adapted variants of the virus as a result of adaptation to a new host are
described. Hemagglutinin of a highly virulent adapted variant differed from the
parental avirulent strain by antigenic structure, electrophoretic mobility, and
receptor activity during interactions with murine red cells.
Descriptors: adaptation, physiological, hemagglutinins
viral metabolism, influenza A virus avian physiology, cultured cells, chick
embryo, dogs, erythrocytes virology, hemagglutinin glycoproteins, influenza
virus, hemagglutinins viral chemistry, avian metabolism, avian pathogenicity,
lethal dose 50, mice.
Lipatov, A.S., A.K. Gitelman, and Y.U.A. Smirnov
(1997). Prevention and treatment of lethal influenza A virus
bronchopneumonia in mice by monoclonal antibody against haemagglutinin stem
region. Acta Virologica 41(6): 337-40. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The protective properties of monoclonal
antibody (MoAb) C179 directed to the stem region of haemagglutinin (HA) H2 that
possessed fusion-inhibition and unique broad cross-neutralizing activities were
examined in a mouse model. The MoAb efficiently protected mice against a lethal
challenge with pneumovirulent human (H1) and avian (H2) strains of influenza A
virus. Survival rates in mice that received intraperitonealy (i.p.) 1000
micrograms of the MoAb per mouse a day before the virus challenge were 90% for
H1 and 100% for H2 strain. The dose of the MoAb of 100 micrograms per mouse
significantly decreased mortality in mice. Moreover, the MoAb was also
efficient in treatment of lethal bronhopneumonia caused by H2 influenza virus.
The survival rate in mice that received 1000 micrograms of the MoAb per mouse 2
days after the virus challenge was 90%, while that in the control group was 30%
only. These results indicate that the MoAb was effective in protection of
animals against lethal influenza A infection without significant difference
between H1 and H2 subtypes. The MoAb exerted significant effect in treatment of
mice infected with H2 influenza virus. Thus, these data allow to suggest that
the stem region of HA might be a potential target for prevention of influenza
virus infection and antiviral therapy.
Descriptors: antibodies, monoclonal therapeutic use,
bronchopneumonia therapy, hemagglutinins viral immunology, influenza therapy,
influenza A virus avian immunology, human immunology, pneumonia, viral therapy,
antibodies, monoclonal immunology, bronchopneumonia prevention and control,
dose response relationship, immunologic, influenza prevention and control,
mice, pneumonia, viral prevention and control, random allocation, time factors.
Lipkind, M., K. Hornstein, E. Shihmanter, K. Davidov,
and D. Shoham (1983). Retrospective identification as influenza virus of a
hemagglutinating agent isolated from turkeys in Israel in 1973. Comparative
Immunology, Microbiology and Infectious Diseases 6(2): 135-9. ISSN: 0147-9571.
NAL
Call Number: QR180.C62
Descriptors: hemagglutinins viral isolation and
purification, influenza A virus avian isolation and purification, turkeys
microbiology, hemagglutinins viral immunology, avian immunology, Israel.
Lipkind, M., I.V. Tsvetkova, and N.V. Gribkova (
1973). Neuraminidase and hemagglutinin activities in subcellular fractions
of NDV- and FPV-infected chick embryo cells and their re-distribution following
Triton X 100 treatment. Archiv
Fur Die Gesamte Virusforschung
40(3): 300-6. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: hemagglutinins viral analysis, influenza A
virus avian immunology, neuraminidase analysis, Newcastle disease virus
immunology, surface active agents pharmacology, cell fractionation, cell
nucleus, cultured cells, centrifugation, density gradient, chick embryo, avian
enzymology, avian growth and development, microsomes, mitochondria, Newcastle
disease virus enzymology, Newcastle disease virus growth and development,
ribosomes, subcellular fractions analysis.
Lipkind, M., Y. Weisman, and E. Shihmanter (1987). The
isolation of influenza virus from chickens in Israel and studies on its
antigenic relationships with other native isolates of the same antigenicity by
means of monoclonal antibodies. Comparative Immunology, Microbiology and
Infectious Diseases 10(2): 133-9. ISSN:
0147-9571.
NAL
Call Number: QR180.C62
Abstract: A hemagglutinating (HA) agent isolated from
an outbreak of a respiratory disease in a kibbutz broiler farm was identified
as influenza virus A/chicken/Degania, Israel/80(H7N2). Investigation using a panel
of 5 monoclonal antibodies against H7 antigenic subtype has shown substantial
difference of the isolate from the other H7-containing influenza viruses
isolated in Israel. Antigenic relationships between the native H7-containing
strains revealed by means of the monoclonal antibodies led to re-evaluation of
the suggested views on local epizootiology and interspecies transfer of avian
influenza.
Descriptors: antigens, viral analysis, chickens, fowl
plague microbiology, influenza A virus avian immunology, antibodies, monoclonal
immunology, chick embryo, hemagglutination inhibition tests, avian isolation
and purification, Israel.
Lipkind, M.A., I.V. Tsvetkova, and V.N. Muraviyov
(1977). Animal influenza virus neuraminidase: studies on dependence of some
of its properties on its association with hemagglutinin. Developments in
Biological Standardization 39: 447-52.
ISSN: 0301-5149.
NAL
Call Number: QR180.3.D4
Abstract: Neuraminidase (Nase) thermostability and
sensitivity to pH treatment as well as specific enzymatic activity (Nase
activity per 1 HA unit) were determined in two groups of animal influenza virus
strains containing equine 1 and equine 2 Nase subtypes, respectively
(A/equine/Prague/56 (Heq1 Neq1), A/equine/Cambridge/63 (Heq1 Neq1), A/FPV/Dutch/34
(Hav1 Neq1), A/chicken/Germany "N" (Hav2 Neq1), in one group, and
A/equine/Miami/1/63 (Heq2 Neq2), A/turkey/Canada/63 (Hav6 Neq2),
A/duck/Ukraine/1/63 (Hav7 Neq2), in the other group). Nase of all the strains
used was thermotabile when heated at pH 4.5. Nase of Neq1 subtype irrespective
of strain containing it was thermolabilt when heated both at pH 6.5 and 8.1 and
sensitive to pH 4.5 treatment as such (without heating). Inversely, Nase of
Neq2 antigenic subtype irrespective of the strain containing it, was
thermostable when heated at pH 6.5 AND 8.1 and resistant to the treatment of pH
4.5. Specific enzymatic activity was considerably higher in all the strains
containing Neq2 as compared to Neq1-containing strains (4-6 times as much). The
results suggest that thermostability and pH sensitivity of equine Nases of both
antigenic subtypes, as well as their specific activities, do not depend on the
sort of HA which is coupled with enzyme subunits at viral envelope, but
attributed rather to properties of the subunits themselves, such as
glycoprotein entities. The data concerning specific activities may suggest that
in the case of various combinations of Nase subunits with different HA subunits
the amount of enzyme per virion is of the same order.
Descriptors: influenza A virus immunology, neuraminidase
immunology, antigens, viral, heat, hemagglutinins viral, hydrogen-ion
concentration, influenza A virus avian immunology, influenza A virus
enzymology, influenza A virus genetics, recombination, genetic.
Lipkind, M. and E. Shihmanter (1995). Antigenic
heterogeneity of N2 neuraminidases of avian influenza viruses isolated in
Israel. Comparative Immunology Microbiology and Infectious Diseases
18(1): 55-68. ISSN: 0147-9571.
NAL
Call Number: QR180.C62
Abstract: Twenty one N2 neuraminidase (NA)-containing
viruses isolated in Israel from different avian hosts during 1971-1984 were
studied comparatively by means of the panel of 7 monoclonal antibodies (MAB)
against A/Guiyang/57(H2N2) virus. Fifteen from the 21 viruses were studied in
comprehensive cross reaction NA inhibition (NI) tests with the corresponding
polyclonal antisera. The principal result of the studies is that all the
isolates can be distributed into two main groups. The 1st group includes the
majority of the isolates whose NA shows close relatedness to the
"early" (1957 type) N2 NA by NI tests with polyclonal antisera, and
demonstrates remarkable stability in the NI tests by reacting with the same 6
from 7 MABs of the panel. The 2nd group does not show any special kinship to
either "early" or "late" (1968 type) N2 when analyzed with
polyclonal antisera and demonstrates heterogeneity by the analysis with the
MABs. A hypothetical explanation of the phenomenon of co-circulation in the local
avian reservoir of viral strains displaying either remarkable stability or wide
heterogeneity of their NAs is suggested. In accordance with it, the viruses
with "stable" ("conservative") N2 NA did not leave the
avian reservoir and, hence, did not drift because of very low antibody
"selection pressure". Contrary to it, the viruses with heterogeneous
N2 NA had been circulating in the human (mammalian) reservoir during various
periods before their transfer into the avian reservoir; they drifted
accordingly and, being then isolated from birds and designated as
"avian" viruses, demonstrate heterogeneity of their NAs which is
typical for human viruses.
Descriptors: enzymology, immune system, infection,
microbiology, nervous system, veterinary medicine, antigenicity viral ecology.
Lisovskaya, K.V., L.M. Garmashova, and T.E. Medvedeva
(1981). Analysis of ts mutations of cold-adapted influenza
A/Leningrad/134/57 virus variants. Acta Virologica 25(6):
415-7. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: By recombination of ts mutants of fowl plague
virus belonging to different complementation groups with two cold-adapted
variants of human influenza virus, the number and gene localization of ts
mutations occurring in these variants was determined. In the course of
passaging of human influenza virus at lowered temperature, the number of genes
with ts mutations increased.
Descriptors: genes viral, influenza A virus avian
genetics, human genetics, cold, genetic complementation test, mutation,
recombination, genetic.
Litvinov, A.N. (1967). Vliianie interferona na
dinamiku obrazovaniia antitel u kur pri psevdochume ptits. [Effect of
interferon on the dynamics of antibody formation in chickens in avian
pseudopest]. Antibiotiki
12(7): 602-4. ISSN: 0003-5637.
NAL
Call Number: 396.8 An84
Descriptors: antibody formation drug effects, interferons
pharmacology, orthomyxoviridae infections immunology, poultry diseases
immunology, chick embryo, hemagglutination inhibition tests, influenza A virus
avian immunology.
Liu, H., J. Cheng, D. Peng, L. Jia, R. Zhang, and X. Liu (2002). [Comparison
of sequences of the hemagglutinin gene and phylogenetical analysis of H9
subtype avian influenza viruses isolated from some regions in China]. Weishengwu
Xuebao 42(3): 288-97. ISSN:
0001-6209.
NAL
Call Number: 448.3 Ac83
Abstract: In order to explore the genetic mutaions of
the hemagglutinin(HA) gene and the law of molecular epidemiology of H9 subtype
avian influenza viruses in China, 23 H9 subtype avian influenza viruses(AIVs)
were isolated from 12 provinces of China in recent years. Their nucleotide
sequences of cDNA of HA gene were determined by RT-PCR and sequencing. Their
nucleotide and putaive amino acid sequences homology was compared. The results
showed that their nucleotide sequence homology was from 94.1% to 100% and that
amino acid sequence homology was 95.4% to 100%. The sequences of the HA gene of
these isolates were analyzed and compared with that of another 8 isolates from
reference. The similedty indicated that HK170499 isolated from Hong Kong was
close to the 2 isolates of Japan. And of the 31 isolates with complete HA gene
sequences there were 5 isolates, HA gene of which were loss of one potelltial
glycosylation site, which were CKGS199, CKTJ196, CKT296, CKSH300 and CKBJ197.
Then 1098 nucleotide regions (bases 55 to 1,152) of HA gene of 23 isolates in
this study were analyzed phylogenetically and compared with sequences from 31
H9 subtype viruses available in the GenBank database. Although considerable
variation at the cleavage sites of the different viruses was observed, giving
10 different amino acid motits, none had multiple basic amino acids that
correlate with highly pathogenic avian influenza (HPAI) isolates. Examination
of amino acid sequences involved in repeptor binding site(RBS) revealed that
the amino acid residue at position 191 characteristically distributed in the 54
isolates, that is, this amino acid residue of the isolates of mainland China
and several Hong Kong strains was Asn(N) and that of the others was His(H). And
the 141 143 amino acid residues, involved in forming the potential
glycosylation sites, had the similary characteristic distribution with the
191aa position. The isolates with Asn-191. excluding CKBJ197, had NVS in the
position 141aa143aa, meanwhile those with His-191 had NVT. Twenty-six mainland
China isolates was genetically in Eurasian lineage but did not show distinctly
geographical and temporal relationship. It is concluded that in recent years
H9N2 subtype AIV, circulating in chicken flocks of mainland China, may have a
common origini. These findings provides importan basis for establishment of
scientifically preventive measurements to control H9 subtype avian influenza.
Descriptors: genes viral, hemagglutinin glycoproteins, influenza
virus genetics, influenza A virus avian genetics, phylogeny, amino acid
sequence, base sequence, chickens, China, DNA, complementary genetics, fowl
plague virology, avian classification, avian isolation and purification,
sequence homology.
Liu HongQi, Huang Yong, Cheng Jian, Peng DaXin, Jia
LiJun, Zhang RuKuan, and Liu XiuFan (2002). Genetic mutations of the
hemagglutinin gene of H9N2 subtype avian influenza
viruses under the selective pressure of vaccination. Chinese Journal of
Virology 18(2): 149-154. ISSN:
1000-8721.
Descriptors: vaccination, avian influenza virus, genetic
mutations, poultry.
Liu, H., X. Liu, J. Cheng, D. Peng, L. Jia, and Y.
Huang (2003). Phylogenetic analysis of the hemagglutinin genes of twenty-six
avian influenza viruses of subtype H9N2 isolated from chickens in China during
1996-2001. Avian Diseases 47(1): 116-127. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The complete coding region of hemagglutinin
genes from 26 influenza A viruses of H9N2 subtype isolated Prom chicken flocks
in China during 1996-2001 was amplified and sequenced. Sequence analysis and
phylogenetic studies of H9N2 subtype viruses on the basis of data of 26 viruses
in this study and 71 selected strains available in the GenBank were conducted.
The results revealed that all the mainland China isolates showed high homology
(94.1%-100%) and were assigned to a special sublineage in the major Eurasian
lineage, in contrast to the high heterogeneity of Hong Kong SAR isolates. All
the 29 mainland China isolates and six Hong Kong SAR strains also had the
following common characteristics: sharing the same sequence of proteolytic
cleavage site with one additional basic amino acid, RSSR, with only two
exceptions; having the same amino acid motif of the receptor-binding site,
YWTNV/ALY; 23 of 28 isolates bearing seven potential glycosylation sites and
the remaining five having six; and sharing characteristic deduced amino acid
residues Asn-183 at the receptor-binding site and Ser-130 at the potential
glycosylation site. We concluded that the H9N2 subtype influenza viruses
circulating in chicken flocks in China since the 1990s and Ck/HK/G9/97-like
viruses isolated in Hong Kong SAR should have a common origin, whereas
Qu/HK/G1/97-like viruses including human strains isolated in Hong Kong SAR
might originate from other places. The available evidence also suggests that
the H9N2 viruses of special lineage themselves and factors prone to secondary
infections may contribute to the widespread and dominant distribution of
viruses of this subtype in chicken flocks in China and other Asian countries.
Descriptors: infection, molecular genetics, systematics
and taxonomy, virology, phylogenetic analysis mathematical and computer
techniques, reverse transcriptase polymerase chain reaction, genetic
techniques, laboratory techniques, sequence analysis, sequence homology.
Liu, J.H., K. Okazaki, W.M. Shi, and H. Kida (2003). Phylogenetic
analysis of hemagglutinin and neuraminidase genes of H9N2 viruses isolated from
migratory ducks. Virus Genes 27(3): 291-6. ISSN: 0920-8569.
NAL
Call Number: QH434.V57
Abstract: Genetic analysis indicated that the pandemic
influenza strains derived from wild aquatic birds harbor viruses of 15
hemagglutinin (HA) and 9 neuraminidase (NA) antigenic subtypes. Surveillance
studies have shown that H9N2 subtype viruses are worldwide in domestic poultry
and could infect mammalian species, including humans. Here, we genetically
analyzed the HA and NA genes of five H9N2 viruses isolated from the migratory
ducks in Hokkaido, Japan, the flyway of migration from Siberia during
1997-2000. The results showed that HA and NA genes of these viruses belong to
the same lineages, respectively. Compared with those of A/quail/Hong
Kong/G1/97-like and A/duck/Hong Kong/Y280/97-like viruses, HA and NA of the
migratory duck isolates had a close relationship with those of H9N2 viruses
isolated from the chicken in Korea, indicating that the Korea H9N2 viruses
might be derived from the migratory ducks. The NA genes of the five isolates
were located in the same cluster as those of N2 viruses, which had caused a
human pandemic in 1968, indicating that the NA genes of the previous pandemic
strains are still circulating in waterfowl reservoirs. The present results
further emphasize the importance of carrying out molecular epidemiological
surveillance of H9N2 viruses in wild ducks to obtain more information for the
future human influenza pandemics preparedness.
Descriptors: ducks virology, influenza A virus avian
genetics, amino acid sequence, base sequence,
binding sites genetics, DNA, viral genetics, disease reservoirs,
epidemiology, molecular, genes viral, hemagglutinins viral genetics, avian
enzymology, avian immunology, avian isolation and purification, Japan,
neuraminidase genetics, phylogeny.
Liu, J.H., Q.M. Wu, W.M. Shi, and Y.P. Guo (2003). Cloning
and expression of the nonstructural protein (NS1) of the H9N2 chicken influenza
virus. Virologica Sinica 18(5): 503-505. ISSN: 1003-5125.
NAL
Call Number: QR355.P5
Descriptors: Western blot, cloning, influenza virus.
Liu, J.H., K. Okazaki, G.R. Bai, W.M. Shi,
A. Mweene, and H. Kida (2004). Interregional transmission of the internal
protein genes of H2 influenza virus in migratory ducks from North America to
Eurasia. Virus Genes 29(1):
81-6. ISSN: 0920-8569.
NAL
Call Number: QH434.V57
Abstract: H2 influenza virus caused a pandemic in 1957
and has the possibility to cause outbreaks in the future. To assess the
evolutionary characteristics of H2 influenza viruses isolated from migratory
ducks that congregate in Hokkaido, Japan, on their flyway of migration from
Siberia in 2001, we investigated the phylogenetic relationships among these
viruses and avian and human viruses described previously. Phylogenetic analysis
showed that the PB2 gene of Dk/Hokkaido/107/01 (H2N3) and the PA gene of
Dk/Hokkaido/95/01 (H2N2) belonged to the American lineage of avian virus and
that the other genes of the isolates belonged to the Eurasian lineage. These
results indicate that the internal protein genes might be transmitted from
American to Eurasian avian host. Thus, it is further confirmed that
interregional transmission of influenza viruses occurred between the North
American and Eurasian birds. The fact that reassortants could be generated in
the migratory ducks between North American and Eurasian avian virus lineage
further stresses the importance of global surveillance among the migratory
ducks.
Descriptors: ducks virology, emigration and immigration,
influenza A virus, avian genetics, influenza, avian virology, viral proteins
genetics, Asia, Europe, avian influenza A virus classification, molecular
sequence data, North America, phylogeny, sequence analysis, DNA.
Lohmann, W. (1976). A possible mechanism for the
action of some myxoviruses. Radiation and Environmental Biophysics
13(4): 273-80. ISSN: 0301-634X.
NAL
Call Number: 442.8 B5242
Abstract: The redox properties of some myxoviruses
[Fowl plaque virus strain Rostock (FPV), New Castle Disease virus strain Italy
(NDV), B/Hong Kong, A/Port Chalmers, A/Victoria, A/Scotland, and A/Fort Dir)
and electron microscopic studies as well as by the determination of the
hemagglutination (HA) titer (antigen efficiency). The results have shown that
viruses decrease the spin concentration of Cu2+ by acting as a reducing species
(electron donor) which will result in the inactivation (oxidation) of the
virus. Addition of an oxidizing substance, such as H2O2, to a virus suspension
also leads to an oxidation of the viruses, and, thus, to their inability to
reduce Cu2+. This result is confirmed by the decrease of the HA titer of
viruses with increasing Cu2+ concentrations. H2O2 could not be applied for the
HA titer test since it interacts with the erythrocytes of the chicken blood
used for this determination. Therefore, another oxidizing substance (oxidized
glutathione, GSS) was selected which exhibited a slightly less pronounced
effect than Cu2+. Since reduced glutathione (GSH) exerts a similar but less
pronounced effect than GSS, it might be concluded that viruses have a redox
system of their own and act as reducing or oxidizing substance depending on the
biological receptor system. Electron microscopic studies confirm this
hypothesis. As can be seen by the electron micrographs, increasing
concentrations of either Cu2+, GSS, H2O2, KMnO4, or GSH will, finally, result
in a complete destruction of the virus. Because of structural similarities it
might be assumed that other types of viruses behave very similarly.
Descriptors: influenza A virus metabolism, Newcastle
disease virus metabolism, copper, electron spin resonance spectroscopy,
glutathione, hemagglutination, viral, avian metabolism, avian ultrastructure,
human metabolism, human ultrastructure, Newcastle disease virus ultrastructure,
oxidation reduction, peroxides, potassium permanganate, time factors.
Lohmeyer, J. and H.D. Klenk (1979). A mutant of
influenza virus with a temperature-sensitive defect in the posttranslational
processing of the hemagglutinin. Virology 93(1): 134-45. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: endoplasmic reticulum metabolism,
hemagglutinins viral immunology, influenza A virus avian metabolism, viral
proteins metabolism, carbohydrates metabolism, cell line, hemagglutination,
viral, avian genetics, mutation, neuraminidase metabolism, temperature.
Lohmeyer, J., L.T. Talens, and H.D. Klenk (1979). Biosynthesis
of the influenza virus envelope in abortive infection. Journal of
General Virology 42(1): 73-88. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Synthesis and processing of the envelope
proteins of influenza A virus (fowl plague virus) have been analysed in BHK,
HeLa and L cells, in which the virus undergoes abortive replication and does
not form virus particles, and in the productive chick embryo fibroblast system.
In abortive infection, synthesis of the M protein is specifically inhibited.
The extent of this defect varies depending on the host cell and the amount of
virus particles formed closely reflects the amount of M synthesized. Cell
fractionation experiments demonstrated that the haemagglutinin glycoprotein HA
is synthesized in abortive as well as in productive cells at the rough
endoplasmic reticulum, that it migrates via smooth internal membranes to the
plasma membrane and that it is cleaved by proteolysis into fragments HA1 and
HA2 in the course of migration. Immune electron
microscopy using monospecific antibodies against haemagglutinin and
neuraminidase showed that both glycoproteins are exposed at the cell surface.
Thus, synthesis and processing of the virus glycoproteins does not depend on
the formation of the M protein. However, the M protein appears to be necessary
for budding and thus for particle formation.
Descriptors: influenza A virus avian growth and
development, viral proteins biosynthesis, cell line, cell membrane analysis,
cultured cells, endoplasmic reticulum metabolism, glycoproteins biosynthesis,
hemagglutinins viral analysis, neuraminidase biosynthesis, viral proteins
analysis.
Lomniczi, B., F.X. Bosch, A.J. Hay, and J.J. Skehel
(1977). Influenza virus infection of a cell-cycle mutant of Chinese hamster
ovary cells. Journal of General Virology 35(1): 187-90. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: cell line, influenza A virus avian growth and
development, mutation, cell division, DNA biosynthesis, hamsters, avian
metabolism, ovary, peptide synthesis, temperature, viral proteins biosynthesis,
virus replication.
Long, W. and D.C. Burke (1968). The effect of
infection with fowl-plague virus on protein synthesis in chick-embryo cells.
Biochemical Journal 110(3):
41. ISSN: 0264-6021.
NAL
Call Number: QP501,B64
Descriptors: chick embryo metabolism, influenza A virus
avian metabolism, avian radiation effects, orthomyxoviridae infections
metabolism, proteins biosynthesis, depression, chemical, interferons
biosynthesis, RNA viral biosynthesis, ultraviolet rays, viral proteins
biosynthesis, virus replication drug effects.
Long, W.F. (1971). Effect of metabolic inhibitors
on viral and polynucleotide induction of chick cell interferon. Microbios
4(15): 253-9. ISSN: 0026-2633.
NAL
Call Number: QR1.M54
Descriptors: cycloheximide pharmacology, dactinomycin
pharmacology, influenza A virus avian radiation effects, interferons
biosynthesis, poly I C pharmacology, puromycin pharmacology, reoviridae, chick embryo, radiation effects,
tissue culture, ultraviolet rays.
Long, W.F. and D.C. Burke (1970). The effect of
infection with fowl plague virus on protein synthesis in chick embryo cells.
Journal of General Virology 6(1): 1-14.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian metabolism, proteins
biosynthesis, carbon isotopes, chick embryo, cycloheximide pharmacology,
dactinomycin pharmacology, avian drug effects, avian radiation effects,
interferons pharmacology, phenylalanine pharmacology, puromycin pharmacology,
RNA biosynthesis, RNA viral biosynthesis, radiation effects, time factors,
tritium, ultraviolet rays, uridine metabolism, valine metabolism, virus
cultivation.
Long, W.F. and J. Olusanya (1972). Adamantanamine
and early events following influenza virus infection. Archiv Fur Die
Gesamte Virusforschung 36(1): 18-22.
ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, RNA viral antagonists and inhibitors, carbon isotopes, cultured
cells drug effects, cultured cells metabolism, chick embryo, cycloheximide
pharmacology, dactinomycin pharmacology, depression, chemical, electrophoresis,
disc, avian growth and development, avian metabolism, avian radiation effects,
interferons biosynthesis, proteins biosynthesis, RNA analysis, RNA
biosynthesis, viral biosynthesis, radiation effects, time factors, tritium,
ultraviolet rays, uridine metabolism, virus replication drug effects.
Lu, B.L., R.G. Webster, and V.S. Hinshaw (1982). Failure
to detect hemagglutination-inhibiting antibodies with intact avian influenza
virions. Infection and Immunity 38(2): 530-5. ISSN: 0019-9567.
NAL
Call Number: QR1.I57
Descriptors: antibodies, viral analysis, hemagglutinins
viral immunology, influenza A virus avian immunology, orthomyxoviridae
infections immunology, ducks immunology, ferrets immunology, hemagglutination
inhibition tests, avian physiology, mice, mice inbred BALB c immunology, T
lymphocytes, cytotoxic immunology, virus replication.
Lu, H. and A.E. Castro (2004). Evaluation of the
infectivity, length of infection, and immune response of a low-pathogenicity
H7N2 avian influenza virus in specific-pathogen-free chickens. Avian
Diseases 48(2): 263-70. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The H7N2 subtype of avian influenza virus
(AIV) field isolate (H7N2/chicken/PA/3779-2/97), which caused the 1997-98 AIV
outbreak in Pennsylvania, was evaluated for its infectivity, length of
infection, and immune response in specific-pathogen-free (SPF) chickens. The
composite findings of three clinical trials with various concentrations of
virus indicated that this H7N2 subtype contained minimal pathogenicity for
chickens. The concentration of the virus in the inoculum proved critical in the
establishment of a productive infection in a chicken. Seven-day-old SPF
chickens were not infected when inoculated with 10(0.7-2.0) mean embryo lethal
dose (ELD50) of the H7N2 virus per bird. At this dose level, the immune
response to this virus was not detected by the hemagglutination-inhibition (HI)
test. Nonetheless, chickens at ages of 5 and 23 wk old tested were successfully
infected when exposed to 10(4.7-5.7) ELD50 of H7N2 infectious doses per bird by
various routes of administration and also by direct contact. Infected birds
started shedding virus as early as 2 days postinoculation, and the period of
virus shedding occurred mostly within 1 or 2 wk postinoculation (WPI). This
H7N2 subtype of AIV induced a measurable immune response in all birds within 2 wk
after virus exposure. Antibody titers were associated with AIV infectious doses
and age of exposure of birds. Challenge of these infected birds with the same
H7N2 virus at 5 and 10 WPI indicated the infective virus was recoverable from
cloacal swabs at 3 days postchallenge and disappeared thereafter. In these
challenged birds, the antibody levels as measured by the HI test spiked within
1-2 wk.
Descriptors: antibodies, viral analysis, chickens
virology, influenza A virus, avian pathogenicity, avian virology, poultry
diseases virology, antibody formation, cloaca virology, hemagglutination
inhibition tests methods, hemagglutination inhibition tests veterinary,
immunophenotyping, avian immunology, avian isolation and purification, avian
immunology, poultry diseases immunology, specific pathogen free organisms,
virus shedding.
Lu, J., Peng DaXin, Wu YanTao, Zhang RuKuan, and Liu
XiuFan (2003). Amplification of full-length hemagglutinin and neuraminidase
genes of H9N2 avian influenza virus and gene sequence comparison. Journal
of Yangzhou University, Agricultural and Life Sciences Edition, Yangzhou China
24(1): 18-22. ISSN: 1671-4652.
NAL
Call Number: S19.Y36
Descriptors: amino acid, complementary DNA,
hemagglutinins, strains, avian influenza virus, China.
Lyon, J.A. and V.S. Hinshaw (1993). Inhibition of
nitric oxide induction from avian macrophage cell lines by influenza virus.
Avian Diseases 37(3): 868-73.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The virulent avian influenza virus A/Ty/Ont/7732/66
(H5N9) (Ty/Ont) causes a rapid destruction of lymphoid cells in infected birds.
Avian macrophage cell lines, HD11 and MQ-NCSU, support productive replication
of Ty/Ont and other influenza viruses. Therefore, the ability of these cell
lines to produce nitric oxide (NO), a potentially cytotoxic mediator, in
response to infection with Ty/Ont was examined. Although treatment with
bacterial lipopolysaccharides (LPS) resulted in high NO levels, infection of
macrophages with Ty/Ont resulted in NO levels lower than NO levels in untreated
cells. Furthermore, Ty/Ont was able to inhibit the positive response to LPS in
cultures simultaneously treated with LPS and virus. However, inactivated
influenza virus did not exhibit this inhibitory effect. Different strains of
influenza virus varied in their ability to inhibit NO production by the
macrophages; this may be related to the level of virus replication in these
cells. These data suggest that the ability of the avian macrophage to activate
the NO synthesis pathway is seriously impaired by infection with virulent
influenza viruses such as Ty/Ont.
Descriptors: influenza A virus avian pathogenicity,
macrophages metabolism, macrophages microbiology, nitric oxide biosynthesis,
amino acid oxidoreductases antagonists and inhibitors, arginine analogs and
derivatives, arginine pharmacology, cell line, chickens, fowl plague etiology,
avian physiology, macrophages immunology, mice, nitric oxide synthase, orthomyxoviridae pathogenicity,
orthomyxoviridae physiology, species specificity, virus replication, omega n
methylarginine.
Lyon, J.A. and V.S. Hinshaw (1991). Replication of
influenza A viruses in an avian macrophage cell line. Journal of General Virology 72(Pt. 8):
2011-3. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The virulent avian influenza virus
A/Ty/Ont/7732/66 (H5N9) (Ty/Ont) causes severe destruction of the lymphoid
cells in infected birds. Previous studies have suggested that viral infection
of macrophages may be involved. However, Ty/Ont failed to replicate
productively in primary cultures of chicken macrophages. Therefore, in an
effort to develop an in vitro system for our studies, we examined the
susceptibility of an avian macrophage cell line, HD11, to Ty/Ont. We found that
Ty/Ont replicated in the HD11 cells to high titres, as measured by
haemagglutination (HA) assays and infectivity yields. To determine whether this
property was unique to Ty/Ont, we also examined the replication of influenza
viruses representative of all 13 HA subtypes and an attenuated variant of
Ty/Ont. All of the tested viruses replicated in HD11 cells; the avirulent
strains required the presence of trypsin in the culture medium whereas virulent
viruses and the attenuated variant of Ty/Ont did not. These results suggest
that the HD11 cells can support the replication of a wide variety of influenza
viruses and that this continuous avian cell line may prove useful for in vitro
studies on these viruses.
Descriptors: influenza A virus avian physiology,
macrophages microbiology, virus replication, cell line, chickens.
Machavariani, A.T. (1970 ). Primenenie zhivykh
vaktsin protiv psevdochumy ptits. [Use of live vaccine against fowl
pseudoplague]. Veterinariia (2): 49-52. ISSN: 0042-4846.
NAL
Call Number: 41.8 V6426
Descriptors: fowl plague immunology, avian influenza
virus, viral vaccines, aerosols, chickens.
Madeley, C.R., W.H. Allan, and A.P. Kendal (1971). Studies
with avian influenza A viruses: serological relations of the hemagglutinin and
neuraminidase antigens of ten virus isolates. Journal of General
Virology 12(Pt. 2): 69-78. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: avian influenza A virus, strain comparisons,
hemagglutinin, neuraminidase anitgens, chickens.
Mahy, B.W., T. Barrett, D.J. Briedis, J.M. Brownson,
and A.J. Wolstenholme (1980). Influence of the host cell on influenza virus
replication. Philosophical Transactions of the Royal Society of London.
Series B Biological Sciences 288(1029): 349-57. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Abstract: The replication of influenza virus is
characterized by a unique dependence upon host cell nuclear function. In
contrast to all other negative strand RNA viruses, transcription from host
cellular DNA is a prerequisite for the synthesis of virus-specific messenger
RNA; new DNA synthesis is not required. We have analysed the distribution of
each of the nine virus-specified proteins between the nucleus and cytoplasm of
virus-infected cells, and find that in addition of the NP and the NS1 proteins,
two of the three P proteins show preferential migration into the nucleus. This
subgroup of virus proteins may be involved in the early transcription of the
viral genome which probably occurs in the nucleus. In non-permissive cell lines
and in cells whose DNA function has been impaired by treatment with ultraviolet
light, N-acetoxyacetaminofluorene or low doses of actinomycin D, production of
some late virus proteins is inhibited. The specific host function required for
this switch to late protein synthesis is unknown but in the cells treated with
actinomycin D an abnormal accumulation of virus-specific mRNA occurs in the
nucleus. In all cases studied, synthesis of new vRNA ceases when production of
these late proteins has been blocked.
Descriptors: influenza A virus avian genetics, RNA viral
biosynthesis, virus replication drug effects, biological transport drug
effects, cell nucleus physiology, cultured cells, cytoplasm metabolism,
dactinomycin pharmacology, poly A metabolism, messenger metabolism,
transcription, genetic, viral proteins metabolism.
Mahy, B.W. and P.A. Bromley (1969). Synthesis of
ribonuclease-resistant ribonucleic acid by fowl-plague-virus-induced
ribonucleic acid polymerase. Biochemical Journal 114(4): 64. ISSN: 0264-6021.
NAL
Call Number: QP501,B64
Descriptors: influenza A virus avian, RNA biosynthesis,
RNA nucleotidyltransferases metabolism, ribonucleases, chick embryo,
fibroblasts metabolism, tissue culture, virus cultivation.
Mahy, B.W., N.J. Cox, S.J. Armstrong, and R.D. Barry
(1973). Multiplication of influenza virus in the presence of cordycepin, an
inhibitor of cellular RNA synthesis. Nature New Biology 243(127):
172-4. ISSN: 0090-0028.
NAL
Call Number: QH301.N33
Descriptors: deoxyadenosines pharmacology, influenza A
virus avian drug effects, Newcastle disease virus drug effects, RNA
biosynthesis, virus replication drug effects, cell nucleolus metabolism, cell
nucleus metabolism, cultured cells, chick embryo, depression, chemical, kinetics,
tritium, uridine metabolism.
Makarova, K.S., Y.I. Wolf, E.P. Tereza, and V.A.
Ratner (1998). Different patterns of molecular evolution of influenza A
viruses in avian and human populations. Genetika 34(7):
890-896. ISSN: 0016-6758.
NAL
Call Number: QH431.A1G4
Abstract: Patterns of molecular evolution of the
influenza virus proteins and genes are discussed. The subsets of all viral
genes corresponding to statistically significant clusters on dendrogram were
shown to fall into two distinct groups. The first group was characterized by
the presence of an exact linear relationship between the year of the strain
isolation and the evolutionary distance. The subsets of human influenza virus
genes belong to this group. A method for eliminating the "frozen"
strains from the subsets and for calculating the evolutionary rates without
construction of phylogenetic trees has been elaborated. The substitution rates
calculated according to this technique agreed with the data obtained
previously. A linear relationship was not observed in the second group. This
group was predominantly composed of avian influenza virus genes. The lack of
linear correlation pointed to the cocirculation of a large amount of different
influenza virus genomic segments in the avian population. An approach for an examination
of the role of intragenic recombination in the development of the antigenic
subtypes of hemagglutinin is suggested. Our results suggest that recombination
did not play a considerable role in this process, and that all modern subtypes
of this protein were probably formed before the introduction of the influenza
viruses into the human population. These findings are consistent with the
hypothesis that influenza viruses penetrated into human population from their
pools in avian populations.
Descriptors: evolution and adaptation, genetics, influenza
virus, human, avian.
Makarova, N.V., N.V. Kaverin, S. Krauss, D. Senne,
and R.G. Webster (1999). Transmission of Eurasian avian H2 influenza virus
to shorebirds in North America. Journal of General Virology 80(Pt.
12): 3167-71. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Influenza A virus of the H2 subtype caused a
serious pandemic in 1957 and may cause similar outbreaks in the future. To
assess the evolution and the antigenic relationships of avian influenza H2
viruses, we sequenced the haemagglutinin (HA) genes of H2 isolates from
shorebirds, ducks and poultry in North America and derived a phylogenetic tree
to establish their interrelationships. This analysis confirmed the divergence of
H2 HA into two geographical lineages, American and Eurasian. One group of
viruses isolated from shorebirds in North America had HA belonging to the
Eurasian lineage, indicating an interregional transmission of the H2 gene.
Characterization of HA with a monoclonal antibody panel revealed that the
antigenicity of the Delaware strains differed from the other avian strains
analysed. The data emphasizes the importance of avian influenza surveillance.
Descriptors: fowl plague transmission, fowl plague
virology, hemagglutinin glycoproteins, influenza virus genetics, influenza A
virus avian genetics, Asia, birds virology, Europe, genes viral,
hemagglutination inhibition tests, avian isolation and purification, North
America, phylogeny, poultry virology.
Mandler, J., K. Muller, and C. Scholtissek (1991). Mutants
and revertants of an avian influenza A virus with temperature-sensitive defects
in the nucleoprotein and PB2. Virology 181(2): 512-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: ts19 is a temperature-sensitive (ts) mutant
of the influenza A fowl plague virus with a defect in the nucleoprotein (NP).
In ts19-infected chicken embryo cells all viral components are synthesized in
normal yields at the nonpermissive temperature, but infectious virus is not
formed. Under these conditions the migration of the NP and M of ts19 from the
cell nucleus to the cytoplasm is affected. This ts defect is due to a single
amino acid replacement (R162K) in a completely conserved region of the NP.
Another mutant with a different defect in the NP is ts81. After infection with
ts81 at 40 degrees no vRNA is being synthesized. By backcross of a revertant
derived from ts81 many isolates with a ts defect in the PB2 protein were
obtained. This ts defect seems to extragenically suppress the ts defect in the
NP gene and to be dominant in a wild-type background.
Descriptors: genes viral, influenza A virus avian
genetics, nucleoproteins genetics, suppression, genetic, viral core proteins
genetics, amino acid sequence, chick embryo, crosses, genetic, avian growth and
development, molecular sequence data, nucleoproteins chemistry, sensitivity and
specificity, temperature, viral core proteins chemistry, virus replication
genetics.
Mandler, J. and C. Scholtissek (1989). Localisation
of the temperature-sensitive defect in the nucleoprotein of an influenza
A/FPV/Rostock/34 virus. Virus Research 12(2): 113-21. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The nucleotide sequences of the nucleoprotein
(NP) genes of fowl plague virus (FPV) and of a temperature-sensitive (ts)
mutant (ts81) derived therefrom have been determined. The ts81-NP nucleotide
sequence possesses a single nucleotide substitution in comparison to the wild
type. This causes an amino acid exchange at position 332 of the NP. An alanine
in the wild type-NP is substituted by a threonine in ts81-NP. This substitution
leads to a significant difference in the secondary structure prediction.
Although this mutation is located within the karyophilic region of the NP, the
accumulation of the NP in ts81-infected cells is not significantly affected at
40 degrees C. Therefore, we assume that the cooperation with one of the
polymerase proteins (P) is interfered with at 40 degrees C, leading to the loss
of viral vRNA or replicative cRNA synthesis. The comparison of the FPV-NP
nucleotide sequence to a previously published sequence of the same strain
(Tomley and Roditi, 1984) highlights ten nucleotide differences, four of them
leading to amino acid substitutions.
Descriptors: influenza A virus avian genetics,
nucleoproteins genetics, viral core proteins, viral proteins genetics, amino
acid sequence, base sequence, cell nucleus metabolism, DNA, viral genetics,
avian metabolism, avian ultrastructure, molecular sequence data, mutation,
nucleoproteins biosynthesis, RNA viral genetics, temperature, viral proteins
biosynthesis.
Manvell, R.J., P.H. Jorgensen, O.L. Nielsen, and D.J.
Alexander (1998). Experimental assessment of the pathogenicity of two avian
influenza A H5 viruses in ostrich chicks (Struthio camelus) and
chickens. Avian Pathology 27(4): 400-404. ISSN: 0307-9457.
NAL
Call Number: SF995.A1A9
Abstract: Virus excretion, immune response, and, for
chickens, deaths were recorded in 3-week-old ostriches and chickens inoculated
by either the intramuscular or intranasal route with one of two influenza A
viruses of subtype H5. One of the viruses, A/turkey/England/50-92/91 (H5N1)
(50/92), was highly pathogenic for chickens causing 5/5 deaths by each route of
inoculation. The other virus, A/ostrich/Denmark-Q/72420/96 (H5N2) (72420/96),
isolated from ostriches in quarantine in Denmark during 1996, was of low
pathogenicity for chickens, causing no clinical signs by either route of
inoculation. No significant clinical signs were seen in any of the ostriches
infected with either of the viruses by either route of infection. Both viruses
were recoverable from both species up to 12 days post-infection, and low
serological responses were detected in surviving infected ostriches and chickens
at 21 days after inoculation.
Descriptors: ostriches, chickens, chicks, avian influenza
virus, susceptibility, experimental infections, pathogenicity, clinical
aspects, antibody formation, mortality, application methods, intramuscular
injection, virus shedding, intranasal administration.
Markushin, S., H. Ghiasi, N. Sokolov, A. Shilov, B.
Sinitsin, D. Brown, A. Klimov, and D. Nayak (1988). Nucleotide sequence of
RNA segment 7 and the predicted amino sequence of M1 and M2 proteins of
FPV/Weybridge (H7N7) and WSN (H1N1) influenza viruses. Virus Research
10(2-3): 263-71. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Since the gene products (M1 and M2) of
influenza virus RNA segment 7 have been implicated in host range restriction,
sensitivity to the drug amantadine, virus yield in chicken embryos as well as
in virus assembly and morphology, we have determined the nucleotide sequence of
this RNA segment for an avian [A/FPV/Weybridge (H7N7)] and a human [A/WSN/33
(H1N1)] virus and compared it to that of the other influenza A virus strains.
The results show that all ten strains of influenza A virus contain an identical
number of nucleotides (1027 bases) in RNA segment 7 and an identical number of
amino acids in M1 (252 aa) and M2 (97 aa) proteins. The observed amino acid
changes are conservative in nature suggesting the requirement of a critical
structure of both proteins in virus assembly. Furthermore, the presence of some
consistent amino acid substitutions among different human and avian strains also
supports the possible existence of host range and drug resistance determinants
in M1 and M2 proteins.
Descriptors: influenza A virus avian genetics, human
genetics, RNA viral genetics, viral matrix proteins genetics, amino acid
sequence, base sequence, avian analysis, human analysis, molecular sequence
data.
Markushin, S.G. and I.U.Z. Gendon (1981). Izuchenie
reguliatsii virusspetsificheskikh polipeptidov ortomiksovirusov na modeli
ts-mutanta virusa chumy, imeiushchego narushenie protsessa transkriptsii.
[Study of regulation of orthomyxovirus virus-specific polypeptides using the
ts-mutant of fowl plague virus having a transcription abnormality as a model].
Voprosy Virusologii (5): 604-7.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The synthesis of virus-specific polypeptides
in cells infected with a ts-mutant of fowl plague virus with disturbed process
of secondary transcription was studied. Synthesis of all virus-specific
proteins was shown to occur under conditions providing for synthesis of polyA+
cRNA at the stage of primary transcription but with disturbance of the
secondary transcription and blocking of polyA- cRNA and vRNA synthesis. No time
regulation of virus-specific polypeptide synthesis was in effect.
Descriptors: influenza A virus avian metabolism, peptide
synthesis, transcription, genetic, viral proteins biosynthesis, avian genetics,
mutation.
Markushin, S.G. and Y.Z. Ghendon (1973). Genetic
classification and biological properties of temperature-sensitive mutants of
fowl plague virus. Acta Virologica 17(5): 369-76. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: influenza A virus avian classification,
cultured cells, chick embryo, fluorouracil pharmacology, genetic
complementation test, hydroxylamines pharmacology, avian pathogenicity,
mutagens pharmacology, mutation drug effects, nitrites pharmacology,
nitrosourea compounds pharmacology, plaque assay, recombination, genetic,
temperature, virus replication drug effects.
Markushin, S.G. and Y.Z. Ghendon (1984). Studies
of fowl plague virus temperature-sensitive mutants with defects in synthesis of
virion RNA. Journal of General Virology 65(Pt. 3): 559-75. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Three different types of impairment in the
synthesis of virion RNA (vRNA) were detected in three groups of
temperature-sensitive (ts) mutants of fowl plague virus (FPV) having ts
mutations in genes 1, 3 and 5 respectively. Normal synthesis of poly-(A+) cRNA,
poly(A-) cRNA and vRNA was observed under non-permissive conditions early in
infection in cells infected with the ts43 mutant having a ts mutation in gene 1
coding for the PB2 protein. However, 4 h after infection synthesis of vRNA
ceased, synthesis of poly(A+) cRNA was reduced drastically, but the rate of
poly(A-) cRNA synthesis was the same as that in cells infected with wild-type
FPV. In cells infected with the ts 166 mutant having a ts mutation in gene 3,
coding for the PA polypeptide, a drastic reduction was observed in poly(A+)
cRNA synthesis under non-permissive conditions. Synthesis of poly(A-) cRNA was
also reduced and synthesis of vRNA was not detected. The ts 60 mutant, having a
ts mutation in gene 5 coding for the NP polypeptide, induced synthesis of all
types of virus-specific RNA under non-permissive conditions, but the regulation
of synthesis of vRNA and poly(A+) cRNA was affected, there being predominant
syntheses of RNA segments 5 and 8 late in infection. In cells infected with
mutants ts43 and ts 166 synthesis of virus-specific proteins was impaired,
which reflected defects in the synthesis of virus-specific RNAs. The data
obtained suggest that the PB2 protein may be contained in an enzyme complex
responsible for synthesis of vRNA, that different enzyme complexes may be
involved in the synthesis of poly(A-) cRNA and vRNA, and that the NP protein
plays a significant role in the regulation of vRNA synthesis.
Descriptors: influenza A virus avian genetics, mutation,
RNA viral biosynthesis, cycloheximide pharmacology, avian metabolism, peptide
synthesis, recombination, genetic, ribonucleoproteins biosynthesis,
temperature.
Markushin, S.G. and D.B. Ghenkina (1976). Principles
of complementation interaction of ts mutants of orthomyxoviruses. Acta
Virologica 20(6): 449-54. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The possibility of complementation between ts
mutants of fowl plague virus (FPV) belonging to 5 different complementation
groups was studied using various time intervals between inoculation of the
cells with two complementation partners. The structural proteins of virions
formed on complementation of individual ts mutants with wild virus were
analysed by polyacrylamide gel electrophoresis after amino acid pulse label
followed by pulse chase. The features of complementation interactions between
the mutants are discussed.
Descriptors: influenza A virus avian growth and
development, avian metabolism, mutation, genetic complementation test, peptide
synthesis, temperature, viral proteins biosynthesis, virus replication.
Markushin, S.G., V.P. Ginzburg, A.M. Khaider, V.V.
Iarosh, E.A. Ivas'ko, and A.I. Klimov (1992). Faktory, vyzyvaiushchie
izmenenie antigennoi struktury gemaggliutinina viursa grippa. [Factors that
cause a change in the antigenic structure of of the influenza virus
hemagglutinin]. Voprosy Virusologii 37(4): 196-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Crossing of norakin-resistant mutant NR1 of
A/Waybridge (H7N7) strain of fowl plague virus (FPV) with human influenza virus
strains produced recombinants inheriting the hemagglutinin (HA) gene of the NR1
mutant and neuraminidase (NA) genes of human influenza virus strains. The R120
recombinant produced by crossing of NR1 with A/Taiwan/1/86 (H1N1) strain,
unlike other recombinants and NR1 mutant, lost the capacity of reacting in H1
test with two monoclonal antibodies (MCA) to HA7: 71/4 and 46/6. The ts mutant
A/FPV/Rostok which has ts-mutation in HA-gene also had changes in the antigenic
specificity of HA. The RA and RB recombinants produced by crossing R120 with
the A/Krasnodar/101/59 strain and inheriting HA-gene from R120 and NA-gene from
A/Krasnodar/101/59 strain recovered the initial HA antigenic structure. No
changes in the antigenic properties of HA were observed in the recombinants
produced by crossing the original A/FPV/Waybridge strain with A/Taiwan/1/86
strain and inheriting HA-gene from the original A/FPV/Waybridge strain and
NA-gene from A/Taiwan/1/86 strain. It is concluded that ts mutations in
influenza virus HA-gene may be accompanied by changes in the antigenic
specificity of this virus HA. The possibilities of manifestation of phenotypic
suppression at the level of influenza virus virion membrane proteins and the
causes of changes in the HA antigenic structure in this virus recombinants are
discussed.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, human immunology, antiviral agents antagonists and
inhibitors, chick embryo, crosses, genetic, drug resistance, microbial, epitopes
genetics, epitopes immunology, genes viral immunology, hemagglutinins viral
genetics, avian genetics, human genetics, mutation immunology, piperidines
antagonists and inhibitors, recombination, genetic genetics, recombination,
genetic immunology, temperature.
Markushin, S.G., V.A. Isachenko, E.V. Molibog, L.Y.A.
Zakstelskaya, and Y.U.Z. Ghendon (1981). Gene homology and antigenic
specificity of envelope proteins of avian influenza virus strains possessing
haemagglutinin Havl. Acta
Virologica 25(2): 65-70. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Comparison of some avian influenza virus
strains possessing haemagglutinin Havl revealed the greatest differences in
strains A/FPV/Weybridge and A/FPV/Rostock/34. These strains differed in the
degree of homology of eight genome fragments, electrophoretic mobility of the
majority of proteins, size of plaques and rct42 marker and displayed
significant differences in antigenic specificity of haemagglutinin. Strains
A/FPV/Weybridge and A/FPV/Dobson proved to be more close in the degree of
genome homology but differed in three genes, electrophoretic mobility of some
proteins, size of plaques, rct42 marker and antigenic specificity of
haemagglutinin. The data obtained indicate that avian influenza virus strains
of the Havl subtype may differ from each other in the degree of gene homology
and some other properties including antigenic specificity of haemagglutinin
like influenza viruses with other haemagglutinin subtypes.
Descriptors: genes viral, hemagglutinins viral immunology,
influenza A virus avian genetics, electrophoresis, polyacrylamide gel,
epitopes, avian immunology, avian physiology, neuraminidase immunology, nucleic
acid hybridization, plaque assay, temperature, viral envelope proteins, viral
proteins immunology.
Marois, P., A. Boudreault, E. DiFranco, and V.
Pavilanis (1971). Response of ferrets and monkeys to intranasal infection
with human, equine and avian influenza viruses. Canadian Journal of
Comparative Medicine Revue Canadienne De Medecine Comparee 35(1):
71-6. ISSN: 0008-4050.
NAL
Call Number: 41.8 C162
Descriptors: Carnivora, influenza veterinary, monkey
diseases microbiology, nose microbiology, orthomyxoviridae pathogenicity,
respiratory tract infections microbiology, antigen antibody reactions, birds,
cross reactions, haplorhini, hemagglutination inhibition tests, horses, immune
sera, influenza immunology, orthomyxoviridae isolation and purification,
respiratory tract infections immunology, turkeys, virus replication.
Massin, P., S. van der Werf, and N. Naffakh (2001). Residue
627 of PB2 is a determinant of cold sensitivity in RNA replication of avian
influenza viruses. Journal of Virology 75(11): 5398-404. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Human influenza A viruses replicate in the
upper respiratory tract at a temperature of about 33 degrees C, whereas avian
viruses replicate in the intestinal tract at a temperature close to 41 degrees
C. In the present study, we analyzed the influence of low temperature (33
degrees C) on RNA replication of avian and human viruses in cultured cells. The
kinetics of replication of the NP segment were similar at 33 and 37 degrees C
for the human A/Puerto-Rico/8/34 and A/Sydney/5/97 viruses, whereas replication
was delayed at 33 degrees C compared to 37 degrees C for the avian
A/FPV/Rostock/34 and A/Mallard/NY/6750/78 viruses. Making use of a genetic
system for the in vivo reconstitution of functional ribonucleoproteins, we
observed that the polymerase complexes derived from avian viruses but not human
viruses exhibited cold sensitivity in mammalian cells, which was determined
mostly by residue 627 of PB2. Our results suggest that a reduced ability of the
polymerase complex of avian viruses to ensure replication of the viral genome
at 33 degrees C could contribute to their inability to grow efficiently in
humans.
Descriptors: influenza A virus avian metabolism, human
metabolism, RNA viral metabolism, viral proteins metabolism, cell line,
mutation, viral genetics, temperature, time factors, transcription, genetic,
viral proteins genetics, virus replication.
Masunaga, K., K. Mizumoto, H. Kato, A. Ishihama, and
T. Toyoda (1999). Molecular mapping of influenza virus RNA polymerase by
site-specific antibodies. Virology 256(1): 130-41. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: antibodies, viral, immunoglobulin G,
influenza A virus avian enzymology, RNA replicase chemistry, base sequence,
binding sites, antibody, chick embryo, enzyme linked immunosorbent assay, genome,
viral, avian genetics, mutagenesis, site directed, oligodeoxyribonucleotides,
RNA replicase metabolism, sequence deletion.
Matlin, K.S., H. Reggio, A. Helenius, and K. Simons
(1981). Infectious entry pathway of influenza virus in a canine kidney cell
line. Journal of Cell Biology 91(3, Pt. 1): 601-13. ISSN: 0021-9525.
NAL
Call Number: 442.8 J828
Abstract: The entry of fowl plague virus, and avian
influenza A virus, into Madin-Darby canine kidney (MDCK) cells was examined
both biochemically and morphologically. At low multiplicity and 0 degrees C,
viruses bound to the cell surface but were not internalized. Binding was not
greatly dependent on the pH of the medium and reached an equilibrium level in
60-90 min. Over 90% of the bound viruses were removed by neuraminidase but not
by proteases. When cells with prebound virus were warmed to 37 degrees C, part
of the virus became resistant to removal b neuraminidase, with a half-time of
10-15 min. After a brief lag period, degraded viral material was released into
the medium. The neuraminidase-resistant virus was capable of infecting the
cells and probably did so by an intracellular route, since ammonium chloride, a
lysosomotropic agent, blocked both the infection and the degradation of viral
protein. When the entry process was observed by electron microscopy, viruses
were seen bound primarily to microvilli on the cell surface at 0 degrees C and,
after warming at 37 degrees C, were endocytosed in coated pits, coated
vesicles, and large smooth-surfaced vacuoles. Viruses were also present in
smooth-surfaced invaginations and small smooth-surfaced vesicles at both
temperatures. At physiological pH, no fusion of the virus with the plasma
membrane was observed. When prebound virus was incubated at a pH of 5.5 or
below for 1 min at 37 degrees C, fusion was, however, detected by ferritin
immunolabeling. t low multiplicity, 90% of the prebound virus became
neuraminidase-resistant and was presumably fused after only 30 s at low pH.
These experiments suggest that fowl plague virus enters MDCK cells by
endocytosis in coated pits and coated vesicles and is transported to the
lysosome where the low pH initiates a fusion reaction ultimately resulting in
the transfer of the genome into the cytoplasm. The entry pathway of fowl plague
virus thus resembles tht earlier described for Semliki Forest virus.
Descriptors: kidney microbiology, cell line, dogs,
endocytosis, hydrogen-ion concentration, lysosomes microbiology, membrane
fusion, microscopy, electron, temperature.
Matlin, K.S. and K. Simons (1983). Reduced
temperature prevents transfer of a membrane glycoprotein to the cell surface
but does not prevent terminal glycosylation. Cell 34(1):
233-43. ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Abstract: The transport kinetics of the influenza virus
hemagglutinin from its site of synthesis to the apical plasma membrane of
Madin-Darby canine kidney cells, a polarized epithelial cell line, were studied
by a sensitive tryptic assay. Hemagglutinin acquired terminal sugars, as judged
by sensitivity to endo-beta-N-acetylglucosaminidase H, 10-15 min after
synthesis, and first appeared on the apical domain 15 min later. None of the
pulse-labeled hemagglutinin accumulated on the basolateral domain. At 20 degrees
C, terminal glycosylation continued, but no hemagglutinin was detected on the
cell surface within 2 hr. If the incubation temperature was raised from 20
degrees C to 37 degrees C, hemagglutinin was quickly externalized,
demonstrating that the inhibition at low temperature was reversible.
Descriptors: cell membrane metabolism, hemagglutinins
viral, influenza A virus avian metabolism, oligosaccharides metabolism, viral
proteins metabolism, biological transport, cell line, dogs, kinetics,
temperature, viral envelope proteins.
Matrosovich, M., A. Tuzikov, N. Bovin, A. Gambaryan,
A. Klimov, M.R. Castrucci, I. Donatelli, and Y. Kawaoka (2000). Early
alterations of the receptor-binding properties of H1, H2, and H3 avian
influenza virus hemagglutinins after their introduction into mammals. Journal
of Virology 74(18): 8502-12. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Interspecies transmission of influenza A
viruses circulating in wild aquatic birds occasionally results in influenza
outbreaks in mammals, including humans. To identify early changes in the
receptor binding properties of the avian virus hemagglutinin (HA) after interspecies
transmission and to determine the amino acid substitutions responsible for
these alterations, we studied the HAs of the initial isolates from the human
pandemics of 1957 (H2N2) and 1968 (H3N2), the European swine epizootic of 1979
(H1N1), and the seal epizootic of 1992 (H3N3), all of which were caused by the
introduction of avian virus HAs into these species. The viruses were assayed
for their ability to bind the synthetic sialylglycopolymers 3'SL-PAA and
6'SLN-PAA, which contained, respectively, 3'-sialyllactose (the receptor
determinant preferentially recognized by avian influenza viruses) and
6'-sialyl(N-acetyllactosamine) (the receptor determinant for human viruses).
Avian and seal viruses bound 6'SLN-PAA very weakly, whereas the earliest
available human and swine epidemic viruses bound this polymer with a higher
affinity. For the H2 and H3 strains, a single mutation, 226Q-->L, increased
binding to 6'SLN-PAA, while among H1 swine viruses, the 190E-->D and
225G-->E mutations in the HA appeared important for the increased affinity
of the viruses for 6'SLN-PAA. Amino acid substitutions at positions 190 and 225
with respect to the avian virus consensus sequence are also present in H1 human
viruses, including those that circulated in 1918, suggesting that substitutions
at these positions are important for the generation of H1 human pandemic
strains. These results show that the receptor-binding specificity of the HA is
altered early after the transmission of an avian virus to humans and pigs and,
therefore, may be a prerequisite for the highly effective replication and
spread which characterize epidemic strains.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, influenza A virus avian metabolism, receptors, virus
metabolism, amino acid sequence, amino
acid substitution, disease outbreaks, ducks virology, hemagglutinin
glycoproteins, influenza virus chemistry, avian isolation and purification,
models, molecular, molecular sequence data, mutation, missense, phylogeny,
protein binding, seals virology, sequence alignment, sialic acids metabolism,
species specificity, swine virology.
Matrosovich, M., N. Zhou, Y. Kawaoka, and R. Webster
(1999). The surface glycoproteins of H5 influenza viruses isolated from
humans, chickens, and wild aquatic birds have distinguishable properties. Journal
of Virology 73(2): 1146-55. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: In 1997, 18 confirmed cases of human
influenza arising from multiple independent transmissions of H5N1 viruses from
infected chickens were reported from Hong Kong. To identify possible phenotypic
changes in the hemagglutinin (HA) and neuraminidase (NA) of the H5 viruses
during interspecies transfer, we compared the receptor-binding properties and
NA activities of the human and chicken H5N1 isolates from Hong Kong and of H5N3
and H5N1 viruses from wild aquatic birds. All H5N1 viruses, including the human
isolate bound to Sia2-3Gal-containing receptors but not to Sia2-6Gal-containing
receptors. This finding formally demonstrates for the first time that receptor
specificity of avian influenza viruses may not restrict initial avian-to-human
transmission. The H5N1 chicken viruses differed from H5 viruses of wild aquatic
birds by a 19-amino-acid deletion in the stalk of the NA and the presence of a
carbohydrate at the globular head of the HA. We found that a deletion in the NA
decreased its ability to release the virus from cells, whereas carbohydrate at
the HA head decreased the affinity of the virus for cell receptors. Comparison
of amino acid sequences from GenBank of the HAs and NAs from different avian
species revealed that additional glycosylation of the HA and a shortened NA
stalk are characteristic features of the H5 and H7 chicken viruses. This
finding indicates that changes in both HA and NA may be required for the
adaptation of influenza viruses from wild aquatic birds to domestic chickens
and raises the possibility that chickens may be a possible intermediate host in
zoonotic transmission.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, influenza A virus avian metabolism, human metabolism, alpha
globulins metabolism, amino acid sequence, carbohydrates metabolism, chickens,
fowl plague virology, Hong Kong, horseradish peroxidase metabolism, influenza
veterinary, influenza virology, avian classification, avian isolation and
purification, human classification, human isolation and purification, molecular
sequence data, neuraminidase metabolism, ovomucin metabolism, phenotype,
receptors, virus metabolism, sequence homology, amino acid.
Matrosovich, M.N., S. Krauss, and R.G. Webster (
2001). H9N2 influenza A viruses from poultry in Asia have human virus-like
receptor specificity. Virology 281(2): 156-62. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, poultry
virology, receptors, virus metabolism, amino acid substitution, Asia, binding
sites, fowl plague transmission, fowl plague virology, hemagglutinin
glycoproteins, influenza virus genetics, hemagglutinin glycoproteins, influenza
virus metabolism, avian classification, avian genetics, human classification,
human genetics, human metabolism, mutation, neuraminidase genetics,
neuraminidase metabolism, phylogeny, viral envelope proteins genetics, viral
envelope proteins metabolism.
Matrosovich, M.N., T.Y. Matrosovich, T. Gray, N.A.
Roberts, and H.D. Klenk (2004). Human and avian influenza viruses target
different cell types in cultures of human airway epithelium. Proceedings
of the National Academy of Sciences of the United States of America
101(13): 4620-4. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: The recent human infections caused by H5N1,
H9N2, and H7N7 avian influenza viruses highlighted the continuous threat of new
pathogenic influenza viruses emerging from a natural reservoir in birds. It is
generally believed that replication of avian influenza viruses in humans is
restricted by a poor fit of these viruses to cellular receptors and
extracellular inhibitors in the human respiratory tract. However, detailed
mechanisms of this restriction remain obscure. Here, using cultures of
differentiated human airway epithelial cells, we demonstrated that influenza
viruses enter the airway epithelium through specific target cells and that
there were striking differences in this respect between human and avian
viruses. During the course of a single-cycle infection, human viruses
preferentially infected nonciliated cells, whereas avian viruses as well as the
egg-adapted human virus variant with an avian virus-like receptor specificity
mainly infected ciliated cells. This pattern correlated with the predominant
localization of receptors for human viruses (2-6-linked sialic acids) on
nonciliated cells and of receptors for avian viruses (2-3-linked sialic acids)
on ciliated cells. These findings suggest that although avian influenza viruses
can infect human airway epithelium, their replication may be limited by a
nonoptimal cellular tropism. Our data throw light on the mechanisms of
generation of pandemic viruses from their avian progenitors and open avenues
for cell level-oriented studies on the replication and pathogenicity of
influenza virus in humans.
Descriptors: influenza A virus, avian pathogenicity, human
pathogenicity, respiratory mucosa microbiology, bronchi, cell line, dogs, avian
isolation and purification, avian physiology, human isolation and purification,
human physiology, kidney, lectins, microscopy, confocal, nasal mucosa
microbiology, sialic acids analysis, trachea.
Matrosovich, M.N., T.Y. Matrosovich, T. Gray, N.A.
Roberts, and H.D. Klenk (2004). Neuraminidase is important for the
initiation of influenza virus infection in human airway epithelium. Journal
of Virology 78(22): 12665-7. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Influenza virus neuraminidase (NA) plays an
essential role in release and spread of progeny virions, following the
intracellular viral replication cycle. To test whether NA could also facilitate
virus entry into cell, we infected cultures of human airway epithelium with
human and avian influenza viruses in the presence of the NA inhibitor
oseltamivir carboxylate. Twenty- to 500-fold less cells became infected in
drug-treated versus nontreated cultures (P < 0.0001) 7 h after virus
application, indicating that the drug suppressed the initiation of infection.
These data demonstrate that viral NA plays a role early in infection, and they
provide further rationale for the prophylactic use of NA inhibitors.
Descriptors: bronchi virology, nasal mucosa virology,
neuraminidase physiology, orthomyxoviridae physiology, trachea virology,
acetamides pharmacology, orthomyxoviridae enzymology.
Matsuda, K., C.H. Park, Y. Sunden, T. Kimura, K.
Ochiai, H. Kida, and T. Umemura (2004). The vagus nerve is one route of
transneural invasion for intranasally inoculated influenza A virus in mice.
Veterinary Pathology 41(2): 101-7.
ISSN: 0300-9858.
NAL
Call Number: 41.8 P27
Abstract: Intranasally inoculated neurotropic influenza
viruses in mice infect not only the respiratory tract but also the central
nervous system (CNS), mainly the brain stem. Previous studies suggested that
the route of invasion of virus into the CNS was via the peripheral nervous
system, especially the vagus nerve. To evaluate the transvagal transmission of
the virus, we intranasally inoculated unilaterally vagectomized mice with a
virulent influenza virus (strain 24a5b) and examined the distribution of the
viral protein and genome by immunohistochemistry and in situ hybridization over
time. An asymmetric distribution of viral antigens was observed between vagal
(nodose) ganglia: viral antigen was detected in the vagal ganglion of the
vagectomized side 2 days later than in the vagal ganglion of the intact side.
The virus was apparently transported from the respiratory mucosa to the CNS
directly and decussately via the vagus nerve and centrifugally to the vagal
ganglion of the vagectomized side. The results of this study, thus, demonstrate
that neurotropic influenza virus travels to the CNS mainly via the vagus nerve.
Descriptors: brain stem virology, influenza A virus,
avian, orthomyxoviridae infections virology, vagus nerve virology,
immunohistochemistry, in situ hybridization, lung virology, mice, nodose
ganglion virology, respiratory mucosa virology.
Matsuura, Y., R. Yanagawa, and H. Noda (1979). Experimental
infection of mink with influenza A viruses. Brief report. Archives of
Virology 62(1): 71-6. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Mink were found to be susceptible to the
intranasal inoculation of human, swine, equine and avian influenza A viruses.
The viruses were recovered until the 7th post inoculation (p.i.) day from the
respiratory tract. The inoculated mink showed antibody response against these
viruses. Contact infection in mink with A/Kumamoto/22/77 (H3N2) was possible.
Descriptors: influenza A virus pathogenicity,
orthomyxoviridae infections microbiology, antibodies, viral biosynthesis,
disease models, animal, hemagglutination inhibition tests, influenza A virus
immunology, influenza A virus isolation and purification, orthomyxoviridae
infections immunology, orthomyxoviridae infections transmission, respiratory
system microbiology.
McCahon, D. and G.C. Schild (1971). An investigation
of some factors affecting cross-reactivation between influenza A viruses. Journal
of General Virology 12(3): 207-19.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: genetics, microbial, influenza A virus avian
pathogenicity, orthomyxoviridae pathogenicity, recombination, genetic,
antigens, viral analysis, azirines pharmacology, chick embryo, fetal membranes,
fibroblasts, heat, hemagglutination inhibition tests, hemagglutinins viral
analysis, horses, immune sera, avian drug effects, avian immunology, avian
radiation effects, neuraminidase analysis, orthomyxoviridae immunology,
orthomyxoviridae radiation effects, quinones pharmacology, rabbits, radiation
effects, tissue culture, ultraviolet rays, virus cultivation.
McCauley, J.W., B.W. Mahy, and S.C. Inglis (1982). Nucleotide
sequence of fowl plague virus RNA segment 7. Journal of General Virology
58(Pt. 1): 211-5. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Nucleotide sequence analysis of a recombinant
DNA clone of RNA segment 7 from FPV/Rostock/34 has shown it to be highly
conserved in comparison with RNA segment 7 from two human strains (Allen et
al., 1980; Winter & Fields, 1980; Lamb & Lai, 1981). FPV RNA segment 7
contains the coding capacity for two polypeptide chains. The sequence homology
between RNA segment 7 of avian and human viruses was greater than 90%, and most
of the changes did not result in amino acid substitutions.
Descriptors: influenza A virus avian genetics, RNA viral
analysis, base sequence, cloning, molecular,
DNA restriction enzymes, DNA, recombinant analysis, Escherichia coli
genetics, plasmids.
McCauley, J.W. and C.R. Penn (1990). The critical
cut-off temperature of avian influenza viruses. Virus Research
17(3): 191-8. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: We have measured the pathogenicity for
6-week-old chicks of infection by H7 avian influenza viruses. One virus, strain
S3 from A/FPV/Rostock/34(H7N1) showed a temperature sensitive phenotype at 41.5
degrees C and reduced pathogenicity. By analysis of reassortants made between
virus S3 and A/FPV/Dobson/27(H7N7), a fully pathogenic virus, two conclusions
arise. (1) The critical cut-off temperature for avian influenza virus in
6-week-old chicks is 41.5 degrees. (2) RNA segment 1 of virus S3 is responsible
for the lack of pathogenicity in reassortant viruses. Nucleotide sequencing of
RNA segment 1 from S3 and its parent, A/FPV/Rostock/34 has revealed a single
mutation at nucleotide 1561. This results in a substitution of isoleucine for
leucine at amino acid position 512 in the cap-binding protein, PB2.
Descriptors: carrier proteins genetics, fowl plague
microbiology, influenza A virus avian pathogenicity, RNA caps metabolism, amino
acid sequence, base sequence, carrier proteins metabolism, chickens, avian
genetics, avian growth and development, molecular sequence data, mutation,
phenotype, plaque assay, RNA cap binding proteins, RNA viral genetics, temperature.
McDowell, W., A. Tlusty, R. Rott, J.N. BeMiller, J.A.
Bohn, R.W. Meyers, and R.T. Schwarz (1988). Inhibition of glycoprotein
oligosaccharide processing in vitro and in influenza-virus-infected cells by
alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene. Biochemical Journal
255(3): 991-8. ISSN: 0264-6021.
NAL
Call Number: QP501,B64
Abstract: The effects of
alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene (MMNT) on mannosidases
involved in asparagine-linked oligosaccharide processing were investigated.
MMNT was found to inhibit the activity of rat liver Golgi alpha-mannosidase I
in a concentration-dependent manner (50% inhibition with 0.18 mM-MMNT), whereas
rat liver endoplasmic-reticulum alpha-mannosidase appeared to be resistant
(less than 5% inhibition at 1 mM-MMNT). Jack-bean alpha-mannosidase was also
sensitive to inhibition by MMNT (50% inhibition with 0.32 mM-MMNT). Treatment
of influenza-virus-infected chick-embryo cells with 1 mM-MMNT led to a decrease
in the formation of complex-type asparagine-linked oligosaccharides and an
accumulation of high-mannose-type oligosaccharides with the composition
Man8(GlcNAc)2 and Man7(GlcNAc)2 on the viral glycoproteins. The biological
activities of influenza-virus haemagglutinin and neuraminidase synthesized in
the presence of 1 mM-MMNT remained unchanged, but the virus was less infectious
than the control.
Descriptors: glycoproteins metabolism, mannosidases
antagonists and inhibitors, oligosaccharides metabolism, triazenes
pharmacology, chick embryo, endoplasmic reticulum drug effects, endoplasmic
reticulum metabolism, fabaceae drug effects, fabaceae enzymology, Golgi
apparatus drug effects, Golgi apparatus enzymology, influenza A virus avian
physiology, liver drug effects, liver enzymology, mannans metabolism, plants,
medicinal, rats, alpha mannosidase.
McGeoch, D., P. Fellner, and C. Newton (1976). Influenza
virus genome consists of eight distinct RNA species. Proceedings of the
National Academy of Sciences of the United States of America 73(9):
3045-9. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: The genomic RNA of the avian influenza A
virus, fowl plague, was fractionated into eight species by electrophoresis in
polyacrylamide-agarose gels containing 6 M urea. The separated 32P-labeled RNA
species were characterized by digestion with RNase T1 and fractionation of the
resulting oligonucleotides by two-dimensional gel electrophoresis; this
demonstrated that each species has a distinct nucleotide sequence. A tentative
correlation of each genome RNA species with the virus protein that it encodes
was made.
Descriptors: influenza A virus avian analysis, RNA viral
analysis, base sequence, genes, structural, molecular weight,
oligoribonucleotides analysis, viral isolation and purification, viral proteins
biosynthesis.
McKimm Breschkin, J.L., A. Sahasrabudhe, T.J. Blick, M. McDonald,
P.M. Colman, G.J. Hart, R.C. Bethell, and J.N. Varghese (1998). Mutations in
a conserved residue in the influenza virus neuraminidase active site decreases
sensitivity to Neu5Ac2en-derived inhibitors. Journal of Virology
72(3): 2456-62. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The influenza virus neuraminidase
(NA)-specific inhibitor zanamivir (4-guanidino-Neu5Ac2en) is effective in
humans when administered topically within the respiratory tract. The search for
compounds with altered pharmacological properties has led to the identification
of a novel series of influenza virus NA inhibitors in which the triol group of
zanamivir has been replaced by a hydrophobic group linked by a carboxamide at
the 6 position (6-carboxamide). NWS/G70C variants generated in vitro, with
decreased sensitivity to 6-carboxamide, contained hemagglutinin (HA) and/or NA
mutations. HA mutants bound with a decreased efficiency to the cellular
receptor and were cross-resistant to all the NA inhibitors tested. The NA
mutation, an Arg-to-Lys mutation, was in a previously conserved site, Arg292,
which forms part of a triarginyl cluster in the catalytic site. In enzyme
assays, the NA was equally resistant to zanamivir and 4-amino-Neu5Ac2en but
showed greater resistance to 6-carboxamide and was most resistant to a new
carbocyclic NA inhibitor, GS4071, which also has a hydrophobic side chain at
the 6 position. Consistent with enzyme assays, the lowest resistance in cell
culture was seen to zanamivir, more resistance was seen to 6-carboxamide, and
the greatest resistance was seen to GS4071. Substrate binding and enzyme
activity were also decreased in the mutant, and consequently, virus replication
in both plaque assays and liquid culture was compromised. Altered binding of
the hydrophobic side chain at the 6 position or the triol group could account
for the decreased binding of both the NA inhibitors and substrate.
Descriptors: conserved sequence, enzyme inhibitors
pharmacology, influenza A virus human enzymology, mutation, N-acetylneuraminic
acid analogs and derivatives, neuraminidase antagonists and inhibitors,
neuraminidase genetics, acetamides
chemistry, acetamides pharmacology, adsorption, binding sites, birds, cell
line, dogs, drug resistance, microbial, enzyme inhibitors chemistry, heating,
hemagglutinin glycoproteins, influenza virus genetics, avian enzymology, human
growth and development, human metabolism, kinetics, molecular structure,
N-acetylneuraminic acid chemistry, N-acetylneuraminic acid pharmacology,
phenotype, plaque assay, sialic acids chemistry, sialic acids pharmacology,
substrate specificity, virus replication.
Medvedeva, T.E., K.V. Lisovskaya, F.I. Polezhaev,
L.M. Garmashova, G.I. Alexandrova, and Y.Z. Ghendon (1984). Location of ts
defects in the genome of cold-adapted recombinant influenza A virus vaccine
strains. Acta Virologica 28(3): 204-11. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The ts phenotype and location of ts mutations
were studied in the genome of parent viruses and those obtained by
recombination of cold-adapted strains A/Leningrad/134/17/57 or
A/Leningrad/134/47/57 with epidemic H1N1 and H3N2 influenza A virus strains.
The epidemic H1N1 and H3N2 strains under study possessed a ts phenotype and
contained ts mutations in one or two genes. The ts phenotype was lost following
three clonings at 40 degrees C, suggesting that influenza virus strains
isolated from humans may be heterogeneous and contain virions either carrying
or not carrying the ts mutations in their genomes. Two cold-adapted strains
possessing a distinct ts phenotype contained ts mutations in three
(A/Leningrad/134/17/57 virus after 17 passages at 25 degrees C) or in five
(A/Leningrad/134/47/57 variant after 30 additional passages at 25 degrees C)
genes coding for non-glycosylated proteins. When compared with cold-adapted
donor strains, the recombinants had either the same set or additional ts
mutations. However, no ts mutation was detected in a gene which had been
inherited from the donor strain. It is suggested that, in addition to the
analysis of the genome composition, in cold-adapted recombinant influenza virus
strains recommended as vaccine candidates it is necessary to control the number
of genes containing ts mutations.
Descriptors: genes viral, influenza A virus avian
genetics, human genetics, mutation, vaccines, attenuated, acclimatization,
adult, child, cold, avian immunology, avian pathogenicity, human immunology,
human pathogenicity, phenotype, recombination, genetic, variation genetics,
virulence.
Meijer, A., J.A. van der Goot, G. Koch, M. van Boven,
and T.G. Kimman (2004). Oseltamivir reduces transmission, morbidity, and
mortality of highly pathogenic avian influenza in chickens. International
Congress Series 1263: 495-498.
Abstract: The effect of the neuraminidase inhibitors
zanamivir and oseltamivir on the transmission of highly pathogenic avian
influenza (HPAI) in chickens was studied. Per group, five chickens inoculated
with HPAI A/Chicken/Pennsylvania/1370/83 H5N2 virus were placed 1 day
post-inoculation (p.i.) in one cage with five contact chickens. Inoculated and
contact chickens were treated twice daily from 1 day before inoculation up to
day 7 p.i. All untreated inoculated and contact chickens became infected and
four inoculated and two contact chickens died. Similarly, all of the
zanamivir-treated inoculated and contact chickens became infected and all
inoculated and four contact chickens died. Obviously, locally active zanamivir
has no effect. In contrast, although oseltamivir could not prevent tracheal
infection of the inoculated chickens, none had an infected cloaca and only one
died. More important, only after stopping treatment three contact chickens
became positive, suggesting limited transmission within or after the treatment
period. In conclusion, treatment with systemically active oseltamivir limits to
a large extent a severe outcome and chicken-to-chicken transmission of HPAI
virus.
Descriptors: highly pathogenic avian influenza virus,
chicken, transmission, antiviral treatment, antiviral prophylaxis,
neuraminidase inhibitors, zanamivir, oseltamivir.
Melnikov, S.Y.A., A.V. Mikheeva, and Y.Z. Ghendon
(1982). Studies on polysomes synthesizing influenza virus haemagglutinin.
Archives of Virology 74(4): 299-310.
ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A fraction of polysomes synthesizing fowl
plague virus (FPV) haemagglutinin (HA) was isolated from an infected chick
embryo fibroblast (CEF) culture using a double immunoprecipitation assay. In an
immunoprecipitate of HA-synthesizing polysomes (HA precipitate) the content of
the HA polypeptide was increased with respect to the M1 + NS1 polypeptides as
compared to a preparation of unprecipitated polysomes. In the HA precipitate,
besides mRNA coding for HA synthesis, we have detected mRNAs corresponding to
genes 1, 2 and 3 coding for high molecular weight P proteins. Studies of a
cytoplasmic extract (CE) from FPV-infected CEF cultures in a sucrose density
gradient revealed a fraction of polysomes with a sedimentation value of about
500S; the composition of virus-specific polypeptides and mRNA of the fraction
was similar to that of the HA precipitate. It is thought that P proteins are
synthesized on membrane-bound polysomes located closely to HA-synthesizing
polysomes.
Descriptors: hemagglutinins isolation and
purification, influenza A virus avian
metabolism, polyribosomes metabolism, viral proteins biosynthesis, cultured
cells, chick embryo, fowl plague immunology, fowl plague metabolism, avian
immunology, RNA, messenger metabolism.
Melnikov, S.Y.A., A.V. Mikheeva, I.A. Leneva, and
Y.Z. Ghendon (1985). Interaction of M protein and RNP of fowl plague virus
in vitro. Virus Research 3(4): 353-65. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The ability of the fowl plague virus (FPV) M
protein to form a complex with FPV RNP and to inhibit the RNP transcriptase
activity in vitro depended on NaCl concentration and did not depend on the
concentration of nonionic detergents. The results obtained indicate that the M
protein-RNP links formed were of an electrostatic rather than a hydrophobic
nature. As demonstrated using individual RNP components, vRNA and RNA-free
protein structures, M protein formed complexes only with vRNA, and the complex
formation was salt-dependent. Analysis of products formed in the in vitro
system containing RNP of FPV in the presence of the M protein showed impairment
in the transcription of all RNA segments. The degree of inhibition correlated
with the size of a segment, transcription of high molecular weight RNA segments
being inhibited significantly more than that of low molecular weight RNA
segments.
Descriptors: influenza A virus avian metabolism,
ribonucleoproteins metabolism, viral proteins metabolism, cultured cells, chick
embryo, avian genetics, RNA replicase metabolism, RNA viral isolation and
purification, ribonucleoproteins isolation and purification, transcription,
genetic, viral matrix proteins, viral proteins isolation and purification.
Meloni, G.A., L. Conventi, F. Busolo, and G.
Bertolini (1980). Effect of Mycoplasma contamination on replication
of some DNA and RNA viruses in cultured cells. Microbiologica 3(4): 461-469. ISSN: 0391-5352.
NAL
Call Number: QR1.M57
Descriptors: Mycoplasma, contamination, viruses,
DNA, RNA, arginine, cell culture.
Men'shikh, L.K., I.A. Rudneva, G.V. Kornilaeva, M.I.
Sokolov, and V.M. Zhdanov (1975). Infektsionnost' RNK virusa istinnoi chumy
ptits v protsesse infektsii [Infectivity of fowl plague virus RNA in the process of infection].
Voprosy Virusologii (6): 722-5.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The conditions for isolation and detection of
the infectious properties of nucleic acid preparations extracted from cells
infected with fowl plague virus were studied. It is suggested that
double-stranded virus-specific RNAs possess the infectious properties.
Descriptors: influenza A virus avian growth and development,
RNA, viral, virus replication, cultured cells.
Meulemans, G., M.C. Carlier, M. Gonze, and P. Petit
(1987). Comparison of hemagglutination-inhibition, agar gel precipitin, and
enzyme-linked immunosorbent assay for measuring antibodies against influenza
viruses in chickens. Avian Diseases 31(3): 560-3. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Individual variations in serological response
to avian influenza virus infection were demonstrated after experimental
infection of specific-pathogen-free chickens with H6N2 influenza virus.
Homologous antibodies were detected from the 6th to the 157th day after
infection using hemagglutination-inhibition or enzyme-linked immunosorbent
assay and from the 11th to the 157th day by agar gel precipitation test.
Descriptors: antibodies, viral analysis, chickens
immunology, fowl plague immunology, influenza A virus avian immunology, chick
embryo, enzyme linked immunosorbent assay, hemagglutination inhibition tests
veterinary, precipitin tests veterinary, specific pathogen free organisms.
Mikheeva, A. and Y.Z. Ghendon (1982). Intrinsic
interference between influenza A and B viruses. Archives of Virology
73(3-4): 287-94. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Reproduction and synthesis of virus-specific
macromolecules were studied in chick embryo fibroblast cultures co-infected
with influenza viruses type A (FPV) and B (B/Japan/73). When a multiplicity of
infection (MOI) of B/Japan/73 virus (10 EID50/cell and higher) was equal to, or
exceeded that of FPV, formation of infectious FPV virions in coinfected cells
was suppressed significantly. At equal MOI of FPV and B/Japan/73 synthesis of
all proteins of one partner and some proteins of the other was observed.
However, when a MOI of one virus was 10 times higher than that of the other,
proteins of the virus used at a higher MOI were formed. Studies of the
synthesis of virus-specific cRNAs formed in the presence of cycloheximide have
shown that at equal MOI. cRNAs were detected that corresponded only to one of
the partners involved in the reproduction. The data obtained suggest that
intrinsic interference between A and B viruses occurs at a stage of primary
transcription.
Descriptors: influenza A virus avian physiology,
orthomyxoviridae physiology, viral interference, cultured cells, chick embryo,
cycloheximide pharmacology, RNA viral biosynthesis, transcription, genetic,
viral proteins biosynthesis.
Mikheeva, A.V., A.Y.A. Melnikov, and E. Anisimova
(1989). Action of rimantadine on the structure of influenza A virus
haemagglutinin. Acta Virologica 33(2): 131-6. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Rimantadine prevents the conformational
changes of influenza virus haemagglutinin (HA) caused by acid pH and the
acquisition of sensitivity to trypsin, protects the haemolytic activity from
inactivation and prevents the morphological changes of HA spikes on the virus
surface.
Descriptors: adamantane analogs and derivatives,
hemagglutinins viral analysis, influenza A virus avian drug effects, membrane
fusion drug effects, rimantadine pharmacology, chick embryo, hemagglutinin
glycoproteins, influenza virus, hydrogen-ion concentration, avian immunology,
avian physiology, protein conformation drug effects, trypsin, virion drug
effects, virion ultrastructure.
Miller Podraza, H., L. Johansson, P. Johansson, T.
Larsson, M. Matrosovich, and K.A. Karlsson (2000). A strain of human
influenza A virus binds to extended but not short gangliosides as assayed by
thin-layer chromatography overlay. Glycobiology 10(10): 975-82. ISSN: 0959-6658.
NAL
Call Number: QP552.G59G593
Abstract: A human strain of influenza virus (A, H1N1)
was shown to bind in an unexpected way to leukocyte and other gangliosides when
compared with avian virus (A, H4N6) as assayed on TLC plates. The human strain
bound only to species with about 10 or more sugars, while the avian strain
bound to a wide range of gangliosides including the 5-sugar gangliosides. By
use of specific lectins, antibodies, and FAB and MALDI-TOF mass spectrometry an
attempt was done to preliminary identify the sequences of leukocyte
gangliosides recognized by the human strain. The virus binding pattern did not
follow binding by VIM-2 monoclonal antibody and was not identical with binding
by anti-sialyl Lewis x antibody. There was no binding by the virus of linear
NeuAcalpha3- or NeuAcalpha6-containing gangliosides with up to seven
monosaccharides per mol of ceramide. Active species were minor
NeuAcalpha6-containing molecules with probably repeated HexHexNAc units and
fucose branches. This investigation demonstrates marked distinctions in the
recognition of gangliosides between avian and human influenza viruses. Our data
emphasize the importance of structural factors associated with more distant
parts of the binding epitope and the complexity of carbohydrate recognition by
human influenza viruses.
Descriptors: gangliosides metabolism, influenza A virus
human metabolism, carbohydrate sequence, chromatography, thin layer methods,
avian metabolism, leukocytes chemistry, molecular sequence data, species
specificity, spectrometry, mass, fast atom bombardment, spectrometry, mass,
matrix assisted laser desorption ionization.
Miller Podraza, H., T. Larsson, J. Nilsson, S.
Teneberg, M. Matrosovich, and L. Johansson (1998). Epitope dissection of
receptor-active gangliosides with affinity for Helicobacter pylori and influenza
virus. Acta Biochimica Polonica 45(2): 439-49. ISSN: 0001-527X.
NAL
Call Number: 385 AC85
Abstract: Receptor-active gangliosides with affinity
for Helicobacter pylori and influenza virus were chemically modified and
analyzed by negative ion fast atom bombardment mass spectrometry (FAB MS) or
electron ionization mass spectrometry (EI MS) after permethylation.
Derivatizations included mild periodate oxidation of the sialic acid glycerol
tail or conversion of the carboxyl group to primary alcohol or amides. The
modified gangliosides were then tested for binding affinity using thin-layer
plates overlaid with labeled microbes or microbe-derived proteins. Mild
periodate oxidation, which shortens sialic acid tail without destruction of
sugar cores, abolished or drastically reduced binding of H. pylori and avian
influenza virus to sialyl-3-paragloboside (S-3-PG). The same effect was
observed in the case of binding of the human influenza virus to receptor-active
gangliosides of human leukocytes. Conversion of S-3-PG or leukocyte
gangliosides to primary alcohols or amides also abolished the binding. However,
mild periodate oxidation had no effect on binding of NAP (neutrophil-activating
protein of H. pylori) to the active ganglioside.
Descriptors: gangliosides metabolism, Helicobacter
pylori metabolism, orthomyxoviridae metabolism, binding sites, gangliosides
chemistry, methylation, receptors, cell surface chemistry, receptors, cell
surface metabolism, spectrum analysis.
Minor, P.D. and N.J. Dimmock (1979). The coupling
of transcription from influenza virions to translation in vitro. Archives
of Virology 59(3): 201-12. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The optimum conditions for the coupling of
fowl plague virus (FPV) transcription to an in vitro reticulocyte translation
system have been established and shown to be close to those required for
maximum RNA synthesis by purified FPV virions. Products have been characterized
by the peptides they yield on limited proteolysis in SDS and it has been shown
that virus nucleoprotein (NP) and matrix (M) protein are made. The smallest
virus coded polypeptide, the non-structural protein (NS), is made in only small
amounts in the coupled system although it is a major virus coded product of infected
cells early in infection.
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, viral proteins biosynthesis, cell free system, fluorometry, avian
genetics, peptide synthesis, rabbits, reticulocytes metabolism, transcription,
genetic, translation, genetic.
Minor, P.D. and N.J. Dimmock (1975). Inhibition of
synthesis of influenza virus proteins: evidence of two host-cell-dependent
events during multiplication. Virology 67(1): 114-23. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, viral
proteins biosynthesis, virus replication, amanitins pharmacology, camptothecin
pharmacology, cell line, cell nucleus metabolism, dactinomycin pharmacology,
hemagglutinins viral analysis, avian growth and development, avian immunology,
neuraminidase biosynthesis, RNA viral biosynthesis.
Minor, P.D. and N.J. Dimmock (1976). The
multiplication of influenza virus in enucleated BHK cells fused with chicken
erythrocytes. Virology 69(1): 336-8.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cell nucleus metabolism, influenza A virus
avian growth and development, virus replication, antigens, viral analysis, cell
fractionation, cell fusion, cycloheximide pharmacology, dactinomycin
pharmacology, hemagglutinins viral, hybrid cells, neuraminidase biosynthesis,
neuraminidase immunology, ribonucleoproteins biosynthesis, ribonucleoproteins
immunology, viral proteins biosynthesis, viral proteins immunology.
Minor, P.D. and N.J. Dimmock (1977). Selective
inhibition of influenza virus protein synthesis by inhibitors of DNA function.
Virology 78(2): 393-406. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian drug effects, viral
proteins biosynthesis, 4 nitroquinoline 1 oxide pharmacology, camptothecin
pharmacology, cell line, dactinomycin pharmacology, daunorubicin pharmacology,
echinomycin pharmacology, ethidium pharmacology, hemagglutinins viral, avian
growth and development, avian metabolism, neuraminidase biosynthesis, Newcastle
disease virus drug effects, Newcastle disease virus growth and development,
Newcastle disease virus metabolism, nogalamycin pharmacology, plicamycin
pharmacology, proflavine pharmacology, virus replication drug effects.
Mitchell, B.W. and M. Brugh (1982). Comparison of
electrocardiograms of chickens infected with viscerotropic velogenic Newcastle
disease virus and virulent avian influenza virus. American Journal of
Veterinary Research 43(12): 2274-8.
ISSN: 0002-9645.
NAL
Call Number: 41.8 Am3A
Abstract: Electrocardiograms of chickens infected with
viscerotropic velogenic Newcastle disease virus (NDV) or virulent avian
influenza virus (AIV) were characterized and compared. The ECG were monitored
by radiotelemetry and were recorded twice daily before virus infection and
during the course of the infection. Thirteen lead II intervals, segments, and
amplitudes were measured and analyzed. The ECG of NDV-infected chickens were
characterized by lengthened (P less than or equal to 0.05) ST segments and
increased (P less than or equal to 0.05) P amplitudes. The ECG of AIV-infected
chickens were characterized by lengthened (P less than or equal to 0.05) RS
intervals, ST segments, TP intervals, and PR segments and by increased (P less
than or equal to 0.05) P amplitudes. The TP intervals and PR segments of ECG of
AIV-infected chickens were significantly (P less than or equal to 0.05) longer
than those of NDV-infected chickens. The pronounced conduction delays indicated
in the ECG of AIV-infected chickens may have diagnostic importance.
Descriptors: chickens, fowl plague physiopathology, heart
physiopathology, Newcastle disease physiopathology, electrocardiography
veterinary, influenza A virus avian pathogenicity, Newcastle disease virus
pathogenicity, specific pathogen free organisms, virulence.
Mitchell, B.W. and M.L. Perdue (1991). Automated
monitoring system for determining embryo movement and death times following
virus infection. Avian Diseases 35(4): 840-6. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Design and performance information is
presented on an automated embryo-monitoring system for intact eggs. The
computer-based system has been used successfully for several months to
characterize viral pathogenicity in embryonated eggs. Features include
electronic sensing of embryo movement, automatic quantification of the amount
of movement, and automatic recording of the results on electronic media. The
system does not require that eggs be removed from the incubator or that the
incubator be opened during the course of an experiment, as is necessary with
the manual candling technique. It has greatly improved discrimination of viral
pathogenicity effects in fertile eggs because of its sensitivity and reduced
intervals between observations. One important potential application involves
using the system to measure the effects on virulence of mixing closely related
variants of the same strain of virus that differ in pathogenicity, which is the
biological scenario most likely approximating a natural disease outbreak.
Descriptors: chick embryo microbiology, influenza A virus
avian pathogenicity, microcomputers, chick embryo physiology, lethal dose 50,
movement, software.
Molibog, E.V., I. Konstantinov Zibelist, G. Starke,
and L.I.A. Zakstel'skaia (1979). Shtammovaia spetsifichnost'
antineiraminidaznykh antitel serotipa N2 shtammov virusa grippa u
perebolevshikh. [Strain specificity of the antineuraminidase antibodies of
influenza virus serotype N2 strains in convalescents]. Voprosy
Virusologii (6): 631-4. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Antineuraminidase antibody was determined in
the subjects who had suffered influenza during the epidemics of 1970-1975 in
the GDR. As early as 1970 the highest titers of antibody (greater than or equal
to 1:60) were found not only to the prototype A/Hong Kong/1/68 strain but also
to its subsequent drift variants A/England/42/72, A/Port Chalmers/1/73. Some
subjects had antineuraminidase antibody to avian influenza virus.
Descriptors: antibodies, viral analysis, influenza
immunology, influenza A virus human immunology, neuraminidase immunology,
adult, child, child, preschool, convalescence, disease outbreaks epidemiology,
Germany, East, influenza epidemiology, human enzymology, neuraminidase
antagonists and inhibitors.
Molibog, E.V., T.V. Pysina, and A.S. Gorbunova (
1968). Sootnoshenie mezhdu eliuikuiushchei i neiraminidaznoi aktivost'iu
virusov gruppa tipa A cheloveka, mlekopitaiushchikh i ptits. [Relationship
between eluting and neuraminidase activity of human, mammalian and avian
influenza type A viruses]. Voprosy Virusologii 13(5): 623-7.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: neuraminidase analysis, orthomyxoviridae
enzymology, orthomyxoviridae physiology.
Molotkovskii, I.u.G., E.M. Manevich, V.I. Shvets,
M.M. Smirnova, and V.N. Krylova (1983). Issledovanie stroeniia membran
remantadinchuvstvitel'nogo i remantadinustoichivogo virusa grippa s pomoshch'iu
fliuorestsentnykh fosfolipidnykh zondov. [Membrane structure of
remantadine-sensitive and remantadine-resistant influenza virus studied with
fluorescent phospholipid probes]. Voprosy Virusologii (2):
182-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Significant differences in the molecular
organization of lipid bilayer in remantadin-resistant and remantadin-sensitive
strains of influenza virus were demonstrated by means of fluorescent
phospholipid probes, analogues of phosphatidylcholine and sphingomyelin. The
data on fluorescence polarization and transfer of excitation energy from
protein tryptophanes on probe fluorophores showed phosphatidylcholine and
sphingomyelin to be segregated in influenza virion membrane. Gradients of
mobility of lipid chains in virion membrane and in phospholipid vesicles have
opposite directions. The results indicate that M protein coming inside virion
into contact with the lipid bilayer does not penetrate further than its middle.
In virions of the resistant strain remantadin destroys the array of the entire
bilayer whereas in the sensitive strain the addition of remantadin results in a
marked decrease of mobility of the chains in the surface area. It is suggested
that the molecular organization of lipids is one of the factors determining
influenza virus sensitivity to remantadin.
Descriptors: adamantane analogs and derivatives, capsid
analysis, influenza A virus avian ultrastructure, membrane proteins analysis,
rimantadine pharmacology, viral proteins analysis, drug resistance, microbial, energy transfer,
fluorescent dyes analysis, avian drug effects, lipid bilayers analysis,
phosphatidylcholines analysis, spectrometry, fluorescence, sphingomyelins
analysis.
Moore, J.T., L.M. Spence, T.D. Sanders, and A.K.
Adams (1999). Human influenza: viral mutations and altered tropisms. Clinical
Laboratory Science Journal of the American Society for Medical Technology
12(2): 67-9. ISSN: 0894-959X.
NAL
Call Number: RB37.A1C5
Abstract: Influenza is a virus that is capable of
causing a pandemic of the human race. Influenza has the ability to infect
humans by mutating and altering its pathogenic characteristics. Efforts must be
made worldwide to educate people about the possibilities of a potential
outbreak. Awareness of optimal conditions which could lead to viral mutation
and human to human transmission of a neogenetic strain of influenza appears to
be a key deterrent against future cases.
Descriptors: influenza genetics, influenza transmission,
influenza A virus genetics, mutation, adolescent, adult, birds, child,
preschool, disease outbreaks, Hong Kong epidemiology, infant, influenza
physiopathology, influenza virology, influenza A virus avian genetics, middle
aged, species specificity.
Moran, T.M., H. Park, A. Fernandez Sesma, and J.L.
Schulman (1999). Th2 responses to inactivated influenza virus can Be
converted to Th1 responses and facilitate recovery from heterosubtypic virus
infection. Journal of Infectious Diseases 180(3): 579-85. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: Immunization with live influenza virus
expands Th1 memory cells and facilitates more rapid recovery after
heterosubtypic virus challenge. Immunization with inactivated virus generates a
Th2 response and does not lead to heterosubtypic immunity. Creation of a Th1
priming environment by the inclusion of interleukin (IL)-12 with antibodies to
IL-4 converted the response against inactivated virus to a Th1 response that
was able to facilitate virus clearance upon heterosubtypic virus challenge.
Evaluation of memory responses of mice immunized by the various protocols
demonstrated that the type of immunization imprints T cell memory, dictating
the nature of the response to subsequent infection. After live virus challenge,
expansion of Th1 cells seems to facilitate the generation of cytotoxic T
lymphocytes from naive precursors. This latter finding may be the mechanism by
which inactivated virus immunization in a Th1 cytokine context mediates
heterosubtypic immunity.
Descriptors: influenza immunology, influenza A virus avian
physiology, human physiology, influenza vaccine, Th1 cells immunology, Th2
cells immunology, virus latency physiology, cell line, cytokines biosynthesis,
dogs, immunologic memory, avian radiation effects, human radiation effects, mice, inbred BALB
c, spleen immunology, T lymphocytes,
cytotoxic immunology, Th1 cells virology, Th2 cells virology, ultraviolet rays.
Morgan, D.J., C. Kurts, H.T. Kreuwel, K.L. Holst,
W.R. Heath, and L.A. Sherman (1999). Ontogeny of T cell tolerance to
peripherally expressed antigens. Proceedings of the National Academy of
Sciences of the United States of America 96(7): 3854-8. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Transgenic expression of the influenza virus
hemagglutinin (HA) in the pancreatic islet beta cells of InsHA mice leads to
peripheral tolerance of HA-specific T cells. To examine the onset of tolerance,
InsHA mice were immunized with influenza virus A/PR/8 at different ages, and
the presence of nontolerant T cells was determined by the induction of
autoimmune diabetes. The data revealed a neonatal period wherein T cells were
not tolerant and influenza virus infection led to HA-specific beta cell
destruction and autoimmune diabetes. The ability to induce autoimmunity
gradually waned, such that adult mice were profoundly tolerant to viral HA and
were protected from diabetes. Because cross-presentation of islet antigens by
professional antigen-presenting cells had been reported to induce peripheral
tolerance, the temporal relationship between tolerance induction and activation
of HA-specific T cells in the lymph nodes draining the pancreas was examined.
In tolerant adult mice, but not in 1-week-old neonates, activation and
proliferation of HA-specific CD8(+) T cells occurred in the pancreatic lymph
nodes. Thus, lack of tolerance in the perinatal period correlated with lack of
activation of antigen-specific CD8(+) T cells. This work provides evidence for
the developmental regulation of peripheral tolerance induction.
Descriptors: aging immunology, hemagglutinin
glycoproteins, influenza virus immunology, influenza A virus immunology, islets
of langerhans immunology, receptors, antigen, T cell immunology, T lymphocytes
immunology, animals, newborn, diabetes mellitus, type I immunology, diabetes
mellitus, type I pathology, hemagglutinin glycoproteins, influenza virus
genetics, immune tolerance, influenza A virus avian immunology, islets of
langerhans growth and development, islets of langerhans pathology, lymphocyte activation,
mice, mice inbred BALB c, mice, transgenic, receptors, antigen, T cell
genetics.
Moya, P., M.L. Alonso, E. Baixeras, and E. Ronda
(1984). Immunomodulatory activity of isoprinosine on experimental viral
infections in avian models. International Journal of Immunopharmacology
6(4): 339-43. ISSN: 0192-0561.
NAL
Call Number: QR180.I52
Abstract: The immunomodulatory activity of Isoprinosine
treatments have been experimentally verified on chicken infected by three
different viruses: Newcastle disease, fowl plague and avian infectious
bronchitis. In protection tests, positive variations in the mean day of death
rather than in the mortality rate were found depending on the modality of
treatment. A stimulatory influence on primary anti-Newcastle disease virus
antibody response was observed. In the avian model the Isoprinosine antiviral
effect appears as due mainly to the enhancement of interferon production and to
a synergistic interferon-isoprinosine interaction.
Descriptors: adjuvants, immunologic pharmacology, inosine
analogs and derivatives, inosine pranobex pharmacology, virus diseases
immunology, antibodies, viral biosynthesis, chickens, hemagglutination
inhibition tests, infectious bronchitis virus immunology, influenza A virus
avian immunology, interferons therapeutic use, kinetics, Newcastle disease
virus immunology, vesicular stomatitis Indiana virus immunology, virus diseases
drug therapy.
Mucke, K. and C. Scholtissek (1987). Extragenic
and intragenic suppression of a transport mutation in the hemagglutinin gene of
an influenza A virus as revealed by backcross and sequence determination. Virology
158(1): 112-7. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Cooperation of viral proteins, or functional
domains within a protein, can be studied by analyzing temperature-sensitive
(ts) mutants and revertants carrying suppressor mutations. Accordingly, we have
sequenced the hemagglutinin (HA) genes of a ts mutant of fowl plague virus
(FPV), with a transport defect in the HA, and of five independent ts+
revertants (R1, R3, R4, R5, and R9). The amino acid replacement in position 480
from Thr to Ile, leading to the loss of a complex carbohydrate side chain, is
responsible for the ts phenotype. R3, R4, and R5 are true revertants in that
they have Thr in position 480, while R1 and R9 have kept Ile. The sequence of
the HA of R1 is exactly the same as that of the ts mutant, while the R9 HA has
two additional amino acid replacements in positions 91 (Lys-Thr) and 104 (Gly-Val).
By doing a backcross with wild-type virus, it was shown that R1 carries an
extragenic suppressor mutation, while R9 is intragenically suppressed. We
conclude that the HA is transported from the site of its synthesis in the rough
endoplasmic reticulum (RER) to the plasma membrane along with another viral
gene product, which by mutation can complement the ts defect. An alternative
interpretation is that the ts mutation results from a change in HA which allows
an interacting protein to bind HA too soon, holding it back in the RER. The
suppressor mutation may remove this premature interaction.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian genetics, suppression, genetic, base sequence,
biological transport, cultured cells, crosses, genetic, avian immunology, avian
metabolism, mutation, temperature.
Munk, K., E. Pritzer, E. Kretzschmar, B. Gutte, W.
Garten, and H.D. Klenk (1992). Carbohydrate masking of an antigenic epitope
of influenza virus haemagglutinin independent of oligosaccharide size. Glycobiology
2(3): 233-40. ISSN: 0959-6658.
NAL
Call Number: QP552.G59G593
Abstract: Comparison of the haemagglutinins (HA) of the
pathogenic avian influenza viruses A/FPV/Dutch/27 (H7N7) and A/FPV/Rostock/34
(H7N1) revealed 94.7% nucleotide and 93.8% amino acid sequence homologies. Six
of the seven N-glycosidic oligosaccharides of the Rostock HA are at the same
positions as the six carbohydrates of the Dutch strain. The additional
oligosaccharide side chain of the Rostock strain, which is of the complex type,
is attached to asparagine149 in antigenic epitope B. The accessibility of this
antigenic epitope has been analysed by using rabbit antisera raised against
synthetic peptides comprising amino acids 143-162. The carbohydrates of the HA
of the Rostock strain have been modified (i) to truncated cores by expression
in insect cells using a baculovirus vector, (ii) to oligomannosidic side chains
by growth in the presence of the trimming inhibitor methyldeoxynojirimycin and
(iii) to a single N-acetylglucosamine residue by removal of the oligomannosidic
sugar with endo-beta-N-acetylglucosaminidase H. Neither the authentic nor the
modified oligosaccharides allowed antibody binding, as indicated by
enzyme-linked immunosorbent assay (ELISA) and Western blot analyses. Reactivity
was observed, however, after complete removal of the carbohydrate from HA of
the Rostock strain by digestion with peptide-N-glycosidase F. HA of the Dutch
strain was reactive without prior peptide-N-glycosidase F treatment. These
results demonstrate that a single N-acetyl-glucosamine at asparagine149 is
sufficient to prevent recognition of the peptide epitope.
Descriptors: hemagglutinins viral chemistry, influenza A
virus avian chemistry, avian immunology, oligosaccharides chemistry,
oligosaccharides immunology, amino acid sequence, antigens, viral chemistry,
epitopes chemistry, hemagglutinins viral immunology, models, molecular,
molecular conformation, molecular sequence data, sequence homology, nucleic
acid, species specificity.
Murakami, M., T. Towatari, M. Ohuchi, M. Shiota, M.
Akao, Y. Okumura, M.A. Parry, and H. Kido (2001). Mini-plasmin found in the
epithelial cells of bronchioles triggers infection by broad-spectrum influenza
A viruses and Sendai virus. European Journal of Biochemistry FEBS
268(10): 2847-55. ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: Extracellular cleavage of virus envelope
fusion glycoproteins by host cellular proteases is a prerequisite for the
infectivity of mammalian and nonpathogenic avian influenza viruses, and Sendai
virus. Here we report a protease present in the airway that, like tryptase
Clara, can process influenza A virus haemagglutinin and Sendai virus envelope
fusion glycoprotein. This protease was extracted from the membrane fraction of
rat lungs, purified and then identified as a mini-plasmin. Mini-plasmin was
distributed predominantly in the epithelial cells of the upward divisions of
bronchioles and potentiated the replication of broad-spectrum influenza A viruses
and Sendai virus, even that of the plasmin-insensitive influenza A virus
strain. In comparison with plasmin, its increased hydrophobicity, leading to
its higher local concentrations on membranes, and decreased molecular mass may
enable mini-plasmin to gain ready access to the cleavage sites of various
haemagglutinins and fusion glycoproteins after expression of these viral
proteins on the cell surface. These findings suggest that mini-plasmin in the
airway may play a pivotal role in the spread of viruses and their
pathogenicity.
Descriptors: bronchi cytology, epithelial cells chemistry,
infection, influenza A virus metabolism, peptide fragments chemistry, plasmin
chemistry, respirovirus metabolism, amino acid sequence, blotting, western,
bronchi metabolism, bronchi pathology, bronchi virology, cell membrane
metabolism, dose response relationship, drug, electrophoresis, polyacrylamide
gel, immunohistochemistry, isoflurophate pharmacology, lung metabolism, lung
pathology, lung virology, molecular sequence data, rats, rats, wistar, sequence
analysis, protein, sequence homology, amino acid, substrate specificity, viral
envelope proteins chemistry, viral envelope proteins metabolism.
Murakami, Y., K. Nerome, Y. Yoshioka, S. Mizuno, and
A. Oya (1988). Difference in growth behavior of human, swine, equine, and
avian influenza viruses at a high temperature. Archives of Virology
100(3-4): 231-44. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Growth characteristics of a wide range of
influenza A viruses from different mammals and bird species were examined in an
established line of canine kidney (MDCK) cells at an ordinary (37 degrees C)
and a high temperature (42 degrees C). Although all viruses employed in the
present study possessed a capability of replicating at 37 degrees C, virus
growth at 42 degrees C showed considerable variation and reflected differences
in the natural hosts of the isolates. All reference strains and isolates from
bird species grew well in the MDCK cells maintained at 42 degrees C, but human
viruses did not, showing an asymmetrical growth behavior. In contrast to this,
growth of swine and equine viruses showed growth characteristics intermediate
between human and avian viruses. Of the two swine viruses examined, replication
of one strain occurred equally well at both temperatures and another failed to
grow at 42 degrees C. Similarly, two of the three equine viruses tested
belonging to H3N8 antigenic subtypes grew at 42 degrees C. However, the results
obtained from comparison of plaque sizes and growth curves indicated that the
replication of the above swine and equine viruses was restricted under a
stringent temperature when compared to avian viruses. The detailed analysis of
cloned viruses revealed that some of the swine and equine viruses contained two
variants which are readily distinguished by growth behavior at 42 degrees C.
Genome analysis of parental and virus clones by oligonucleotide mapping and
migration profiles of RNA segments did not detect any differences among the above
variants exhibiting the asymmetrical growth characteristics at 42 degrees C.
Descriptors: influenza A virus avian growth and
development, human growth and development, influenza A virus growth and
development, cell line, genes viral, horses, avian genetics, human genetics,
porcine genetics, porcine growth and development, influenza A virus genetics,
plaque assay, RNA viral genetics, temperature.
Murphy, B.R., A.J. Buckler White, W.T. London, J.
Harper, E.L. Tierney, N.T. Miller, L.J. Reck, R.M. Chanock, and V.S. Hinshaw
(1984). Avian-human reassortant influenza A viruses derived by mating avian
and human influenza A viruses. Journal
of Infectious Diseases 150(6): 841-50.
ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: Reassortant influenza A viruses were produced
by mating an avian virus (A/Mallard/NY/78, A/Mallard/Alberta/78, or
A/Pintail/Alberta/79) with a wild-type human influenza A virus. From each
mating a reassortant virus was obtained that contained the genes coding for the
hemagglutinin and neuraminidase surface antigens of the human influenza A
wild-type virus and the six other RNA segments ("internal genes") of
the avian influenza A virus parent. The avian-human reassortant influenza
viruses produced resembled their avian virus parent in that they produced
plaques on MDCK monolayers at 42 C, a temperature restrictive for the human
influenza viruses. In the trachea of squirrel monkeys, each avian-human
reassortant influenza virus was as restricted in its replication as was its
avian influenza virus parent. Thus, one or more of the six internal genes of
each avian parent virus was responsible for restriction of the reassortant
virus in monkeys. The A/Washington/80 X A/Mallard/NY/78 reassortant virus
retained its phenotype of restricted replication in monkeys after five serial
passages in vivo. It also failed to transmit to cagemates or induce resistance
to wild-type virus challenge, and it did not initiate a systemic or enteric
infection. These findings form the basis for evaluation of these attenuated
avian-human reassortant influenza A viruses as live attenuated vaccines for
humans.
Descriptors: crosses, genetic, influenza A virus avian
genetics, human genetics, neuraminidase genetics, chickens, child, ducks,
hemagglutinins viral genetics, immunization, avian physiology, human
physiology, saimiri, virus replication.
Murphy, B.R., A.J. Buckler White, W.T. London, and
M.H. Snyder (1989). Characterization of the M protein and nucleoprotein
genes of an avian influenza A virus which are involved in host range
restriction in monkeys. Vaccine 7(6): 557-61. ISSN: 0264-410X.
NAL
Call Number: QR189.V32
Abstract: A reassortant virus possessing RNA segment 7,
which codes for the M1 and M2 proteins, of the avian influenza A/Mallard/New
York/6750/78 (H2N2) virus and the other seven RNA segments of the human
influenza A/Udorn/307/72 (H3N2) virus had been shown previously to be markedly
restricted in replication in the respiratory tract of squirrel monkeys. In
contrast, a reassortant possessing segment 7 of another avian influenza virus,
A/Pintail/Alberta/119/79 (H4N6), and the seven other RNA segments from the
A/Udorn/72 virus was not restricted. The nucleotide and deduced amino acid
sequence of the RNA segment 7 of each virus was determined to identify the
structural basis for the attenuation phenotype specified by RNA segment 7 of
the A/Mallard/78 virus. Analysis of the deduced amino acid sequences revealed
only two amino acid differences in the M1 protein and one difference in the M2
protein, suggesting that the attenuation phenotype of a reassortant virus
possessing segment 7 of the A/Mallard/78 virus may be specified by one to three
amino acids. Reassortant viruses possessing RNA segment 6, which codes for the
nucleoprotein, of either avian influenza virus and the other seven RNA segments
of a human influenza virus were also restricted in replication in squirrel
monkeys. A comparison of the deduced amino acid sequences of the two avian
nucleopeoteins demonstrated only three amino acid differences indicating that
these two avian viruses possess NP genes that are highly related. The high
degree of relatedness of both the NP and M proteins of these two avian viruses
contrasts with their divergent surface antigens.(ABSTRACT TRUNCATED AT 250
WORDS)
Descriptors: genes viral, influenza A virus avian
genetics, nucleoproteins genetics, viral core proteins, viral matrix proteins
genetics, viral proteins genetics, amino acid sequence, base sequence, human
genetics, RNA viral analysis, saimiri, virus replication.
Murphy, B.R., M.L. Clements, E.L. Tierney, R.E.
Black, J. Stienberg, and R.M. Chanock (1985). Dose response of influenza
A/Washington/897/80 (H3N2) avian-human reassortant virus in adult volunteers.
Journal of Infectious Diseases 152(1): 225-9. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Descriptors: antibodies, viral biosynthesis, influenza A
virus avian immunology, human immunology, influenza vaccine immunology, adult,
dose response relationship, immunologic, influenza microbiology, influenza transmission,
avian genetics, human genetics, recombination, genetic, vaccination, vaccines,
attenuated.
Murphy, B.R., D.L. Sly, E.L. Tierney, N.T. Hosier,
J.G. Massicot, W.T. London, R.M. Chanock, R.G. Webster, and V.S. Hinshaw
(1982). Reassortant virus derived from avian and human influenza A viruses
is attenuated and immunogenic in monkeys. Science 218(4579):
1330-2. ISSN: 0036-8075.
NAL
Call Number: 470 Sci2
Abstract: An influenza A reassortant virus that
contained the hemagglutinin and neuraminidase genes of a virulent human virus,
A/Udorn/72 (H3N2), and the six other influenza A virus genome segments from an
avirulent avian virus, A/Mallard/New York/6750/78 (H2N2), was evaluated for its
level of replication is squirrel monkeys and hamsters. In monkeys, the
reassortant virus was as attenuated and as restricted in its level of
replication in the upper and lower respiratory tract as its avian influenza
virus parent. Nonetheless, infection with the reassortant induced significant
resistant to challenge with virulent human influenza virus. In hamsters, the
reassortant virus replicated to a level intermediate between that of its
parents. These findings suggest that the nonsurface antigen genes of the avian
parental virus are the primary determinants of restriction of replication of
the reassortant virus in monkeys. Attenuation of the reassortant virus for
primates is achieved by inefficient functioning of the avian influenza genes in
primate cells, while antigenic specificity of the human influenza virus is
provided by the neuraminidase and hemagglutinin genes derived from the human
virus. This approach could lead to the development of a live influenza A virus
vaccine that is attenuated for man if the avian influenza genes are similarly
restricted in human cells.
Descriptors: influenza A virus avian genetics, human
genetics, influenza vaccine immunology, antigens, surface genetics, epitopes
genetics, epitopes immunology, hamsters, hemagglutinins genetics,
hemagglutinins immunology, neuraminidase genetics, neuraminidase immunology,
saimiri, vaccines, attenuated immunology.
Naeve, C.W., V.S. Hinshaw, and R.G. Webster (1984). Mutations
in the hemagglutinin receptor-binding site can change the biological properties
of an influenza virus. Journal of Virology 51(2): 567-9.
ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Avian influenza virus reassortants containing
human influenza virus hemagglutinins do not replicate in ducks. Two mutations
in the receptor-binding site of a human hemagglutinin at residues 226 and 228
allowed replication in ducks. The mutations resulted in a receptor-binding-site
sequence identical to the known avian influenza virus sequences.
Descriptors: influenza A virus avian genetics, human
genetics, mutation, receptors, immunologic genetics, base sequence, DNA
replication, ducks, genes viral, avian immunology, human immunology, species
specificity, virus replication.
Naeve, C.W. and R.G. Webster (1983). Sequence of
the hemagglutinin gene from influenza virus A/Seal/Mass/1/80. Virology
129(2): 298-308. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: A double-strand DNA copy of the influenza
virus A/Seal/Mass/1/80 (H7N7) [seal] hemagglutinin (HA) gene was cloned into
the plasmid pAT153/PvuII/8 and sequenced to deduce the primary amino acid
sequence. The gene is 1731 nucleotides long and codes for a protein of 560
amino acids with a nonglycosylated molecular weight of 62098 Da. The deduced
amino acid sequence displays similarities to all other sequenced hemagglutinins
by retaining six of seven potential glycosylation sites, showing conversation
in the number and position of cysteine residues, conservation in the fusion and
anchor peptides, and conservation in the putative receptor site of the
molecule. However, three features of the primary amino acid sequence could be
distinguished from the H7 amino acid sequence of A/fowl plague/Rostock/34
(FPV), another avian H7 influenza virus which does not produce disease in mammals.
First, the seal HA sequence has three fewer amino acids in the connecting
peptide region of the HA than FPV. This lack of multiple basic amino acids in
the connecting peptide is similar to that found in avirulent H7 avian strains
and to mammalian serotypes H1, H2, and H3. Second, the seal HA has gained four
additional proline residues, all in HA1, as compared to FPV. These residues may
alter the tertiary structure of the HA and ultimately contribute to the
biological features of this virus. Third, the seal HA has lost a potential
carbohydrate attachment site at residue 149 which lies at the tip of the HA
structure. The loss of this carbohydrate could alter the seal HAs interaction
with host cell receptors.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus genetics, amino acid sequence, base sequence, chemistry,
DNA, hemagglutinins viral analysis,
influenza A virus avian genetics, influenza A virus immunology, proline
analysis, protein conformation, structure activity relationship.
Naeve, C.W., R.G. Webster, and V.S. Hinshaw (1983). Phenotypic
variation in influenza virus reassortants with identical gene constellations.
Virology 128(2): 331-40. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Abstract: To determine which gene segments of influenza
A viruses are responsible for the property of tissue tropism, reassortants were
produced between the avian influenza strain, A/Mal/NY/6750/78 [H2N2] (Mal/NY),
and a human strain, A/Udorn/307/72 [H3N2] (Udorn). The avian strain replicates
in the intestinal tract of ducks and the human strain does not. Eight
reassortants were shown by hybridization analysis to have the same gene
constellation, having received hemagglutinin gene segment 4 from Udorn and the
remaining seven gene segments from Mal/NY. With one exception, all reassortants
containing the Udorn HA were restricted in their ability to traverse the
digestive tract of ducks and replicate therein. The exception, reassortant R2,
replicated to high titers in the intestinal tract. The R2 virus was shown to
possess a hemagglutinin molecule that was antigenically distinguishable from
the Udorn parent with polyclonal and monoclonal antibodies. The virus was
"nonavid" in reaction with antihemagglutinin antibodies and was phenotypically
similar to avian influenza viruses. The results suggest that the R2
hemagglutinin has undergone mutation(s) altering tissue tropism and antigenic
properties of the virus. These studies illustrate the importance of the
hemagglutinin gene in determining tissue tropism and present an example of
phenotypic variation in a virus population with the same gene constellation but
do not exclude a requirement for other gene products.
Descriptors: ducks microbiology, genes viral, influenza A
virus avian genetics, influenza A virus human genetics, virus replication,
hemagglutinins viral genetics, hemagglutinins viral immunology, influenza A
virus avian immunology, influenza A virus avian physiology, influenza A virus
human immunology, influenza A virus human physiology, intestines microbiology,
nucleic acid hybridization, recombination, genetic.
Naffakh, N., P. Massin, N. Escriou, B. Crescenzo
Chaigne, and S. van der Werf (2000). Genetic analysis of the compatibility
between polymerase proteins from human and avian strains of influenza A
viruses. Journal of General Virology 81(Pt. 5): 1283-91. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: In order to determine how efficiently the
polymerase proteins derived from human and avian influenza A viruses can
interact with each other in the context of a mammalian cell, a genetic system
that allows the in vivo reconstitution of active ribonucleoproteins was used.
The ability to achieve replication of a viral-like reporter RNA in COS-1 cells
was examined with heterospecific mixtures of the core proteins (PB1, PB2, PA
and NP) from two strains of human viruses (A/Puerto Rico/8/34 and
A/Victoria/3/75), two strains of avian viruses (A/Mallard/NY/6750/78 and
A/FPV/-Rostock/34), and a strain of avian origin (A/Hong Kong/156/97) that was
isolated from the first human case of H5N1 influenza in Hong Kong in 1997. In
accordance with published observations on reassortant viruses, PB2 amino acid
627 was identified as a major determinant of the replication efficiency of
heterospecific complexes in COS-1 cells. Moreover, the results showed that
replication of the viral-like reporter RNA was more efficient when PB2 and NP
were both derived from the same avian or human virus or when PB1 was derived
from an avian virus, whatever the origin of the other proteins. Furthermore,
the PB1 and PB2 proteins from the A/Hong- Kong/156/97 virus exhibited
intermediate properties with respect to the corresponding proteins from avian
or human influenza viruses, suggesting that some molecular characteristics of
PB1 and PB2 proteins might at least partially account for the ability of the
A/Hong Kong/156/97 virus to replicate in humans.
Descriptors: influenza A virus avian genetics, influenza A
virus human genetics, nucleoproteins, RNA replicase, viral core proteins
genetics, viral core proteins metabolism, cos cells, chloramphenicol o
acetyltransferase, cloning, molecular, DNA, complementary, DNA directed RNA
polymerases genetics, DNA directed RNA polymerases metabolism, influenza A
virus avian metabolism, influenza A virus human metabolism, molecular sequence
data, plasmids genetics, sequence analysis, DNA, transcription, genetic,
transfection, viral proteins genetics, viral proteins metabolism, virus
replication.
Nakajima, K., E. Nobusawa, and S. Nakajima (1990). Evolution
of the NS genes of the influenza A viruses. II. Characteristics of the amino
acid changes in the NS1 proteins of the influenza A viruses. Virus Genes
4(1): 15-26. ISSN: 0920-8569.
NAL
Call Number: QH434.V57
Abstract: We compared the amino acid sequences of the
NS1 proteins of human, equine, and avian influenza viruses. The ratios of the
amino acid substitutions per nucleotide substitutions in the NS1 proteins were
about 27-45%, suggesting the existence of constraints on the amino acid changes
of the NS1 protein in evolution. As a measure of constraints exerted on the
regions of a protein, a changeability index is proposed. There was a highly
conserved region between amino acid residues 30 and 50. The C-terminal region
of amino acid residue 165 was a continuously changeable region. We have either
introduced several nucleotide substitutions to the NS cDNA of the A/Udorn/72
virus in vitro or constructed the recombinant NS cDNAs between the A/Udorn/72
and A/chick/Japan/24 viruses, and then expressed them in animal cells. We have
found that the amino acid substitutions introduced to the low-conserved region
of the NS1 protein affected the stability and nuclear localization of the NS1
protein. One of the chimeric proteins between the A/Udorn/72 and
A/chick/Japan/24 viruses did not move to the nucleus of the cell and remained
in the cytoplasm.
Descriptors: capsid genetics, evolution, genes viral,
influenza A virus genetics, viral core proteins genetics, amino acid sequence,
base sequence, birds, chimera, cytoplasm ultrastructure, DNA, viral analysis,
fluorescent antibody technique, horses, molecular sequence data, mutation,
structure activity relationship, viral nonstructural proteins.
Nakajima, K., E. Nobusawa, and S. Nakajima (1984). Genetic
relatedness between A/Swine/Iowa/15/30(H1N1) and human influenza viruses. Virology
139(1): 194-8. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The nucleotide sequences of the M and NS1
genes of influenza virus A/Swine/Iowa/15/30 (A/SW/IW/30)(H1N1) were determined
with cloned DNAs and compared with reported sequences of human and avian
influenza viruses. A/SW/IW/30 virus was found to be closely similar to
A/PR/8/34(H1N1) virus in the nucleotide sequences of the M and NS1 genes, the
base differences between the two strains being 64 out of 1027 nucleotides in
the M gene and 52 out of 740 in the NS1 gene. Based on the assumptions that
these two viruses were derived from a common ancestor and that the rate of base
changes per year was the same in man and in swine, it was estimated that the
progenitor virus was in circulation during the period from 1915 to 1920. This
estimation was compatible with the epidemiological findings suggesting that the
progenitor of the swine influenza virus was the agent of the 1918 influenza
pandemic. Furthermore, the M and NS1 gene sequences of A/FPV/Rostock/34(H7N6)
virus were much closer to those of A/SW/IW/30 and A/PR/8/34 viruses than to
A/duck/Alberta/60/76(H12N5) virus, but not as close as the A/SW/IW/30 virus was
to A/PR/8/34 virus.
Descriptors: influenza A virus human genetics, influenza A
virus, porcine genetics, influenza A virus genetics, base sequence, evolution,
genes viral.
Nakajima, K., E. Nobusawa, T. Ogawa, and S. Nakajima
(1990). Evolution of the NS genes of the influenza A viruses. I. The genetic
relatedness of the NS genes of animal influenza viruses. Virus Genes 4(1): 5-13. ISSN: 0920-8569.
NAL
Call Number: QH434.V57
Abstract: We compared the nucleotide sequences of the
NS genes of 13 animal influenza viruses belonging to human, swine, avian, and
equine viruses for the study of the genetic relatedness of the NS genes in
animal influenza viruses. The NS genes of three virus strains
A/chicken/Brescia/02, A/equine/Prague/56, and A/equine/Miami/63 were newly
sequenced. The base sequence homologies between the NS genes of avian, human,
swine, and the A/equine/Miami/63 viruses were 87.8% or higher. On the other
hand, the base sequence of the NS gene of the A/equine/Prague/56 virus differed
widely from those of other viruses analyzed in the present study. We
constructed a model of the genetic tree of the NS genes of avian and equine
influenza viruses by a modified Farris method. For comparison of the NS genes
between human and avian viruses, we estimated the speed of the nucleotide
substitutions of the avian influenza NS genes. It was roughly constant, even
though the substitutions did not occur sequentially. The nucleotide
substitution rate of the NS genes of avian influenza viruses was one-third to
one-fourth that of human influenza viruses. We deduced the time of separation
between the NS genes of human and avian influenza viruses during evolution.
Descriptors: base sequence, capsid genetics, evolution,
genes viral, influenza A virus genetics, sequence homology, nucleic acid, viral
core proteins genetics, DNA, viral analysis, molecular sequence data, viral
nonstructural proteins.
Nakajima, K., E. Nobusawa, T. Ogawa, and S. Nakajima
(1987). Genetic divergence of the NS genes of avian influenza viruses. Virology
158(2): 465-8. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The nucleotide sequences of the NS genes of
avian influenza A viruses, A/Chicken/Japan/24, A/Duck/England/56, A/Tern/South
Africa/61, A/Duck/Ukraine/1/63, and A/Mynah/Haneda-Thai/76, were determined and
compared among themselves and with two reported NS sequences of the avian
viruses, A/FPV/Rostock/34 and A/Duck/Alberta/60/76. Thirty-six to two hundred
forty base differences in the NS genes were found in pairwise comparisons among
the viruses. The numbers of base differences in the NS genes increased with
time, except A/Duck/Alberta/60/76 virus. However, the NS genes of the avian
viruses did not change sequentially with time and were arranged in separate
evolutionary lineages. When the NS genes of avian viruses employed in the
present study were compared with those of human viruses, sequence similarity
was confirmed (M. Baez, R. Taussig, J. J. Zarza, J. F. Young, P. Palese, A.
Reisfield, and A. M. Skalka, 1980, Nucleic Acids Res. 8, 5845-5858). The
numbers of base differences in the NS genes between avian viruses and the
A/PR/8/34 virus were 61 to 83, and the NS gene of the oldest avian isolate,
A/Chicken/Japan/24, was most closely related to that of the A/PR/8/34 virus. It
was hypothesized that NS genes of human influenza viruses and those of some
avian influenza viruses had been derived from a common ancestor gene.
Descriptors: antigens, viral genetics, influenza A virus
immunology, viral proteins genetics, base sequence, influenza A virus genetics,
variation genetics, viral nonstructural proteins.
Naruse, H., C. Scholtissek, and H.D. Klenk (1986). Temperature-sensitive
mutants of fowl plague virus defective in the intracellular transport of the
hemagglutinin. Virus Research 5(2-3): 293-305. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Nine mutants of fowl plague virus with
temperature-sensitive defects in the biosynthesis of the hemagglutinin have been
characterized by analyzing the processing and the intracellular location of
this glycoprotein in MDCK and chick embryo cells. It was found that with all of
these mutants the transport of the hemagglutinin to the cell surface was
impeded at the non-permissive temperature. There were differences, however, in
the site of the block. With mutants tsl, ts227, ts478 and ts658 the precursor
HA was not cleaved and the oligosaccharide side chains remained sensitive to
endoglucosaminidase H. When the hemagglutinin was analyzed in permeabilized
cells by immunofluorescence, usually only cytoplasmic labeling was seen.
Immunofluorescence of non-permeabilized cells and hemadsorption revealed that
the hemagglutinin did not reach the cell surface. In contrast, the hemagglutinin
of mutants ts79, ts482, ts532, ts546 and ts651 was cleaved and oligosaccharides
were processed to the endoglucosaminidase H-resistant form at non-permissive
temperature. In permeabilized cells, the cytoplasm and juxtanuclear regions
typical for the Golgi apparatus were labeled by immunofluorescence. Except for
ts482, ts532 and ts546 which were leaky, hemagglutinin could not be detected at
the cell surface. These observations indicate that, with the first group of
mutants, hemagglutinin transport is usually arrested already in the rough
endoplasmic reticulum, whereas with the second group it is inhibited at a late
stage between the Golgi apparatus and the plasma membrane.
Descriptors: defective viruses genetics, hemagglutinins
viral, influenza A virus avian genetics, mutation, cell line, chick embryo,
defective viruses growth and development, hemagglutination, influenza A virus
avian growth and development, temperature.
Neighbor, N.K., L.A. Newberry, G.R. Bayyari, J.K.
Skeeles, J.N. Beasley, and R.W. McNew (1994). The effect of microaerosolized
hydrogen peroxide on bacterial and viral poultry pathogens. Poultry
Science (USA) 73(10): 1511-1516.
ISSN: 0032-5791.
NAL
Call Number: 47.8 Am33P
Abstract: The effect of microaerosolized H2O2 on
bacterial and viral poultry pathogens was investigated. Bacterial cultures and
viruses were dried on sterile glass Petri dishes and subjected to direct and
indirect 5% (H2O2) microaerosol mist. In the trials using Escherichia coli
and Staphylococcus aureus, there was complete inactivation following
exposure to H2O2. Using Salmonella typhimurium, indirect exposure
resulted in only partial inactivation whereas direct exposure to H2O2 gave
complete inactivation. For the viruses studied, 5% H2O2 microaerosol mist
completely inactivated infectious laryngotracheitis virus. Newcastle disease
virus, infectious bronchitis virus, and avian influenza virus showed reduced
infectivity but were not completely inactivated. Avian reovirus susceptibility
varied with the method of exposure and infectious bursal disease virus was
highly resistant. The use of 10% H2O2 mist, however, resulted in total
inactivation of infectious bursal disease virus. The effect of 10% H2O2 on
equipment and selected materials representative of a hatcher or poultry house
was investigated. A solar cell calculator, a thermostat containing a
microswitch, and samples of uncoated steel, galvanized steel, and uncoated
aluminum were subjected to 10 fumigation cycles. No damage was detected in the
calculator and the thermostat. Both the uncoated steel and the galvanized steel
showed signs of oxidation. The aluminum did not show signs of oxidation.
Descriptors: aerosols, fumigation, hydrogen peroxide, cell
counting, bacteria, pathogens, avian infectious bronchitis virus, avian
laryngotracheitis virus, avian influenza virus, Newcastle disease virus, Salmonella
typhimurium, Staphylococcus aureus, Escherichia coli,
reoviridae, avian infectious bursitis, corrosion, application methods,
bacteria, biological analysis, colloids, coronaviridae, deterioration,
dispersions, enterobacteriaceae, Escherichia, herpetoviridae, infectious
diseases, influenza virus, micrococcaceae, oxides, paramyxoviridae, peroxides,
physical states, Salmonella, Staphylococcus, viroses,
viruses, inactivation, avian reovirus,
infectious bursal disease virus.
Nerome, K., Y. Yoshioka, S. Sakamoto, H. Yasuhara,
and A. Oya (1985). Characterization of a 1980-swine recombinant influenza
virus possessing H1 hemagglutinin and N2 neuraminidase similar to that of the
earliest Hong Kong (H3N2) virus. Archives of Virology 86(3-4):
197-211. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A recombinant (H1N2, formerly Hsw 1N2),
A/swine/Ehime/1/80 was found to possess antigenic, biological and genomic
characteristics different from those of a previous A/swine/Kanagawa/2/78 (H1N2)
strain. Five monoclonal antibodies to A/NJ/8/76 definitely differentiated the
hemagglutinin molecules of the former virus from the latter, showing that these
viruses differed, at least, at two antigenic determinants.
Neuraminidase-inhibition tests with monoclonal antibodies to different H2N2 and
H3N2 viruses revealed that the A/swine/Ehime/1/80 strain contained a
neuraminidase very similar to that of the late human Asian (H2N2) and the earliest
Hong Kong (H3N2) viruses. Growth comparison of swine and human isolates
indicated that A/swine/Ehime/1/80 and A/swine/Shizuoka/1/78 (H1N1) failed to
grow at 42 degrees C, while A/swine/Kanagawa/2/78 and its possible parental
virus, A/swine/Kanagawa/4/78 (H1N1) replicated efficiently at this stringent
temperature. These results revealed that the viruses having growth
characteristics similar to those of avian influenza virus were present in the
swine population. RNA analysis by oligonucleotide mapping suggested that
A/swine/Ehime/1/80 may be a recombinant between A/swine/Shizuoka/1/78-like and
A/Aichi/2/68 (H3N2)-like viruses. To further determine the gene constellation
of this recombinant virus, DNA-RNA hybridization was performed by using DNA
segments complementary for swine (H1N1) virus RNA and the entire RNAs of three
viruses. The molecular hybridization could define the genomic composition of
the recombinant, indicating that only the neuraminidase gene of this virus is
derived from the earliest Hong Kong (H3N2)-like virus and remaining seven genes
from swine (H1N1) virus.
Descriptors: hemagglutinins viral analysis, influenza A
virus human immunology, influenza A virus, porcine immunology, influenza A
virus immunology, neuraminidase analysis, hemagglutination, viral, influenza A
virus human enzymology, influenza A virus, porcine enzymology, influenza A
virus, porcine genetics, nucleic acid hybridization, oligonucleotides analysis,
RNA viral analysis, recombination, genetic, swine, temperature, virus
replication.
Nerome, K., Y. Yoshioka, C.A. Torres, A. Oya, P.
Bachmann, K. Ottis, and R.G. Webster (1984). Persistence of Q strain of H2N2
influenza virus in avian species: antigenic, biological and genetic analysis of
avian and human H2N2 viruses. Archives of Virology 81(3-4):
239-50. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The characteristics of an avian influenza
virus were compared in detail with those of human Asian (H2N2) influenza
viruses. Antigenic analysis by different antisera against H2N2 viruses and
monoclonal antibodies to both the hemagglutinin and neuraminidase antigens
showed that an avian isolate, A/duck/Munchen/9/79 contained hemagglutinin and
neuraminidase subunits closely related to those of the early human H2N2 viruses
which had been prevalent in 1957. However, this avian virus gave low HI titers
with absorbed and non-absorbed antisera to different human H2N2 viruses
isolated in 1957. Like human Q phase variant, such as A/RI/5-/57 (H2N2),
hemagglutination of the above avian strain was not inhibited by the purified
non-specific gamma-inhibitor from guinea pig serum. Growth behavior at
restrictive temperature (42 degrees C) clearly differentiate the avian H2N2
virus from human influenza viruses, showing that the former virus grew well in
MDCK cells at 42 degrees C but not the latters. Genomic analysis of these
viruses revealed that the oligonucleotide map of H2N2 virus isolated from a
duck was quite different from those of human H2N2 viruses from 1957 to 1967.
The oligonucleotide mapping also indicated that different H2N2 influenza virus
variants had co-circulated in humans in 1957.
Descriptors: influenza A virus avian immunology, influenza
A virus human immunology, hemagglutinins viral immunology, influenza A virus
avian genetics, influenza A virus human genetics, influenza A virus growth and
development, neuraminidase immunology, RNA viral genetics.
Nestorowicz, A., Y. Kawaoka, W.J. Bean, and R.G.
Webster (1987). Molecular analysis of the hemagglutinin genes of Australian
H7N7 influenza viruses: role of passerine birds in maintenance or transmission?
Virology 160(2): 411-8. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Abstract: In 1985 a fowl plague-like disease occurred
in chickens in Lockwood, Victoria, Australia and caused high mortality. An H7N7
influenza virus was isolated from the chickens (A/Chicken/Victoria/1/85);
additionally, an antigenically similar virus was isolated from starlings
(A/Starling/Victoria/5156/85) and serological evidence of H7N7 virus infection
was found in sparrows. Antigenic analysis with monoclonal antibodies to H7,
oligonucleotide mapping of total vRNA, and sequence analysis of the HA genes
established that the chicken and starling influenza viruses were closely
related and probably came from the same source. There was high nucleotide
sequence homology (95.3%) between the HA genes of A/Chick/Vic/85 and a fowl
plague-like virus isolated from chickens in Victoria 9 years earlier
[A/Fowl/Vic/76 (H7N7)]. The sequence homologies indicated that the
A/Chick/Vic/85 and A/Fowl/Vic/76 were derived from a common recent ancestor,
while another recent H7N7 virus, Seal/Mass/1/80 originated from a different
evolutionary lineage. Experimental infection of chickens and starlings with
A/Chick/Vic/1/85 (H7N7) was associated with high mortality (100%), transmission
to contact birds of the same species, and virus in all organs. In sparrows
one-third of the birds died after infection and virus was isolated from most
organs; transmission to contact sparrows did not occur. In contrast, the H7N7
virus replicated in ducks and spread to contact ducks but caused no mortality.
These studies establish that the host species plays a role in determining the
virulence of avian influenza viruses, and provide the first evidence for
transmission of virulent influenza viruses between domestic poultry and
passerine birds. They support the hypothesis that potentially virulent H7N7
influenza viruses could be maintained in ducks where they cause no apparent
disease and may sometimes spread to other wild birds and domestic poultry.
Descriptors: birds microbiology, hemagglutinins viral
genetics, influenza A virus avian genetics, amino acid sequence, animals, wild
microbiology, Australia, base sequence, chickens microbiology, disease reservoirs,
genes viral, molecular sequence data, nucleotide mapping, RNA viral genetics,
species specificity, virus replication.
Netesov, S.V., S.I.A. Golovin, I.V. Frolov, T.P.
Mikriukova, and P.F. Safronov (1989). Pervichnaia struktura gena
gemaggliutinina virusa grippa ptits A/FPV/Weybridge. [Primary structure of the
avian influenza virus A/FVP/Weybridge hemagglutinin gene]. Molekuliarnaia
Genetika, Mikrobiologiia i Virusologiia (5): 26-34. ISSN: 0208-0613.
NAL
Call Number: QH506.M65F2
Abstract: The complete primary structure of cDNA for
hemagglutinin gene of influenza virus A/FPV/weybridge/27 subtype H7 has been
determined. Its comparison with the structures of analogous genes from other
strains of the same subtype has shown 75% of base changes resulting in silent
mutations. This suggests the weak immunological pressing in course of evolution
of this subtype strains. The reason for apathogenicity of this avian strain is
supposed to be elimination of a glycosylation site present in the strain A/FPV/Rostock/34.
The possibility of using the obtained data for construction of the new
generation of vaccines is discussed.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian genetics, amino acid sequence, base sequence, molecular
sequence data.
Neumann, G., M. Hatta, and Y. Kawaoka (2003). Reverse
genetics for the control of avian influenza. Avian Diseases
47(Special Issue): 882-887. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Avian influenza viruses are major contributors
to viral disease in poultry as well as humans. Outbreaks of high-pathogenicity
avian influenza viruses cause high mortality in poultry, resulting in
significant economic losses. The potential of avian influenza viruses to
reassort with human strains resulted in global pandemics in 1957 and 1968,
while the introduction of an entirely avian virus into humans claimed several
lives in Hong Kong in 1997. Despite considerable research, the mechanisms that
determine the pathogenic potential of a virus or its ability to cross the
species barrier are poorly understood. Reverse genetics methods, i.e., methods
that allow the generation of an influenza virus entirely from cloned cDNAs,
have provided us with one means to address these issues. In addition, reverse
genetics is an excellent tool for vaccine production and development. This
technology should increase our preparedness for future influenza virus
outbreaks.
Descriptors: epidemiology, infection, molecular genetics,
avian influenza, genetics, infectious disease, prevention and control,
respiratory system disease, viral disease, disease control, economic losses,
global pandemics, reverse genetics, viral outbreaks, viral pathogenicity.
Neumann, G., T. Watanabe, H. Ito, S. Watanabe, H.
Goto, P. Gao, M. Hughes, D.R. Perez, R. Donis, E. Hoffmann, G. Hobom, and Y.
Kawaoka (1999). Generation of influenza A viruses entirely from cloned
cDNAs. Proceedings of the National Academy of Sciences of the United
States of America 96(16): 9345-50.
ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: We describe a new reverse-genetics system
that allows one to efficiently generate influenza A viruses entirely from
cloned cDNAs. Human embryonic kidney cells (293T) were transfected with eight
plasmids, each encoding a viral RNA of the A/WSN/33 (H1N1) or A/PR/8/34 (H1N1)
virus, flanked by the human RNA polymerase I promoter and the mouse RNA
polymerase I terminator-together with plasmids encoding viral nucleoprotein and
the PB2, PB1, and PA viral polymerases. This strategy yielded >1 x 10(3)
plaque-forming units (pfu) of virus per ml of supernatant at 48 hr
posttransfection. The addition of plasmids expressing all of the remaining
viral structural proteins led to a substantial increase in virus production, 3
x 10(4)-5 x 10(7) pfu/ml. We also used reverse genetics to generate a
reassortant virus containing the PB1 gene of the A/PR/8/34 virus, with all
other genes representing A/WSN/33. Additional viruses produced by this method
had mutations in the PA gene or possessed a foreign epitope in the head of the
neuraminidase protein. This efficient system, which does not require helper
virus infection, should be useful in viral mutagenesis studies and in the
production of vaccines and gene therapy vectors.
Descriptors: DNA, complementary, DNA, viral genetics,
influenza A virus genetics, RNA viral genetics, cell line, chick embryo, dogs,
hn protein genetics, influenza A virus avian genetics, influenza A virus human
genetics, influenza A virus physiology, kidney, mice, plasmids, RNA polymerase
I metabolism, reverse transcriptase polymerase chain reaction, transfection,
viral structural proteins genetics, virus replication.
Neykova, N., D. Simov, G. Galunska, E. Velichkova,
A.S. Galabov, and A. Karparov (1981). Benzoxazolone-5-sulphonanilides,
1-(benzoxazolone-5'-sulphonyl)-benzotriazoles and
4-hydroxy-3,2'-diaminobenzenesulphonanilides with antiviral activity. Arzneimittel
Forschung 31(5): 747-52. ISSN:
0004-4172.
NAL
Call Number: RS1.A7
Abstract: benzoxazolone-5-(2'-nitro)-sulphonanilides
were synthesized by acylation of o-nitroanilines with
benzoxazolone-5-sulphochloride or 3-methylbenzoxazolone-5-sulphochloride. The
nitro group in these compounds was subjected to reduction and the resulting
amino derivatives were cyclysed to yield the corresponding
1-(benzoxazolone-5'-sulphonyl)-benzotriazoles. Decyclization of the oxazolone
cycle of benzoxazolone-5-(2'-amino)-sulphonanilides resulted in
4-hydroxy-3,2'-diaminobenzenesulphonanilides. In vitro testing of the antiviral
activity of the compounds obtained during successive synthetic steps revealed
that some of them exhibited marked antiviral effect against toga, orthomixo,
oncorna and herpes viruses.
Descriptors: antiviral agents chemical synthesis,
benzoxazoles chemical synthesis, sulfanilamides chemical synthesis, antiviral
agents pharmacology, benzoxazoles pharmacology, chemistry, cytopathogenic
effect, viral drug effects, herpesvirus 1, suid drug effects, influenza A virus
avian drug effects, mice, mice inbred BALB c, moloney murine leukemia virus
drug effects, Semliki Forest virus drug effects, sulfanilamides pharmacology,
triazoles chemical synthesis, triazoles pharmacology.
Nichol, S.T., C.R. Penn, and B.W. Mahy (1981). Evidence
for the involvement of influenza A (fowl plague Rostock) virus protein P2 in
ApG and mRNA primed in vitro RNA synthesis. Journal of General Virology
57(Pt. 2): 407-13. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Eleven temperature-sensitive (ts) mutants of
influenza A (fowl plague, Rostock) virus were analysed for in vitro RNA
transcriptase activity in reactions primed by ApG or globin mRNA at 31 degrees
C or at 40.5 degrees C, the restrictive temperature for ts mutant growth. Only
those ts mutants studied which were defective in RNA segment 1, coding for the
virion P2 protein, were defective in RNA transcriptase activity when compared
to wild-type virus. Mutants having a defect in the P2 protein had no
significant RNA transcriptase activity in reactions at 40.5 degrees C primed by
globin mRNA. However, one mutant showed RNA transcriptase activity similar to
wild-type virus at 40.5 degrees C when ApG (0.3 mM) was used as primer. The
results suggest that influenza (fowl plague, Rostock) P2 protein is directly
involved in the mRNA priming reaction, as well as in the RNA transcription
reaction in vitro.
Descriptors: dinucleoside phosphates, influenza A virus
avian metabolism, RNA nucleotidyltransferases metabolism, RNA replicase
metabolism, RNA viral biosynthesis, viral proteins physiology, adenosine
monophosphate analogs and derivatives, adenosine monophosphate physiology,
globins, guanosine analogs and derivatives, guanosine physiology, influenza A
virus avian genetics, mutation, RNA, messenger physiology, transcription,
genetic.
Nicolau, C., H.D. Klenk, A. Reimann, K. Hildenbrand,
and H. Bauer (1978). Molecular events during the interaction of envelopes of
myxo- and RNA-tumor viruses with cell membranes. A 270 MHz H nuclear magnetic
resonance study. Biochimica Et Biophysica Acta 511(1): 83-92. ISSN: 0006-3002.
NAL
Call Number: 381 B522
Descriptors: cell membrane physiology, cell
transformation, viral, influenza A virus avian, influenza A virus, Newcastle
disease virus, sarcoma viruses, avian, cell membrane ultrastructure, chick
embryo, fibroblasts physiology, magnetic
resonance spectroscopy.
Niemann, H., J. Dabrowski, U. Dabrowski, R. Geyer, W.
Keil, H.D. Klenk, and S. Stirm (1985). The major oligosaccharides in the
large subunit of the hemagglutinin from fowl plague virus, strain Dutch.
Structure elucidation by one-dimensional and two-dimensional 1H nuclear
magnetic resonance and by methylation analysis. European Journal of
Biochemistry FEBS 146(3): 523-32.
ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: The N-glycosidically linked glycans in the
large subunit (HA1) of the hemagglutinin from fowl plague virus, strain Dutch
(containing about 15%, w/w, of carbohydrates), were liberated by alkaline
hydrolysis, and were filtrated through Bio-Gel as the re-N-acetylated
oligosaccharide alditols. One major fraction (90%, mol/mol) was obtained. It
was subfractionated by concanavalin A affinity chromatography and was analyzed
by methylation/capillary gas chromatography/mass fragmentography and especially
by one-dimensional and two-dimensional 1H nuclear magnetic resonance. The major
HA1 glycans, which are not sialylated, were thus found to comprise about 40%,
30% and 20% (mol/mol), respectively, of biantennary intersected, biantennary,
and triantennary N-acetyllactosaminic ('complex') oligosaccharides. About two
thirds of the internal GlcNAc residues in these glycans are substituted by
Fuc(alpha 1----6), all the triantennary species carry the third Gal(beta
1----4)GlcNAc(beta 1----unit at the Man(alpha 1----6)-branch, and roughly one
fourth of the N-acetyllactosamine units in the non-intersected biantennary
oligosaccharides are incomplete.
Descriptors: hemagglutinins viral, influenza A virus avian
analysis, oligosaccharides analysis, amino acids analysis, chemistry,
hemagglutination tests, hemagglutinin glycoproteins, influenza virus,
hexosamines analysis, magnetic resonance spectroscopy methods, mass
fragmentography, methylation, polysaccharides analysis.
O'Neill, R.E., R. Jaskunas, G. Blobel, P. Palese, and
J. Moroianu (1995). Nuclear import of influenza virus RNA can be mediated by
viral nucleoprotein and transport factors required for protein import. Journal
of Biological Chemistry 270(39): 22701-4.
ISSN: 0021-9258.
NAL
Call Number: 381 J824
Abstract: We have fluorescently labeled one of the
eight genomic segments of influenza virus RNA and a recombinant influenza viral
protein, the nucleoprotein (NP), to investigate the requirement for their
uptake into nuclei of digitonin-permeabilized cells. We found that the influenza
viral NP behaves like a nuclear localization sequence (NLS) containing protein.
Thus, at 0 degrees C it docks at the nuclear envelope only in the presence of
the heterodimeric karyopherin (either karyopherin alpha 1 beta or karyopherin
alpha 2 beta), and docking is competitively inhibited by an unlabeled NLS
containing substrate. Like other NLS-containing proteins, at 20 degrees C NP is
imported into the nucleus after further addition of the GTPase Ran and of p10.
In contrast, the fluorescently labeled, 890-nucleotide-long viral RNA segment
does not dock to the nuclear envelope or enter the nucleus either in the
presence of exogenous cytosol or of karyopherin heterodimer, Ran, and p10.
However, in the presence of NP the RNA is able to dock and enter the nucleus
with transport requirements indistinguishable from those for docking and entry
of NP. These data indicate that uptake of the influenza virus RNA segment is
not via a signal in the RNA but via an NLS of a viral protein such as NP.
Descriptors: cell nucleus metabolism, influenza A virus
avian physiology, nuclear proteins metabolism, RNA viral metabolism, binding,
competitive, cell nucleus virology, digitonin, kinetics, liver virology,
macromolecular systems, nuclear envelope metabolism, rats, rats, inbred buf.
Obrosova Serova, N.P., N.L. Pushkarskaia, S.V.
Lavrov, and A.I. Kuznetsov (1976). Deistvie proizvodnykh adamantana na
reproduktsiiu virusa grippa A v kul'ture tkani i na zhivotnykh [Effect of
adamantan derivatives on reproduction of influenza A virus in tissue culture
and in animals]. Voprosy Virusologii (6): 689-92. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: amantadine analogs and derivatives, antiviral
agents, influenza prevention and control, influenza A virus avian drug effects,
amantadine pharmacology, amantadine therapeutic use, mice, virus replication
drug effects.
Ogawa, T. and M. Ueda (1981). Genes involved in
the virulence of an avian influenza virus. Virology 113(1):
304-13. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus genetics,
brain, chick embryo, chickens, electrophoresis, genotype, influenza A virus
growth and development, influenza A virus pathogenicity, RNA viral genetics,
recombination, genetic.
Ohuchi, M., A. Cramer, M. Vey, R. Ohuchi, W. Garten,
and H.D. Klenk (1994). Rescue of vector-expressed fowl plague virus
hemagglutinin in biologically active form by acidotropic agents and coexpressed
M2 protein. Journal of Virology 68(2): 920-6. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The hemagglutinin of the Rostock strain of
fowl plague virus was expressed in CV-1 cells by a simian virus 40 vector, and
its stability in the exocytotic transport process was examined by a fusion
assay. A 50-fold increase in the fusion activity of the hemagglutinin was
observed when expression occurred in the presence of ammonium chloride,
Tris-HCl, or high doses of amantadine. When chloroquine, another acidotropic
agent, was used, the hemagglutinin exposed at the cell surface had to be
activated by trypsin, because intracellular cleavage was inhibited by this
compound. Hemagglutinin mutants resistant to intracellular cleavage did not
require acidotropic agents for full expression of fusion activity, when treated
with trypsin after arrival at the cell surface. These results indicate that
fowl plague virus hemagglutinin expressed by a simian virus 40 vector is
denatured in the acidic milieu of the exocytotic pathway and that cleavage is a
major factor responsible for the pH instability. Coexpression with the M2
protein also markedly enhanced the fusion activity of the hemagglutinin, and
this effect was inhibited by low doses of amantadine. These results support the
concept that M2, known to have ion channel function, protects the hemagglutinin
from denaturation by raising the pH in the exocytotic transport system. The
data also stress the importance of acidotropic agents or coexpressed M2 for the
structural and functional integrity of vector-expressed hemagglutinin.
Descriptors: hemagglutinins viral biosynthesis, influenza
A virus avian metabolism, viral matrix proteins pharmacology, ammonium chloride
pharmacology, base sequence, biological transport, cell fusion drug effects,
cultured cells, Cercopithecus aethiops, fluorescent antibody technique,
hemagglutinin glycoproteins, influenza virus, hemagglutinins viral genetics,
hemagglutinins viral isolation and purification, hydrogen-ion concentration,
influenza A virus avian genetics, membrane proteins biosynthesis, molecular
sequence data, recombinant proteins biosynthesis, simian virus 40 genetics,
viral fusion proteins biosynthesis, viral fusion proteins genetics, viral
matrix proteins biosynthesis, viral matrix proteins genetics.
Ohuchi, M., A. Feldmann, R. Ohuchi, and H.D. Klenk
(1995). Neuraminidase is essential for fowl plague virus hemagglutinin to
show hemagglutinating activity. Virology 212(1): 77-83. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: When hemagglutinin (HA) of fowl plague virus
(FPV) was expressed in CV-1 cells by a simian virus 40 vector, hemadsorption
was barely detectable, although HA was exposed at the cell surface. However, treatment
of HA-expressing cells with Vibrio cholerae neuraminidase (VCNA)
resulted in extensive hemadsorption. VCNA treatment enhanced the
electrophoretic mobility of the HA1 subunit of HA, indicating the removal of
sialic acid. When two oligosaccharides in the vicinity of the receptor binding
site of FPV HA were deleted by site-specific mutagenesis, VCNA treatment was
not required for hemadsorption. Mutants which retained one of these
oligosaccharides and mutants in which oligosaccharides not adjacent to the
receptor binding site were deleted needed VCNA treatment to show hemadsorption.
VCNA treatment also enhanced hemadsorption of vector-expressed HA of the WSN
strain, which had a complex-type oligosaccharide in the vicinity of the
receptor binding site, but had no effect on hemadsorption of Hong Kong type HA,
which has a high-mannose type oligosaccharide adjacent to the receptor binding
site. These results indicate that sialic acid on oligosaccharides near the
receptor binding site interferes with hemadsorption. Thus, the neuraminidase is
essential for FPV HA to show hemagglutinating activity.
Descriptors: hemagglutination, hemagglutinins viral
metabolism, influenza A virus avian immunology, neuraminidase pharmacology,
glucosaminidase, glycosylation, hemagglutinins viral chemistry,
N-acetylneuraminic acid, sialic acids chemistry.
Ohuchi, M., C. Fischer, R. Ohuchi, A. Herwig, and
H.D. Klenk (1998). Elongation of the cytoplasmic tail interferes with the
fusion activity of influenza virus hemagglutinin. Journal of Virology
72(5): 3554-9. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The hemagglutinin (HA) of fowl plague virus
was lengthened and shortened by site-specific mutagenesis at the cytoplasmic
tail, and the effects of these modifications on HA functions were analyzed
after expression from a simian virus 40 vector. Elongation of the tail by the
addition of one to six histidine (His) residues did not interfere with
intracellular transport, glycosylation, proteolytic cleavage, acylation, cell surface
expression, and hemadsorption. However, the ability to induce syncytia at a low
pH decreased dramatically depending on the number of His residues added.
Partial fusion (hemifusion), assayed by fluorescence transfer from
octadecylrhodamine-labeled erythrocyte membranes, was also reduced, but even
with the mutant carrying six His residues, significant transfer was observed.
However, when the formation of fusion pores was examined with hydrophilic
fluorescent calcein, transfer from erythrocytes to HA-expressing cells was not
observed with the mutant carrying six histidine residues. The addition of
different amino acids to the cytoplasmic tail of HA caused an inhibitory effect
similar to that caused by the addition of His. On the other hand, a mutant lacking
the cytoplasmic tail was still able to fuse at a reduced level. These results
demonstrate that elongation of the cytoplasmic tail interferes with the
formation and enlargement of fusion pores. Thus, the length of the cytoplasmic
tail plays a critical role in the fusion process.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, histidine metabolism, influenza A virus avian metabolism, membrane
fusion physiology, amino acids, biological transport, cell line, cell membrane
metabolism, Cercopithecus aethiops, cytoplasm metabolism, hemagglutinin
glycoproteins, influenza virus chemistry, hemagglutinin glycoproteins,
influenza virus genetics, histidine genetics, influenza A virus avian genetics,
intracellular fluid, mutagenesis.
Ohuchi, M., R. Ohuchi, A. Feldmann, and H.D. Klenk
(1997). Regulation of receptor binding affinity of influenza virus
hemagglutinin by its carbohydrate moiety. Journal of Virology
71(11): 8377-84. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The hemagglutinin (HA) of the fowl plague
virus (FPV) strain of influenza A virus has two N-linked oligosaccharides
attached to Asn123 and Asn149 in the vicinity of the receptor binding site. The
effect of these carbohydrate side chains on the binding of HA to neuraminic
acid-containing receptors has been analyzed. When the oligosaccharides were
deleted by site-specific mutagenesis, HA expressed from a simian virus 40
vector showed enhanced hemadsorbing activity. Binding was so strong under these
conditions that erythrocytes were no longer released by viral neuraminidase and
that release was significantly reduced when neuraminidase from Vibrio cholerae
was used. Similarly, when these oligosaccharides were removed selectively from
purified viruses by N-glycosidase F, such virions were unable to elute from
receptors, although they retained neuraminidase activity. Thus, release of FPV
from cell receptors depends on the presence of the HA glycans at Asn123 and
Asn149. On the other hand, receptor binding was abolished when these
oligosaccharides were sialylated after expression in the absence of
neuraminidase (M. Ohuchi, A. Feldmann, R. Ohuchi, and H.-D. Klenk, Virology
212:77-83, 1995). These observations indicate that the receptor affinity of FPV
HA is controlled by oligosaccharides adjacent to the receptor binding site.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, influenza A virus avian metabolism, neuraminidase chemistry,
receptors, virus metabolism, binding sites, cell line, cultured cells, dogs,
erythrocytes virology, glycosylation, hemagglutinin glycoproteins, influenza
virus metabolism, neuraminidase metabolism, structure activity relationship,
virion metabolism.
Ohuchi, M., M. Orlich, R. Ohuchi, B.E. Simpson, W.
Garten, H.D. Klenk, and R. Rott (1989). Mutations at the cleavage site of
the hemagglutinin after the pathogenicity of influenza virus A/chick/Penn/83
(H5N2). Virology 168(2): 274-80.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Six variants that form plaques in chick
embryo cells in the absence of trypsin have been isolated from the apathogenic
avian influenza virus A/chick/Pennsylvania/1/83 (H5N2). Unlike the wild-type,
the plaque variants contain a hemagglutinin that is cleaved in chick embryo
cells and MDCK cells. The variants differ also from the wild-type in their
pathogenicity for chickens. Nucleotide sequence and oligosaccharide analysis of
the hemagglutinin have revealed that, unlike natural isolates with increased
pathogenicity (Y. Kawaoka et al., 1984, Virology 139, 303-316; Y. Kawaoka and
R. G. Webster, 1985, Virology 146, 130-137), the variants obtained in vitro
have retained an oligosaccharide at asparagine 11 that is believed to interfere
with the cleavage site of the wild-type. However, all variants showed mutations
in the hemagglutinin resulting in an increased number of basic groups at the
cleavage site. These observations demonstrate that masking of the cleavage site
by an oligosaccharide is overcome by an enhancement of the basic charge at the
cleavage site.
Descriptors: hemagglutinins viral genetics, influenza A virus
avian pathogenicity, amino acid sequence, base sequence, cultured cells, chick
embryo, chickens, fowl plague microbiology, genes viral, hemagglutinins viral
analysis, influenza A virus avian genetics, influenza A virus avian growth and
development, molecular sequence data, mutation, oligosaccharides analysis,
plaque assay, trypsin pharmacology.
Ohuchi, R., M. Ohuchi, W. Garten, and H.D. Klenk
(1991). Human influenza virus hemagglutinin with high sensitivity to
proteolytic activation. Journal of Virology 65(7): 3530-7. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: To examine the prerequisites for cleavage
activation of the hemagglutinin of human influenza viruses, a cDNA clone
obtained from strain A/Port Chalmers/1/73 (serotype H3) was subjected to
site-directed mutagenesis and expressed in CV-1 cells by using a simian virus
40 vector. The number of basic residues at the cleavage site, which consists of
a single arginine with wild-type hemagglutinin, was increased by inserting two,
three, or four additional arginines. Like wild-type hemagglutinin, mutants with
up to three additional arginines were not cleaved in CV-1 cells, but insertion
of four arginines resulted in activation. When the oligosaccharide at
asparagine 22 of the HA1 subunit of the hemagglutinin was removed by
site-directed mutagenesis of the respective glycosylation site, only three
inserted arginines were required to obtain cleavage. Mutants containing a
series of four basic residues were also generated by substituting arginine for
uncharged amino acids immediately preceding the cleavage site. The observation
that these mutants were not cleaved, even when the carbohydrate at asparagine
22 of HA1 was absent, underscores the fact that the basic peptide had to be
generated by insertion to obtain cleavage. The data show that the hemagglutinin
of a human influenza virus can acquire high cleavability, a property known to
be an important determinant for the pathogenicity of avian influenza viruses.
Factors important for cleavability are the number of basic residues at the
cleavage site, the oligosaccharide at asparagine 22, and the length of the
carboxy terminus of HA1.
Descriptors: hemagglutinins viral metabolism, influenza A
virus human metabolism, amino acid sequence, arginine chemistry, base sequence,
cloning, molecular, DNA mutational analysis, endopeptidases metabolism,
glycoproteins metabolism, hemagglutinins viral chemistry, hemagglutinins viral
genetics, molecular sequence data, oligonucleotides chemistry, protein
processing, post translational, structure activity relationship.
Okazaki, K., Y. Kawaoka, and R.G. Webster (1989). Evolutionary
pathways of the PA genes of influenza A viruses. Virology 172(2):
601-8. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Nucleotide sequences of the PA genes of
influenza A viruses, isolated from a variety of host species, were analyzed to
determine the evolutionary pathways of these genes and the host specificity of
the genes. Results of maximum parsimony analysis of the nucleotide sequences
indicate at least five lineages for the PA genes. Those from human strains
represent a single lineage, whereas the avian genes appear to have evolved as
two lineages--one comprising genes from many kinds of birds (e.g., chickens,
turkeys, shorebirds, and ducks) and the other comprising only genes from gulls.
H3N2 swine influenza virus PA genes are closely related to the currently
circulating duck virus PA gene. By contrast, the H1N1 swine and equine virus PA
genes appear to have evolved along independent lineages. Comparison of
predicted amino acid sequences disclosed 10 amino acid substitutions in the PA
proteins of all avian and H3N2 swine viruses that distinguished them from human
viruses. The H1N1 swine viruses seem to be chimeras between human and avian
viruses and they contain 8 amino acids not shared by other viruses. The equine
viruses also appear to show their own amino acid substitutions. These findings
indicate that the PA genes of influenza A viruses have evolved in different
pathways defined by apparently unique amino acid substitutions and host
specificities. They also indicate that influenza A viruses have been
transmitted from avian to mammalian species.
Descriptors: genes viral, influenza A virus genetics, RNA
replicase, RNA viral genetics, viral proteins genetics, amino acid sequence,
base sequence, birds, cloning, molecular, ducks, evolution, horses, influenza A
virus avian genetics, influenza A virus human genetics, influenza A virus,
porcine genetics, molecular sequence
data, poultry, sequence homology, nucleic acid, species specificity, swine.
Olofsson, S., U. Kumlin, K. Dimock, and N. Arnberg
(2005). Avian influenza and sialic acid receptors: more than meets the eye?
Lancet Infectious Diseases 5(3): 184-8.
ISSN: 1473-3099.
Abstract: Given our recent discoveries that the ocular
human pathogens adenovirus serotype 37 and enterovirus serotype 70 use sialic
acid linked to galactose via alpha2,3 glycosidic bonds as a cellular receptor,
we propose that the presence of this receptor in the eye also explains the
ocular tropism exhibited by zoonotic avian influenza A viruses such as subtype
H5N1 in Hong Kong in 1997, H7N7 in the Netherlands in 2003, H7N2 in the USA in
2003, and H7N3 in Canada in 2004. We also draw attention to the implications
this hypothesis may have for epizootic and zoonotic influenza, and the
initiation of future pandemics.
Descriptors: Adenoviridae classification, eye diseases
virology, avian influenza pathology, cell surface physiology receptors,
zoonoses virology, Adenoviridae pathology, birds, avian influenza epidemiology,
avian influenza transmission, serotyping, zoonoses transmission, sialic acid.
Orlich, M., D. Khatchikian, A. Teigler, and R. Rott
(1990). Structural variation occurring in the hemagglutinin of influenza
virus A/turkey/Oregon/71 during adaptation to different cell types. Virology
176(2): 531-8. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The influenza virus A/turkey/Oregon/71 (H7N3)
has been adapted to grow in MDCK or chicken embryo cells (CEC) in the absence
of trypsin. Changes occurred in the biological properties of the virus variants
selected, depending on the cell type used for adaptation. They coincided with
enhanced hemagglutinin (HA) activation by intracellular proteolytic cleavage.
In the case of MDCK cell selected variants growth, plaque formation, and HA
cleavability were restricted to this cell type, whereas the CEC-derived
variants displayed altered activities in a broad range of host cells. Unlike
the wild-type virus and its MDCK cell-derived variants, CEC variants had
acquired pathogenic properties for chickens. By nucleotide sequence analysis of
the HA genes of the MDCK cell variants several point mutations were found,
which were localized predominantly at the distal, globular part of the HA
molecule. The mechanism by which these point mutations increased HA
cleavability has not been defined. In the CEC-derived variants besides point
mutations, an insertion of 54 nucleotides adjacent to the cleavage site was
observed, which corresponds in its sequence to a region in the 28 S ribosomal
RNA. This insertion is probably responsible for the altered cleavability of the
CEC variants' HA, leading to increased growth potential and pathogenicity.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, RNA viral genetics, adaptation, physiological, amino acid
sequence, base sequence, cell line, DNA, viral genetics, electrophoresis,
polyacrylamide gel, glycosylation, hemagglutinins viral metabolism, influenza A
virus avian growth and development, influenza A virus avian metabolism,
molecular sequence data, mutation, plaque assay.
Osidze, N.G. (1977). Attenuation of avian
influenza virus A/fowl/SSSR/315/70. Sbornik Nauchnykh Trudov, Moskovskaya
Veterinarnaya Akademiya 93: 60-61.
Descriptors: avian influenza virus, cell culture,
attenuation, fowl.
Otsuki, K., Y. Kawaoka, T. Nakamura, and M. Tsubokura
(1982). Pathogenicity for chickens of avian influenza viruses isolated from
whistling swans and a black-tailed gull in Japan. Avian Diseases
26(2): 314-20. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: We isolated 24 Hav1 Neq1 and 18 Hav6 Nav3
influenza viruses from such free-living wild waterfowl as whistling swans,
black-tailed gulls, and tufted ducks in western Japan in 1980. Two Hav1 Neq1
viruses isolated from a whistling swan and a black-tailed gull and a Hav6 Nav3
virus from a whistling swan were examined for their pathogenicity for chickens.
Five-week-old specific-pathogen-free chickens were inoculated with the viruses
intratracheally or intraperitoneally. Virus was recovered successfully from all
the organs, including the brain, despite the absence of signs of disease. The
intracerebral pathogenicity index scores obtained for the Hav1 Neq1 viruses
were 0.43 and 0.87; the score for the Hav6 Nav3 virus was 0.43. No virus
produced plaques in cultivated chick embryo fibroblast cells in the absence of
trypsin.
Descriptors: animal population groups microbiology,
animals, wild microbiology, birds microbiology, chickens microbiology, ducks
microbiology, influenza A virus avian pathogenicity, chick embryo, Japan,
specific pathogen free organisms, terminology.
Ozaki, H., E.A. Govorkova, C. Li, X. Xiong, R.G.
Webster, and R.J. Webby (2004). Generation of high-yielding influenza A
viruses in African green monkey kidney (Vero) cells by reverse genetics. Journal
of Virology 78(4): 1851-7. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Influenza A viruses are the cause of annual
epidemics of human disease with occasional outbreaks of pandemic proportions.
The zoonotic nature of the disease and the vast viral reservoirs in the aquatic
birds of the world mean that influenza will not easily be eradicated and that
vaccines will continue to be needed. Recent technological advances in reverse
genetics methods and limitations of the conventional production of vaccines by
using eggs have led to a push to develop cell-based strategies to produce
influenza vaccine. Although cell-based systems are being developed, barriers
remain that need to be overcome if the potential of these systems is to be
fully realized. These barriers include, but are not limited to, potentially
poor reproducibility of viral rescue with reverse genetics systems and poor
growth kinetics and yields. In this study we present a modified A/Puerto
Rico/8/34 (PR8) influenza virus master strain that has improved viral rescue
and growth properties in the African green monkey kidney cell line, Vero. The
improved properties were mediated by the substitution of the PR8 NS gene for
that of a Vero-adapted reassortant virus. The Vero growth kinetics of viruses
with H1N1, H3N2, H6N1, and H9N2 hemagglutinin and neuraminidase combinations
rescued on the new master strain were significantly enhanced in comparison to
those of viruses with the same combinations rescued on the standard PR8 master
strain. These improvements pave the way for the reproducible generation of
high-yielding human and animal influenza vaccines by reverse genetics methods.
Such a means of production has particular relevance to epidemic and pandemic
use.
Descriptors: influenza A virus avian growth and
development, influenza A virus human growth and development, influenza vaccine,
reassortant viruses growth and development, vero cells virology, Cercopithecus
aethiops, influenza A virus avian genetics, influenza A virus human
genetics, reassortant viruses genetics, viral nonstructural proteins genetics,
virus cultivation, virus replication.
Padilla, N.R., F.E. Aburto, C.M. Fraire, and N.L.
Padilla (2004). Influenza aviar: histopatologia y deteccion viral por rt-pcr
en tejidos fijados con formalina e incluidos en parafina. [Avian influenza:
histopathology and viral detection in formalin-fixed, paraffin-embedded tissues
by RT-PCR]. Veterinaria Mexico 35(1): 1-19. ISSN: 0301-5092.
NAL
Call Number: SF604.V485
Descriptors: infection, acute renal tubular necrosis,
avian influenza, non suppurative encephalitis, vasculitis, reverse
transcription polymerase chain reaction, clinical techniques, diagnostic
techniques, viral replication, chickens.
Paffenholz, V. and C. Scholtissek (1973). Mode of
replication and temperature characteristics of the RNA polymerase of an influenza
virus in vitro. Zeitschrift Fur Naturforschung. Teil C Biochemie,
Biophysik, Biologie, Virologie 28(3): 208-13. ISSN: 0341-0471.
NAL
Call Number: QH301.Z4
Descriptors: influenza A virus avian enzymology, DNA
directed RNA polymerases biosynthesis, temperature, templates, genetic,
virulence.
Pagnini, P., A. Bonaduce, F. Martone, and M.
Compagnucci (1969). Profilassi della pseudo-peste aviaria. Ricerche con
vaccino inattivato in adiuvante oleoso. [Prevention of avian pseudo-plague.
Research with inactivated vaccine in oily adjuvant]. Acta Medica
Veterinaria 15(5): 267-311. ISSN:
0001-6136.
NAL
Call Number: 41.8 AC84
Descriptors: fowl plague prevention and control, viral
vaccines, influenza A virus avian, vaccination.
Pancheva, S. (1983). Efekt na antibiotika A 23187
vurkhu reproduktsiia na niakoi virusi v kletuchni kulturi. [Effect of
antibiotic A-23187 on the reproduction of viruses in cell cultures]. Acta
Microbiologica Bulgarica 13: 29-32.
ISSN: 0204-8809.
NAL
Call Number: QR1.A37
Descriptors: calcimycin pharmacology, virus replication
drug effects, viruses drug effects, chick embryo, dose response relationship,
drug, herpesvirus 1, suid drug effects, influenza A virus avian drug effects,
Newcastle disease virus drug effects, vaccinia virus drug effects, virus
cultivation, viruses growth and development.
Park, C.H., K. Matsuda, Y. Sunden, A. Ninomiya, A.
Takada, H. Ito, T. Kimura, K. Ochiai, H. Kida, and T. Umemura (2003). Persistence
of viral RNA segments in the central nervous system of mice after recovery from
acute influenza A virus infection. Veterinary Microbiology 97(3-4):
259-68. ISSN: 0378-1135.
NAL
Call Number: SF601.V44
Abstract: One-hundred thirty-seven BALB/c mice were
intranasally inoculated with neurotropic avian influenza A virus (H5N3).
Thirty-nine of these mice died within 16 days post-inoculation (PID) and 98 of
the mice recovered from the infection. To investigate whether viral antigens
and genomes persist in the central nervous system (CNS) of recovered mice, immunohistochemistry
and reverse transcription-polymerase chain reaction (RT-PCR) methods were
performed. Histopathologically, mild interstitial pneumonia and non-suppurative
encephalomyelitis restricted to the basal part of the frontal lobe of the cerebrum,
brain stem and thoracic spinal cord were observed in BALB/c mice until 40 PID.
Small amounts of viral antigens were detected in the brain and spinal cord and
some viral RNA segments (NA, NP, M, PA, HA, NS, PB1) were intermittently
detected in the CNS until 48 PID. Immunosuppression of these mice by
dexamethazone (DEX) treatment did not increase the frequency of detection of
the lesions, viral antigens or genomes. These findings suggest that viral
genomes of neurovirulent influenza virus persist with restricted transcriptive
activity in the CNS of the mice even after clinical recovery from the
infection.
Descriptors: central nervous system virology, fowl plague
virology, influenza A virus avian isolation and purification, RNA viral
analysis, brain pathology, brain virology, central nervous system pathology,
disease models, animal, fowl plague mortality, fowl plague pathology,
immunohistochemistry veterinary, influenza A virus avian genetics, mice, mice
inbred BALB c, random allocation, reverse transcriptase polymerase chain
reaction veterinary, specific pathogen free organisms.
Penn, C. (1989). The role of RNA segment 1 in an
in vitro host restriction occurring in an avian influenza virus mutant. Virus
Research 12(4): 349-59. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: A temperature sensitive mutant, ts C47,
derived from A/FPV/Rostock/34 and with a ts mutation in RNA segment 8, fails to
form plaques in MDCK cells. From data obtained with reassortant viruses using
the human influenza isolate A/FM/1/47 it was apparent that more than one
mutation contributed to the temperature-sensitive (ts) and host range (hr)
phenotypes of ts C47, and the phenotype of reassortants containing RNA segment
1 from A/FM/1/47 indicated that this segment was involved. A single nucleotide
substitution at nucleotide 1961, resulting in valine instead of methionine in
the predicted amino acid sequence of polypeptide PB2, was found in RNA segment
1 of ts C47, but this mutation did not segregate with the attenuated phenotype
on gene reassortment. The following conclusions are drawn: (a) that ts C47 has
at least two mutations in addition to that already known to exist in RNA
segment 8, one of which (that in RNA segment 1) does not contribute to the
observed ts hr phenotypes and (b) that the hr phenotype can be suppressed by
substitution of RNA segment 1 by that of another strain.
Descriptors: influenza A virus avian genetics, RNA viral
physiology, amino acid sequence, base sequence, cultured cells, chick embryo,
dogs, influenza A virus avian growth and development, influenza A virus human
genetics, kidney, phenotype, plaque assay, RNA viral genetics, recombination,
genetic, temperature.
Penn, C.R., D. Blaas, E. Kuechler, and B.W. Mahy
(1982). Identification of the cap-binding protein of two strains of
influenza A/FPV. Journal of General Virology 62(Pt. 1): 177-80. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: We have identified the cap-recognizing
protein of two strains of influenza A fowl plague virus (FPV) by photoaffinity
labelling of virion proteins with a photoreactive analogue of the 5'-methyl cap
structure of messenger RNA. The cap-recognizing protein of influenza
A/FPV/Rostock/34 is the P2 polypeptide, and that of influenza A/FPV/Dutch/27
(Dobson) is the P3 polypeptide. In each case the cap-recognizing protein is the
product of RNA segment 1.
Descriptors: carrier proteins analysis, influenza A virus
avian analysis, viral proteins analysis, affinity labels, carrier proteins
genetics, influenza A virus avian genetics, RNA cap binding proteins, RNA viral
genetics, viral proteins genetics.
Perdue, M.L. (1992). Naturally occurring NS gene
variants in an avian influenza virus isolate. Virus Research 23(3):
223-40. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The A/Turkey/Wisconsin/68 (H5N9) isolate of
avian influenza (AI) consists of two virus populations which have different NS
genes and differ in their biological responses in chicken embryos. They were
classified as being either rapidly embryo-lethal (REL) or slowly embryo-lethal
(SEL), (Avian Dis., 33 (1989) 695-706). In this study, sequence analysis
identified only two nucleotide differences between the two NS genes, creating
single amino acid differences in both the NS1 and the NS2 protein. The
difference in the NS1 protein appears to be neutral, while the differences in
the NS2 places a phenylalanine at position 48. This amino acid has not been
previously demonstrated at this position in an NS2 sequence and its presence
results in a distinct hydrophobic shift in the region. The sequence specifying
the phenylalanine also creates an EcoRI site in the cDNA of the REL NS gene.
Analysis of several clones showed that this site appears to co-segregate with
the REL characteristic. Molecular differences between the two NS gene variants
were reflected by differences in the kinetics of early protein synthesis in
infected cells. In particular, the NS2 protein is in higher concentration
(relative to the NS1) in SEL-infected cells than in REL-infected cells. No
differences were detectable, however, in the rates of viral replication, either
in cell culture or in embryos. Also, the REL or SEL rate was established early
during infection of the embryo and could not be competed out by the other
variant population 3 h after inoculation. Thus, these two natural NS gene
variants appear to specify early differences which influence the time of death
of an infected embryo but the differences do not appear to influence virus
replication.
Descriptors: capsid genetics, influenza A virus avian
genetics, viral core proteins genetics, amino acid sequence, base sequence,
capsid metabolism, chick embryo, cloning, molecular, DNA restriction enzymes,
embryo, nonmammalian microbiology, gene expression regulation, viral, genetic
vectors, influenza A virus avian classification, influenza A virus avian
pathogenicity, molecular sequence data,
polymerase chain reaction, RNA viral isolation and purification,
sequence homology, nucleic acid, variation genetics genetics, viral core
proteins metabolism, viral nonstructural proteins, virus replication.
Perdue, M.L., M. Garcia, J. Beck, M. Brugh, and D.E.
Swayne (1996). An Arg-Lys insertion at the hemagglutinin cleavage site of an
H5N2 avian influenza isolate. Virus Genes 12(1): 77-84. ISSN: 0920-8569.
NAL
Call Number: QH434.V57
Abstract: Recent isolations of H5N2 subtype avian
influenza (AI) viruses in North America have raised questions concerning their
origin, transmission to commercial poultry, and potential for virulence. One
ratite-origin isolate of low pathogenicity, A/emu/TX/39924/93 (H5N2), was
subjected to a procedure that rapidly selects and/or amplifies highly
pathogenic (HP) strains. The resulting highly virulent derivative had an
altered hemagglutinin (HA) gene containing an additional six nucleotides at
position 970-975 in the HA1 coding region. This resulted in an arg-lys
insertion near the proteolytic cleavage site of the HA protein. The remainder
of the HA sequence differed by an additional seven amino acids from the parent.
The HA precursor of the derivative, but not the parent, was readily cleaved
during replication in cell culture without addition of trypsin. In
experimentally infected chickens, the derivative produced lesions typical of highly
pathogenic avian influenza. A reverse transcriptase-polymerase chain reaction
(RT-PCR) primer set was designed to amplify exclusively from molecules with the
inserted six nucleotides. The set yielded product only from the selected
derivative samples and not the parent. Thus, the levels of the HP variants in
the parent stock were undetectable, or the insertion occurred rapidly during
the selection process.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian genetics, arginine, base sequence, chickens,
fowl plague genetics, fowl plague virology, lysine, molecular sequence data,
mutation, phylogeny, polymerase chain reaction, RNA viral genetics.
Perdue, M.L., M. Garcia, J. Crawford, and J. Latimer
(1996). Heterogeneity in the hemagglutinin protein among the H5N2 avian
influenza isolates from central Mexico. Proceedings of the Western
Poultry Diseases Conference 45: 8-13.
NAL
Call Number: SF995.W4
Descriptors: avian influenza virus, Mexico, America,
influenza virus, Latin America, North America, orthomyxoviridae, viruses.
Perdue, M.L., M. Garcia, D. Senne, and M. Fraire
(1997). Virulence-associated sequence duplication at the hemagglutinin
cleavage site of avian influenza viruses. Virus Research 49(2):
173-86. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Recent highly pathogenic (HP) field isolates
of avian influenza (AI) virus from Mexico all possess an insertion of at least
two basic amino acids (arg-lys) at the cleavage site of the hemagglutinin (HA)
glycoprotein. One HP isolate has additional information which yields a 4 amino
acid insert (arg-lys-arg-lys). We present here the nucleotide sequence of the
HA gene of this unique isolate and compare it to recent H5N2 and other avian
influenza isolates. The complete HA nucleotide sequence of the isolate and
phylogenetic relationship suggest that it was derived in direct succession from
a non-pathogenic strain isolated about 1 month earlier. The unique insertion
sequence is a direct duplication of part of the purine-rich region preceding
the arginine codon at the HA cleavage site. This evidence along with other data
in this report provide compelling support for a proposed model explaining the
mechanism of spontaneous, virulence-related insertions in type A influenza
viruses.
Descriptors: hemagglutinins chemistry, hemagglutinins
genetics, influenza A virus avian genetics, influenza A virus avian
pathogenicity, repetitive sequences, nucleic acid, amino acid sequence, base
sequence, chick embryo, chickens, endopeptidases, fowl plague virology,
hydrolysis, influenza A virus avian chemistry, models, molecular, molecular
sequence data, nucleic acid conformation, protein structure, secondary,
sequence alignment, structure activity relationship, virulence.
Perdue, M.L., J. Latimer, C. Greene, and P. Holt
(1994). Consistent occurrence of hemagglutinin variants among avian
influenza virus isolates of the H7 subtype. Virus Research 34(1):
15-29. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Several field isolates of avian influenza
virus of the H7 subtype were analyzed for the presence of hemagglutinin
variants by labeling proteins in cells infected with virus clones, and reacting
with monoclonal antibodies. Each strain was shown to contain two distinct
electrophoretic variants of the uncleaved hemagglutinin. In the A/Tk/Ore/71
(H7N3) isolate, two variants remained in the population through 35 laboratory
passages, indicating both are stable and may be important to expression of the
viral phenotype. Nucleotide sequence analysis of the HA gene of these two variants
demonstrated differences at several amino acid positions in the HA1 subunit
including one glycosylation site. Three additional recent North American
isolates were also each found to contain two electrophoretic variants occurring
within populations as few as one embryo passage away from the original clinical
specimen. Pulse-chase assays indicated none of the variant HA molecules were
cleavable in chick embryo fibroblasts. In the highly pathogenic Australian
isolate; A/Ck/Victoria/75, both HA variants are cleavable in fibroblasts,
without added trypsin, and the differences are localized within the HA1 region.
With all the strains tested, the slower migrating HA variant was associated
with a consistently higher hemagglutinin titer in embryos. Finally, recent H7
isolates from imported birds (A/Soft Bill/Ill/92) also exhibit similar
variants, indicating their occurrence is not limited to domestic poultry. This
consistent presence of two distinct electrophoretic variants in several avian
H7 isolates suggests multiple allelic forms of the H7 hemagglutinin.
Descriptors: antigenic variation genetics, hemagglutinins
viral genetics, influenza A virus avian genetics, antibodies, monoclonal
immunology, antibodies, viral immunology, chick embryo, chickens virology, electrophoresis,
polyacrylamide gel, genes, structural, viral, glycosylation, hemagglutinin
glycoproteins, influenza virus, hemagglutinins viral immunology, influenza A
virus avian classification, influenza A virus avian immunology, mice, mice
inbred BALB c, protein processing, post translational, RNA viral genetics,
sequence analysis, RNA.
Perdue, M.L., J.W. Latimer, and J.M. Crawford (1995).
A novel carbohydrate addition site on the hemagglutinin protein of a highly
pathogenic H7 subtype avian influenza virus. Virology 213(1):
276-281. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The highly pathogenic (HP) avian influenza
isolate, A/Fowl/Victoria/76 (H7N7), contains two naturally occurring
hemagglutinin (HA) variants. The two hemagglutinin proteins differ only in the
possession of a potential asparagine-linked glycosylation site at amino acid
position 188-190, which is near the proposed receptor binding region of the HA.
Expanded virus plaques which possess the addition site exhibit more slowly
migrating HA, subunits and are significantly more lethal in chickens than those
which lack the site. When artificial mixtures of the two variants were
inoculated in birds, as few as 1 in 1000 particles containing the glycosylation
site was sufficient to exhibit 100% lethality in birds. The data raise the
possibility that presence of carbohydrate near the receptor site on the H7
avian influenza virus hemagglutinin may influence virulence.
Descriptors: chickens, avian influenza virus, agglutinins,
chemical composition, pathogenicity, mortality, biological properties, birds,
domestic animals, domesticated birds, Galliformes, influenza virus, livestock,
microbial properties, orthomyxoviridae, poultry, proteins, useful animals,
viruses, glycosylation site, GENBANK z47199, molecular sequence data, viral hemagglutinins, binding site, amino
acid sequences, virulence.
Perdue, M.L. and D.L. Suarez (2000). Structural
features of the avian influenza virus hemagglutinin that influence virulence.
Veterinary Microbiology 74(1-2): 77-86.
ISSN: 0378-1135.
NAL
Call Number: SF601.V44
Abstract: Analysis of the structure of the avian
influenza (AI) virus hemagglutinin (HA) gene and protein has yielded a wealth
of information on the virulence mechanisms of influenza viruses. The AI
hemagglutinin appears to be unique in its capacity to accept basic amino acids
at its proteolytic cleavage site (PCS). The association of multiple basic (MB)
amino acids, HA cleavage, tissue spread and virulence by AI strains first proposed
in the late 1970s and early 1980s [Klenk, H.D., Rott, R., Orlich, M., 1977. J.
Gen. Virol. 36, 151-161; Bosch, F.X., Garten, W., Klenk, H.D., Rott, R., 1981.
Virology 113, 725-735] has held fast for two decades now. While other
structural characteristics and other genes can certainly influence virulence,
the presence of MB amino acids at the PCS has provided a hallmark structural
feature which justifies continuing sequence analysis of emerging field isolates
of AI strains. In addition to this structural feature, the distal tip of the HA
is prone to appearance and disappearance of glycosylation sites, some of which
have been associated with virulence.The recent outbreaks of highly pathogenic
AI in Mexico, Australia, Pakistan, Hong Kong and in the ongoing outbreak of
moderately pathogenic H7 avian influenza in the northeast US have all provided
new and useful information regarding the role of HA RNA and protein structure
in both virulence and host adaptation. We have previously noted that stable RNA
secondary structure near the PCS is related to the acquisition of virulence and
have proposed that the secondary structure may promote the insertion of basic
amino acids. In this report we evaluate the phylogenetic relationships for
three recent isolates of highly pathogenic avian influenza viruses and the
possible virulence factors associated with their primary and secondary
structure.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, influenza A virus avian pathogenicity, glycosylation, hemagglutinin
glycoproteins, influenza virus genetics, influenza A virus avian
classification, numerical analysis, computer assisted, peptide library,
phylogeny, protein structure, secondary, structure activity relationship.
Perdue, M.L., P. Wainright, S. Palmieri, and M. Brugh
(1989). In ovo competition between distinct virus populations in an avian
influenza isolate. Avian Diseases 33(4): 695-706. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Embryo lethality patterns induced by an avian
influenza virus isolate (A/Tk/Ws/68/H5N9) suggested that it contained more than
one genetic form. Two different virus populations were recovered from the
isolate by plaque isolation and limit-dilution cloning and were characterized
with respect to their biological and molecular properties. They were very
closely related but exhibited strikingly different mean death times (MDT) in
10-day-old chick embryos. One was rapidly embryo lethal (REL), while the other
was slowly embryo lethal (SEL). The REL isolate demonstrated a small but
measurable mortality rate in 4-week-old chicks, as did the parental isolate.
The SEL isolate, however, was nonlethal to 4-week-old chicks. The embryo MDT
induced by the parental isolate revealed a biphasic death pattern reflecting
expression of both REL and SEL populations. Mixing experiments, using different
amounts of the two cloned populations, demonstrated that expression of their
unique phenotypic property (either REL or SEL) was competitive. The number of
early or late embryo deaths was directly related to the input levels of each
respective virus. The only molecular difference thus far detected between the
two populations is in the nonstructural (NS) gene, with the REL clone
possessing a faster migrating electrophoretic form of that RNA than the SEL
clone. Both forms of the NS gene were present in the original parental isolate.
This study thus demonstrates the competitive coexistence of two closely related
virus populations within a single natural isolate.
Descriptors: orthomyxoviridae growth and development, RNA
viral analysis, viral proteins analysis, chick embryo, clone cells, influenza
etiology, influenza mortality, influenza veterinary, orthomyxoviridae isolation
and purification, orthomyxoviridae pathogenicity, phenotype, plaque assay,
virulence.
Perdue, M.L., P.O. Wainright, and M. Brugh (1990). Effects
of chicken embryo age on time to death following infection by avian influenza
viruses: implications for distinguishing highly pathogenic isolates. Virus
Research 16(2): 137-52. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: When white leghorn (WL) chick embryos ranging
in age from 8 to 13 days were inoculated with a variety of avian influenza
virus (AIV) isolates, strain-specific differences in embryo mean death times
(MDT) were observed. Non-highly pathogenic (nHP) strains killed 8 or 9 day-old
embryos much more rapidly than 12 or 13 day-old embryos. Highly pathogenic (HP)
strains, however, were less sensitive to embryo age resulting in similar MDTs
in both older and younger embryos. These observations were consistent over a
broad range of virus doses for both HP and nHP strains. When a HP derivative of
H5N2 AIV was compared to its nHP parent, the derivative killed older embryos
more rapidly than the parent virus, while MDTs in younger embryos were the same
for both parent and derivative. The two strains further exhibited clear
differences in the structure of their respective hemagglutinin, a previously
described pathogenicity determinant for this virus. Thus it may be possible to
readily demonstrate the HP phenotype in AIV strains based on MDT measurements
in WL embryos.
Descriptors: chick embryo microbiology, orthomyxoviridae
pathogenicity, orthomyxoviridae infections veterinary, poultry diseases
mortality, antibodies, monoclonal immunology, hemagglutinin glycoproteins,
influenza virus, hemagglutinins viral immunology, orthomyxoviridae infections
mortality, specific pathogen free organisms, time factors, viral envelope
proteins immunology.
Pereira, H.G., A. Rinaldi, and L. Nardelli (1967). Antigenic
variation among avian influenza A viruses. Bulletin of the World Health
Organization 37(4): 553-8. ISSN:
0042-9686.
NAL
Call Number: 449.9 W892B
Descriptors: orthomyxoviridae classification, antigens,
complement fixation tests, Italy, poultry, serotyping.
Petri, T. and N.J. Dimmock (1981). Phosphorylation
of influenza virus nucleoprotein in vivo. Journal of General Virology
57(Pt. 1): 185-90. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Two-dimensional analysis of polypeptides from
A/FPV/Rostock/34 (FP/R)-infected chick embryos fibroblast cells using
non-equilibrium pH gradient gel electrophoresis followed by polyacrylamide gel
electrophoresis, showed that nucleoprotein (NP) was the only detectable virus
phosphoprotein and was present in both the nucleus and cytoplasm. The kinetics
of accumulation of phosphorylated NP in the nucleus and cytoplasm were similar,
suggesting that the presence or absence of phosphate groups did not control the
entry of NP into the nucleus. In the course of this study, two-dimensional
analysis of [35S]methionine-labelled FP/R-infected cells revealed some major
differences from previously published work which are discussed.
Descriptors: cell nucleus metabolism, cytoplasm
metabolism, influenza A virus avian metabolism, nucleoproteins metabolism,
viral proteins metabolism, cultured cells, chick embryo, fibroblasts,
nucleoproteins analysis, phosphoproteins analysis, phosphoproteins metabolism,
phosphorylation, viral proteins analysis.
Petri, T., S. Patterson, and N.J. Dimmock (1982). Polymorphism
of the NS1 proteins of type A influenza virus. Journal of General
Virology 61(Pt. 2): 217-31. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The type-specific non-structural protein 1
(NS1) of influenza A viruses was found to be heterogeneous with respect to
charge, varying in pI by more than two orders of magnitude, and to
phosphorylation. Phosphorylation was strain-specific, variable in extent
between strains, and in some strains NS1 proteins were not detectably
phosphorylated. Phosphorylation was not responsible for the major variations in
charge as, paradoxically, the most acidic NS1 proteins were not phosphorylated.
Cytoplasmic inclusions, which are formed between NS1 proteins and cellular RNA
in infections with a number of human strains, were absent from
A/FP/Rostock-infected cells and do not, therefore, appear to be essential in
virus multiplication. We suggest that the acidic nature of the NS1 of
A/FP/Rostock may prevent it from binding RNA and hence from forming inclusions.
The variation in charge of NS1 proteins which we determined experimentally
correlates with the overall differences in charge adduced from published amino
acid sequence and implications of this variability to the biological role of
NS1 are discussed.
Descriptors: influenza A virus avian analysis, influenza A
virus human analysis, influenza A virus analysis, viral proteins analysis, cell
line, chick embryo, dogs, electrophoresis, polyacrylamide gel, inclusion
bodies, viral analysis, influenza A virus growth and development, isoelectric
point, phosphoproteins analysis, phosphorylation, species specificity, viral
matrix proteins, viral nonstructural proteins, viral proteins metabolism.
Petrov, N.A., L.V. Mamaev, and S.I.A. Golovin (1988).
Pervichnaia struktura gena belka PB2 virusa grippa A/FPV Veibridzh. [Primary
structure of the gene encoding the PB2 protein in influenza virus A/FPB
Weybridge]. Bioorganicheskaia Khimiia 14(4): 548-50. ISSN: 0132-3423.
NAL
Call Number: QD415.A1S62
Abstract: The complete nucleotide sequence of the
cloned full-length DNA copy of the avian influenza virus A/FPV Weybridge PB2
gene has been determined.
Descriptors: genes viral, influenza A virus avian genetics,
viral proteins genetics, amino acid sequence, base sequence, molecular sequence
data.
Philpott, M., B.C. Easterday, and V.S. Hinshaw (
1989). Neutralizing epitopes of the H5 hemagglutinin from a virulent avian
influenza virus and their relationship to pathogenicity. Journal of
Virology 63(8): 3453-8. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: To define and characterize the major
neutralizing epitopes of the H5 hemagglutinin, a panel of monoclonal antibodies
specific for the H5 hemagglutinin of the virulent avian influenza virus
A/Turkey/Ontario/7732/66 (H5N9) was prepared. Antibodies which neutralized
infectivity of the virus were used to select a panel of escape mutants.
Reactivity patterns of the panel of monoclonal antibodies against the panel of
mutants by both enzyme-linked immunosorbent assay serology and hemagglutination
inhibition operationally defined five distinct epitopes on the H5 molecule. The
mutants were analyzed in vivo for virulence in chickens, and the findings indicate
that viruses with mutations in four of five epitopes were no less virulent than
the wild type, producing a rapidly fatal disease, while all viruses with
mutations in the fifth epitope (group 1 mutants) were attenuated. These group 1
mutants were unaltered in the cleavage properties of the hemagglutinin,
suggesting that the mechanism of attenuation is unrelated to processing of the
hemagglutinin. One of the group 1 mutants, 77B1v, was characterized for its
ability to produce necrosis of the spleen and was found to produce none of the
lesions in the spleen which are characteristic of the wild-type virus, although
virus was present in this organ. The results suggest an altered tissue tropism,
perhaps sparing a population of cells critical to an effective immune response.
Descriptors: epitopes analysis, hemagglutinins viral
immunology, influenza A virus avian immunology, antibody specificity, chickens,
cross reactions, enzyme linked immunosorbent assay, epitopes genetics, epitopes
immunology, fowl plague microbiology, hemagglutination inhibition tests,
hemagglutination tests, influenza A virus avian genetics, influenza A virus
avian pathogenicity, mutation, neutralization tests, virulence.
Philpott, M., C. Hioe, M. Sheerar, and V.S. Hinshaw
(1990). Hemagglutinin mutations related to attenuation and altered cell
tropism of a virulent avian influenza A virus. Journal of Virology
64(6): 2941-7. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The H5 hemagglutinin (HA) of a highly
virulent avian influenza virus, A/Turkey Ontario/7732/66 (H5N9), was previously
shown to have five neutralizing epitopes, and escape mutants within one epitope
(group 1) were markedly attenuated (M. Philpott, B. C. Easterday, and V. S.
Hinshaw, J. Virol. 63:3453-3458, 1989). To define the genetic changes related
to these antigenic and biologic properties, the HA genes of mutants within each
of the epitope groups were sequenced by using the polymerase chain reaction.
The mutations in the attenuated group 1 mutants were located near the distal
tip of the HA molecule in close proximity to the receptor-binding site, on the
basis of alignment with the three-dimensional structure of the H3 HA. All group
1 mutations involved charged amino acids. The group 1 mutants, similar to the
wild-type virus, spread systemically and were recovered from the spleens of
infected chickens but, unlike the wild-type virus, failed to produce severe
necrosis in the spleens. Viral replication in the spleens was investigated by
in situ hybridization of spleen sections from chickens infected with the
wild-type or attenuated mutants. Wild-type virus replication was demonstrated
in large, mononuclear, macrophagelike cells; however, group 1 mutant virus was
detected attached only to erythrocytes within the red pulp. These results
suggest that the attenuated mutants differ in their cell tropism within the
spleen.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, mutation, amino acid sequence, base sequence, chick
embryo, chickens, cloning, molecular, DNA, viral genetics, influenza A virus
avian pathogenicity, influenza A virus avian physiology, molecular sequence
data, spleen microbiology, virulence genetics, virus replication.
Philpott, M.S., B.C. Easterday, and V.S. Hinshaw
(1989). Antigenic and phenotypic variants of a virulent avian influenza
virus selected during replication in ducks. Journal of Wildlife Diseases
25(4): 507-13. ISSN: 0090-3558.
NAL
Call Number: 41.9 W64B
Abstract: To evaluate the replication of a highly
virulent avian influenza A virus in a potential reservoir host, mallard ducks (Anas
platyrhynchos) were inoculated with the virulent strain A/Ty/Ont/7732/66
(H5N9). Viruses recovered from the ducks were analyzed by hemagglutination
inhibition (HI) and enzyme-linked immunosorbent assay (ELISA) and found to
possess antigenically altered viral hemagglutinins. Plaque formation on the
Madin-Darby Canine Kidney (MDCK) cell line and on primary chicken embryo cells
was investigated, and isolates recovered from the ducks differed from the wild
type by being unable to form plaques on MDCK cells without trypsin. This
phenotype did not appear to be due to inefficient cleavage of the hemagglutinin
by host cell proteases since hemagglutinin immunoprecipitated from cell lysates
was cleaved. Although the plaquing phenotype suggested attenuation of the
isolates from the ducks, they were not significantly altered in their virulence
for chickens shown by infectivity studies in vivo. These results indicate that
replication of influenza A/Ty/Ont/7732/66 virus in ducks can produce antigenic
and phenotypic variants which are still highly virulent for domestic poultry.
Descriptors: ducks microbiology, fowl plague microbiology,
influenza A virus avian pathogenicity, antibodies, monoclonal immunology,
antigenic variation, cell line, chickens, enzyme linked immunosorbent assay,
fowl plague mortality, hemagglutination inhibition tests, hemagglutinins viral
analysis, hemagglutinins viral metabolism, influenza A virus avian growth and
development, influenza A virus avian immunology, influenza A virus avian
physiology, phenotype, plaque assay, virulence, virus replication.
Pint, L.H. and R.A. Lamb (2004). Viral ion
channels as models for ion transport and targets for antiviral drug action.
FEBS Letters 560(1-3): 1-2. ISSN:
0014-5793.
NAL
Call Number: QD415.F4
Descriptors: influenza infection, solid state NMR,
laboratory techniques, antiviral drug action targets, immune system, membranes,
immune surveillance, ion transport models, proton transfer reaction model,
viral life cycle.
Podcherniaeva, R.I.A., V.K. Blinova, N.D. L'vov, N.L.
Pusharskaia, and G.A. Galegov (1980). Peredacha rezistentnosti k remantadinu
v rezul'tate posledovatel'-nykh rekombinatsii virusov grippa cheloveka i
zhivotnykh. [Transmission of remantadine resistance as a result of successive
recombinations of human and animal influenza viruses]. Voprosy
Virusologii (6): 705-8. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: adamantane analogs and derivatives, influenza
A virus avian genetics, influenza A virus human genetics, recombination,
genetic drug effects, rimantadine antagonists and inhibitors, antigens, viral
genetics, chick embryo, drug resistance, microbial, influenza A virus avian
drug effects, influenza A virus human drug effects, microbial sensitivity
tests, rabbits.
Podcherniaeva, R.I.A., V.K. Blinova, M.V. Ronina,
E.I. Sklianskaia, and N.V. Kaverin (1980). Antigennye rekombinanty virusov
grippa cheloveka s virusami, vydelennymi ot dikikh ptits. [Antigenic
recombinants of human influenza viruses with viruses isolated from wild birds].
Voprosy Virusologii (4): 419-24.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Antigenic recombinants obtained by crossing
of different human and animal influenza viruses were studied for some genetic
markers and specific proteins in the resulting recombinants were analyses. In a
number of cases the origin of inner virion proteins (NP and M) from one or the
other parent and nonstructural NS proteins was established.
Descriptors: antigens, viral genetics, birds microbiology,
influenza A virus avian genetics, influenza A virus human genetics,
recombination, genetic, antigens, viral analysis, genetic markers, species
specificity, viral proteins genetics.
Podcherniaeva, R.I.A., I.A. Miasnikova, V.K. Blinova,
R.V. Belousova, and V.P. Andreev (1979). Izuchenie svoistv virusov grippa,
vydelennykh v 1976 g. ot chaikovykh ptits v Astrakhanskoi oblasti. [Properties
of the influenza viruses isolated in 1976 from gulls in Astrakhan Province].
Voprosy Virusologii (3): 227-32.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Investigation of a number of properties of
influenza viruses isolated from Laridae birds in the Astrakhan region showed
that in one epizootic focus avian influenza viruses with different
hemagglutinins and identical neuraminidase may circulate among Laridae birds.
Among viruses with the antigenic formula Hav5Nav2 clear-cut differences in
virulence and plaque-forming capacity were demonstrated.
Descriptors: birds microbiology, influenza A virus
isolation and purification, antigens, viral analysis, chick embryo, chickens,
cytopathogenic effect, viral, hemagglutination, viral, hemagglutinins viral
analysis, influenza A virus immunology, influenza A virus pathogenicity, mice,
neuraminidase analysis, plaque assay, Russia, virulence, virus replication.
Podcherniaeva, R.I.A., M.I. Sokolov, V.K. Blinova,
A.G. Uzunova, and S.V. Lavrov (1972). Izuchenie mezhvidovoi rekombinatsii
virusov grippa AO i istinnoi chumy ptits. [Interspecies recombination of
influenza AO and fowl plague viruses]. Voprosy Virusologii 17(5):
559-64. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian, orthomyxoviridae
drug effects, recombination, genetic, amantadine pharmacology, drug resistance,
microbial.
Podchernyaeva, R.J., R.G. Webster, V.V. Skovorodka,
A.I. Klimov, and V.M. Zhdanov (1989). Molecular and biological properties of
a variant of avian influenza A/Seal/Massachusetts/1/80 (H7N7) virus that is
pathogenic for mice. Acta Virologica 33(1): 38-42. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: A/Seal/Mass/80 influenza virus has been shown
to be closely related antigenically and genetically to avian influenza H7N7
viruses, however, the virus does not replicate efficiently in avian species but
does replicate in most mammals, except mice (Hinshaw et al., Infect. Immun.,
34, 351-361, 1981). In order to develop a model defining the molecular changes
that occur during acquisition of virulence, the A/Seal/Mass/80 virus was
adapted to growth in mouse lungs. The adaptation was accompanied by changes in
a number of properties of the haemagglutinin as well as by changes in other genes
of the virus as determined by RNA: RNA hybridization.
Descriptors: influenza A virus pathogenicity, genes viral,
hemagglutinins viral, influenza A virus genetics, lethal dose 50, lung
microbiology, mice, neutralization tests, nucleic acid hybridization, RNA viral
analysis, serial passage, variation genetics, virulence.
Podchernyaeva, R.Y.A., V.K. Blinova, N.N. Sokolova,
V.R. Farashyan, V.M. Zhdanov, S.D. Irzhanov, D.K. Lvov, and Y.u.Z. Ghendon
(1983). Comparative studies on biological properties and genome composition
of influenza virus recombinants. Acta Virologica 27(3): 209-16. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Some biological properties and the genome
composition of antigenic recombinants obtained by crossing of human and animal
influenza viruses were studied. Analysis of the recombinants has shown that
upon heating of virions in vitro thermostability of the haemagglutinin (HA)
does not necessarily correlate with the properties of parent HA; apparently it
depended not only on the properties of the HA itself, but also on the
peculiarities of other virion proteins. All recombinants obtained by crossing
of pathogenic and apathogenic for mice parents either had a reduced
pathogenicity for mice or were apathogenic. In some instances, reduction or
loss of pathogenicity was observed in recombinants which inherited only one
gene from the apathogenic parent; however, the data obtained suggest that
pathogenicity involves functions of a number of genes. Human and animal
influenza virus strains under study proved to be capable of replication in
human embryo tracheal and kidney organ cultures. The degree of reproduction of
the recombinants was either lower or higher as compared to the parent strains.
Descriptors: genes viral, influenza A virus avian
genetics, influenza A virus human genetics, recombination, genetic, chick
embryo, hemagglutinins viral immunology, influenza A virus avian immunology,
influenza A virus avian physiology, influenza A virus human immunology,
influenza A virus human physiology, organ culture, virus replication.
Podchernyaeva, R.Y.A., L. Dohner, R.M. Herrmann, V.K.
Blinova, and V.T. Ivanova (1982). Studies on some genetic properties of
antigenic recombinants of influenza viruses. Acta Virologica 26(4):
227-33. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Two groups of antigenic recombinants Hav4N1
were obtained by recombination of human influenza virus H0N1 with two avian
influenza viruses isolated from ducks in 1956 and terns in 1978 and possessing
the same surface antigen Hav4 Nav1. Recombinants obtained by crossing A/PR/8/34
and A/duck/CSSR/56 viruses showed a lower ability to reproduce at optimal and
lowered temperatures and differed in the thermosensitivity of haemagglutinin
and neuraminidase. An analysis of virus-specific proteins of the recombinants
revealed different combinations of genes coding for internal (Pl, NP) and
nonstructural (NS1) proteins. Recombinants obtained by crossing A/PR/8/34 and
A/tern/Frunze/334/78 viruses possessed a thermostable haemagglutinin; they
produced plaques of a size characteristic of avian influenza but, as distinct
from the latter, they were practically not eluted from fowl erythrocytes.
Polypeptide analysis of these recombinants showed that the genes coding for NP,
M and NS1 proteins were inherited from the A/tern/Frunze/334/78 strain.
Descriptors: antigens, viral genetics, influenza A virus
avian genetics, influenza A virus human genetics, recombination, genetic,
antigens, viral analysis, hemagglutinins viral analysis, influenza A virus
avian immunology, influenza A virus human immunology, neuraminidase immunology,
viral proteins analysis.
Poon, L.L., E. Fodor, and G.G. Brownlee (2000). Polyuridylated
mRNA synthesized by a recombinant influenza virus is defective in nuclear
export. Journal of Virology 74(1): 418-27. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The poly(A) tail of influenza virus mRNA is
synthesized by reiterative copying of a U track near the 5' end of the virion
RNA (vRNA) template by the viral RNA polymerase. We have engineered a novel
influenza A/WSN/33 virus which contains a neuraminidase (NA) vRNA with its U
track mutated into an A track. Instead of synthesizing poly(A)-tailed NA mRNA,
this novel virus synthesizes poly(U)-tailed NA mRNA. In infected cells, most
poly(U)-tailed NA mRNA was retained in the nucleus, while most control
polyadenylated NA mRNA was transported to the cytoplasm. These results suggest
that the poly(A) tail is important for efficient nuclear export of NA mRNA. The
mutant virus produced a reduced amount of NA and showed an attenuated
phenotype, suggesting that poly(A) signal mutants of this type might be useful
as potential live attenuated virus vaccines. In addition, this virus mutant
might provide a useful model to further elucidate the basic mechanisms of mRNA
nuclear export.
Descriptors: cell nucleus metabolism, influenza A virus
avian genetics, poly U metabolism, RNA, messenger biosynthesis, recombination,
genetic, base sequence, biological transport, chick embryo, DNA primers,
mutation, neuraminidase genetics, nucleic acid conformation, RNA, messenger
chemistry, RNA, messenger metabolism.
Porter, A.G., C. Barber, N.H. Carey, R.A. Hallewell,
G. Threlfall, and J.S. Emtage (1979). Complete nucleotide sequence of an
influenza virus haemagglutinin gene from cloned DNA. Nature
282(5738): 471-7. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Abstract: A synthetic fowl plague virus (FPV)
haemagglutinin gene has been cloned in bacteria and the complete sequence of
the RNA gene deduced. It is 1,742 nucleotides long and the mRNA codes for 56.3
amino acids in an uninterrupted sequence. The nature of some of the important
domains in the haemagglutinin has been established, and their structure is
discussed in relation to their function. Extensive amino acid sequence
homologies exist between FPV and human influenza haemagglutinins.
Descriptors: genes, structural, genes viral,
hemagglutinins viral genetics, influenza A virus avian genetics, viral proteins
genetics, amino acid sequence, codon, DNA repair, DNA, recombinant, RNA,
messenger genetics.
Porter, A.G., J.C. Smith, and J.S. Emtage (1980). Nucleotide
sequence of influenza virus RNA segment 8 indicates that coding regions for NS1
and NS2 proteins overlap. Proceedings of the National Academy of
Sciences of the United States of America 77(9): 5074-8. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: The smallest RNA segment of influenza A
viruses (vRNA segment 8) has recently been shown to code for two unrelated
nonstructural proteins (NS1 and NS2) translated from separate mRNAs. Molecular
weight considerations indicated that there might not be enough space on vRNA
segment 8 for the two coding regions unless they overlap. We have recently
cloned in bacterial plasmids several genes of an avian influenza A virus, fowl
plague virus (EPV), and now present the complete nucleotide sequence of FPV RNA
segment 8 largely determined from the cloned DNA. The DNA sequence predicts two
open protein synthesis reading frames that can be translated into polypeptides
of sizes similar to those of NS1 and NS2. The coding regions for these
polypeptides overlap by the equivalent of 43-60 amino acids, the exact amount
depending on which of several possible methionines initiates the synthesis of
NS2.
Descriptors: genes, structural, genes viral, influenza A
virus avian genetics, viral proteins genetics, amino acid sequence, base
sequence, cloning, molecular, codon genetics, DNA restriction enzymes, genes,
synthetic, molecular weight, plasmids, RNA viral genetics.
Portincasa, P., G. Conti, and C. Chezzi (1990). Abortive
replication of influenza A viruses in HeLa 229 cells. Virus Research
18(1): 29-40. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Several experimental data support the idea
that certain mammalian cells are unable to replicate influenza viruses type A,
although these viruses can efficiently penetrate the cells. This cannot be
attributed to a lack of specific receptors on the cell surface, but depends upon
the failure of specific step(s) to occur during viral growth. Here we report a
study of abortiveness of human and avian type A influenza viruses in HeLa 229
cells. Viral polypeptide synthesis was monitored by [35S]methionine pulse
labelling at several time points after infection, showing that normal amounts
of virus-induced components were synthesized. Cellular fractionation of HeLa
229 cells infected by influenza viruses showed that the distribution of viral
proteins into nuclear and cytoplasmic compartments was comparable to that seen
in the permissive host, chick embryo fibroblasts. Viral HA glycoprotein,
produced during the infectious cycle, was entirely found in the cytoplasm of
infected HeLa 229 cells. The polypeptide was able to agglutinate red blood
cells but did not show positive haemadsorption even at late times of infection.
Therefore it seems that during the maturation of viral particles there is a
failure of the haemagglutinin to perform a correct insertion into the plasma
membrane of infected HeLa 229 cells.
Descriptors: fibroblasts microbiology, hemagglutinins
viral metabolism, influenza A virus avian growth and development, influenza A
virus human growth and development, cell membrane metabolism, chick embryo,
HeLa cells, hemadsorption, hemagglutinin glycoproteins, influenza virus,
influenza A virus avian metabolism, influenza A virus human metabolism,
methionine metabolism, virus replication.
Portincasa, P., G. Conti, and C. Chezzi (1991). Defective
insertion of haemagglutinin as a cause of abortivity of influenza A viruses in
HeLa 229 cells. Microbiologica 14(4): 351-5. ISSN: 0391-5352.
NAL
Call Number: QR1.M57
Abstract: A number of experimental data demonstrate
that certain mammalian cells are unable to replicate Influenza viruses type A.
In these cellular hosts the viruses can efficiently perform their biological as
well as biochemical activities but the production of mature viral particles is
greatly restricted. Here we report a study of abortiveness of human and avian
type A Influenza viruses in HeLa 229 cells in which the final stages of
maturation of viral particles seem to be affected. We show that the incorrect
insertion of virus-coded haemagglutinin into the plasma membrane might be the
cause of the unpermissive condition of infection exhibited by this cellular
host.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian physiology, influenza A virus human physiology, virus replication,
cultured cells, chick embryo, HeLa cells, hemadsorption.
Portnoy, J. and T.C. Merigan (1971). The effect of
interferon and interferon inducers on avian influenza. Journal of
Infectious Diseases 124(6): 545-52.
ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Descriptors: fluorenes therapeutic use, influenza drug
therapy, influenza A virus avian drug effects, interferons therapeutic use,
polynucleotides therapeutic use, polysaccharides therapeutic use, cultured
cells drug effects, chick embryo, chickens, disease models, animal, ethylamines
therapeutic use, injections,
intravenous, interferons biosynthesis, interferons blood, poly I C
pharmacology, poly I C therapeutic use, polysaccharides pharmacology,
temperature, virus replication drug effects.
Possee, R.D., G.C. Schild, and N.J. Dimmock (1982). Studies
on the mechanism of neutralization of influenza virus by antibody: evidence
that neutralizing antibody (anti-haemagglutinin) inactivates influenza virus in
vivo by inhibiting virion transcriptase activity. Journal of General
Virology 58(Pt. 2): 373-86. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Influenza viruses, which had lost up to
99.999% infectivity by incubation with antibody (a) specific for the
haemagglutinin (HA) or with monoclonal alpha-HA, attached on to and penetrated
chick embryo fibroblast (CEF) cells to the same extent as non-neutralized
virus. Neutralized virus was also uncoated efficiently as shown by the
accumulation of virion RNA in the nucleus and virion envelope in the cytoplasm.
Polyacrylamide gel electrophoresis of virion RNA segments recovered from the
nucleus or cytoplasm of cells inoculated with neutralized or non-neutralized
virus showed that antibody did not potentiate degradation of RNA. However,
these RNAs were not expressed since virus-induced proteins were not detected in
cells to which neutralized virus had been added. Assay of virion transcriptase
of neutralized virus in vitro showed that its activity was reduced up to
sevenfold compared with non-neutralized virus, and annealing studies showed
that no detectable transcription took place in vivo with neutralized virus.
These studies support the conclusion that antibody directed specifically
against the HA protein on the outer surface of the influenza virus particle
neutralizes infectivity by inactivating virion transcriptase activity and it is
suggested that antibody to HA brings about allosteric rearrangements in the HA
molecule which are transmitted across the virus envelope to the interior of the
particle.
Descriptors: antibodies, viral physiology, DNA directed
RNA polymerases antagonists and inhibitors, hemagglutinins viral immunology,
influenza A virus avian immunology, influenza A virus human immunology,
cultured cells, chick embryo, influenza A virus avian enzymology, influenza A
virus avian growth and development, influenza A virus human enzymology,
influenza A virus human growth and development, neutralization tests, viral
proteins biosynthesis.
Pravdina, N.F., T.V. Veselovskaia, N.L. Pushkarskaia,
and G.Z. Galegov (1972). Nekotorye metodicheskie voprosy izucheniia
belkovogo sostava miksovirusov metodom elektroforeza v poliakrilamidonom gele
[Methodological problems of studying the protein composition of myxoviruses by
the polyacrylamide gel electrophoresis method]. Voprosy Meditsinskoi
Khimii 18(2): 158-61. ISSN:
0042-8809.
Descriptors: electrophoresis, polyacrylamide gel methods,
orthomyxoviridae analysis, paramyxoviridae analysis, viral proteins analysis,
influenza A virus avian analysis, influenza A virus avian isolation and
purification, molecular weight, Newcastle disease virus analysis, Newcastle
disease virus isolation and purification, orthomyxoviridae isolation and
purification, paramyxoviridae isolation and purification.
Pravdina, N.F., T.V. Veselovskaia, V.D. Smirnov, and
G.A. Galegov (1985). Ingibiruiushchee deistvie dezoksiadenilil-(3'-5')-dezoksiguanozina
na aktivnost' RNK-polimerazy virusa grippa A. [Inhibitory effect of
deoxyadenylyl-(3'-5')-deoxyguanosine on the RNA-polymerase activity of
influenza virus A]. Voprosy Meditsinskoi Khimii 31(5): 123-5. ISSN: 0042-8809.
Abstract: Deoxyadenylylguanosine (dAdG, 0.2-0.4 mM),
affecting the RNA polymerase activity, caused inhibition of transcription of
the influenza A virus in presence of precursor AdG by 50-60% and a 80-85%
inhibition in absence of the precursor. The inhibitor exhibited its effect
independently on the time of addition into an incubation mixture. Addition of
0.5 mM inhibitor into a cultural medium inhibited reproduction of the influenza
A virus in a culture of chicken embryonal fibroblasts.
Descriptors: DNA directed RNA polymerases antagonists and
inhibitors, deoxyadenine nucleotides, deoxyguanosine, influenza A virus avian
enzymology, oligodeoxyribonucleotides pharmacology, virus replication drug
effects, cultured cells, chickens, influenza A virus avian physiology.
Prokudina, E.N., N.P. Semenova, V.M. Chumakov, and
I.A. Rudneva (2004). Transient disulfide bonds formation in conformational
maturation of influenza virus nucleocapsid protein (NP). Virus Research
99(2): 169-75. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: It has been previously shown that influenza
virus nucleocapsid protein (NP) forms homooligomers in vivo. Our analyses
revealed that the reducing agent dithiothreitol (DTT) introduced in pulse
labeling period prevented further formation of native NP-oligomers. The shortly
pulse-labeled non-reduced newly synthesized NP possessed a relatively faster
mobility in non-reducing PAGE and a higher resistance to protease than the
reduced one. These data suggest that there is an early disulfide-dependent step
in NP maturation and that the newly synthesized NP possesses the intrachain
disulfide bonds. In contrast to the newly synthesized NP, the non-reduced
chased NP possessed the same mobility in non-reducing PAGE and the same
sensitivity to protease as the reduced NP. DTT introduced in the chase period
did not prevent NP-oligomers formation and did not destabilize already formed
NP-oligomers. This suggests that the chased NP monomers and NP-oligomers do not
contain intrachain nor interchain disulfide bonds. It was also shown that the
non-reduced newly synthesized NP could not form NP-NP complexes in vitro, and
acquired such ability only after reducing. The possibility is discussed that
there are several stages in the maturation of NP: the initial formation of
intrachain disulfide-linked NP and conversion into disulfide-free NP, which
forms non-covalently stabilized NP-oligomers. Early intrachain disulfide bonds
may be necessary for the prevention of early spontaneous NP-NP association.
Descriptors: avian influenza A virus chemistry,
nucleoproteins chemistry, RNA binding proteins, viral core proteins chemistry,
cell line, disulfides chemistry, dithiothreitol metabolism, dogs,
electrophoresis, polyacrylamide gel, immunoblotting, avian influenza A virus
growth and development, nucleoproteins isolation and purification, oxidation
reduction, protein binding, protein conformation, viral core proteins isolation
and purification.
Prokudina, E.N., N.P. Semenova, V.M. Chumakov, I.A.
Rudneva, and S.S. Yamnikova (2001). Extracellular truncated influenza virus
nucleoprotein. Virus Research 77(1): 43-9. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: In the culture medium of MDCK cells infected
with influenza A/Duck/Ukraine/1/63(H3N8) virus two kinds of virus nucleoprotein
(NP) are detected: full-length 56 kDa NP and truncated 53 kDa NP. However, in
infected cells 53 kDa NP may be detected only at short pulse and after 10 min
chase it becomes nondetectable. The extracellular truncated 53 kDa NP is detected
in free RNP, and not in the virions. Both extracellular free 53 and 56 kDa NP
in the virions are completely oligomerized. Several data argue against the
possibility of extracellular 53 kDa NP formation being a result of
extracellular 56 kDa NP proteolytic degradation. Thus, the accumulation of
extracellular 53 kDa NP takes place only in the course of infection, and the
amount of 53 kDa NP is not increased during prolonged storage of cell-free
culture medium at +37 degrees C. Moreover, all extracellular 56 kDa NP of
A/Duck/Ukraine/1/63 influenza virus is present in the oligomeric form, and the
latter, in contrast to the mononeric form, is highly resistant to proteases.
The possibility is discussed that in the course of A/Duck/Ukraine/1/63 (H3N8)
influenza virus infection a fraction of the synthesized 56 kDa monomeric NP
undergoes the proteolytic cleavage in the infected cells before oligomerization
and forms the 53 kDa NP. This 53 kDa NP is then oligomerized, enters the RNP
and is quickly secreted from the cells.
Descriptors: influenza A virus avian metabolism,
nucleoproteins metabolism, viral core proteins metabolism, cell line, culture
media, dogs, ducks, fowl plague virology, influenza A virus avian
pathogenicity, nucleoproteins chemistry, viral core proteins chemistry.
Prokudina Kantorovich, E.N. and N.P. Semenova (1996).
Intracellular oligomerization of influenza virus nucleoprotein. Virology
223(1): 51-6. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: It has previously been shown that the
purified influenza virus nucleoprotein (NP) forms the oligomers in vitro in NP
preparations obtained from virions (Wiley et al., 1977, Virology, 79, 446-448;
Ruigrok and Baudin, 1995, J. Gen. Virol., 76, 1009-1014) and infected cells
(Becht and Weiss, 1991, Behring Inst Mitt., Justus-Liebig Universitat, Giessen,
89, 1-11). We have shown in this report that boiling-sensitive NP oligomers
(di- and trimers) are formed in vivo in the course of intracellular influenza
virus replication. They are detected by PAGE about 10 min after monomeric
56-kDa NP molecules are synthesized. NP oligomers are formed by different
strains of influenza virus in different cell lines. Some influenza virus
strains are characterized by complete conversion of NP monomers into oligomers
and others by only partial conversion. In the Triton X-114 phase partitioning
system NP oligomers show more hydrophobicity than NP monomers. NP oligomers are
detected in the sedimentable and soluble fractions of both cell lysate and
extracellular medium. The possibility is discussed that oligomeric NP is a
native and functionally significant form of influenza virus NP.
Descriptors: influenza A virus metabolism, nucleoproteins
metabolism, viral core proteins metabolism, cell line, chick embryo, dogs,
ducks, influenza A virus avian metabolism, influenza A virus human metabolism,
swine.
Pruett, P.S. and G.M. Air (1998). Critical
interactions in binding antibody NC41 to influenza N9 neuraminidase: amino acid
contacts on the antibody heavy chain. Biochemistry 37(30):
10660-70. ISSN: 0006-2960.
NAL
Call Number: 381 B523
Abstract: Antibody NC41 binds to the subtype N9
neuraminidase (NA) of influenza virus A/tern/Australia/ G70c/75 and inhibits
its enzyme activity. To address the molecular mechanisms by which antibodies
interact with neuraminidase and the requirements for successful escape from
antibody inhibition, we made amino acid substitutions in heavy chain CDRs of
NC41. Antibody proteins expressed as a single-chain Fv (scFv) fused with
maltose-binding protein were assayed for binding to NA by ELISA. Association
constants (Ka) for wild-type and mutant scFvs are as follows: wild type, 2 x
10(7) M-1; Asn31-->Gln, 2 x 10(7) M-1; Glu96-->Asp, 1 x 10(7) M-1;
Asp97-->Lys, 6 x 10(6) M-1; and Asn98-->Gln, 8 x 10(6) M-1. The Ka for
intact NC41 antibody was 4 x 10(8) M-1 in the same assay, reflecting increased
stability compared to that of the scFv. Mutations in the scFv antibody had less
of an effect on binding than mutations in their partners on the NA, and
modeling studies suggest that interactions involving the mutant antibody side
chains occur, even without taking increased flexibility into account. Asp97
forms a salt link with NA critical contact Lys434; of the four mutants, D97K
shows the largest reduction in binding to NA. Mutant N98Q also shows reduced
binding, most likely through the loss of interaction with NA residue Thr401.
Substitution N31Q had no effect on Ka. NC41 residue Glu96 interacts with NA
critical contact Ser368, yet E96D showed only a 2-fold reduction in binding to
NA, apparently because the H bond can still form. Asp97 and Asn98 provide the
most important interactions, but some binding is maintained when they are
mutated, in contrast to their partners on the NA. The results are consistent
with maturation of the immune response, when the protein epitope is fixed while
variation in the antibody paratope allows increasing affinity. Influenza
viruses may exploit this general mechanism since single amino acid changes in
the epitope allow the virus to escape from the antibody.
Descriptors: amino acids metabolism, antibodies,
monoclonal metabolism, binding sites, antibody, immunoglobulins, heavy chain
metabolism, influenza A virus avian immunology, neuraminidase immunology, amino
acid sequence, amino acid substitution genetics, amino acids genetics, amino
acids immunology, antibodies, monoclonal biosynthesis, antibodies, monoclonal
chemistry, base sequence, fluorescence
polarization, immunoglobulin fragments biosynthesis, immunoglobulin fragments
chemistry, immunoglobulin fragments metabolism, immunoglobulin variable region
biosynthesis, immunoglobulin variable region chemistry, immunoglobulin variable
region metabolism, immunoglobulins, heavy chain chemistry, immunoglobulins,
heavy chain genetics, models, molecular, molecular sequence data, mutagenesis,
site directed, neuraminidase chemistry, neuraminidase metabolism.
Puertollano, R., F. Martin Belmonte, J. Millan, M.C.
de Marco, J.P. Albar, L. Kremer, and M.A. Alonso (1999). The MAL proteolipid
is necessary for normal apical transport and accurate sorting of the influenza
virus hemagglutinin in Madin-Darby canine kidney cells. Journal of Cell
Biology 145(1): 141-51. ISSN:
0021-9525.
NAL
Call Number: 442.8 J828
Abstract: The MAL (MAL/VIP17) proteolipid is a
nonglycosylated integral membrane protein expressed in a restricted pattern of
cell types, including T lymphocytes, myelin-forming cells, and polarized epithelial
cells. Transport of the influenza virus hemagglutinin (HA) to the apical
surface of epithelial Madin-Darby canine kidney (MDCK) cells appears to be
mediated by a pathway involving glycolipid- and cholesterol- enriched membranes
(GEMs). In MDCK cells, MAL has been proposed previously as being an element of
the protein machinery for the GEM-dependent apical transport pathway. Using an
antisense oligonucleotide-based strategy and a newly generated monoclonal
antibody to canine MAL, herein we have approached the effect of MAL depletion
on HA transport in MDCK cells. We have found that MAL depletion diminishes the
presence of HA in GEMs, reduces the rate of HA transport to the cell surface,
inhibits the delivery of HA to the apical surface, and produces partial
missorting of HA to the basolateral membrane. These effects were corrected by
ectopic expression of MAL in MDCK cells whose endogenous MAL protein was
depleted. Our results indicate that MAL is necessary for both normal apical
transport and accurate sorting of HA.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, proteolipids physiology,
antibodies, monoclonal pharmacology, biological transport drug effects,
cell polarity, detergents pharmacology, dogs, epithelial cells metabolism,
kidney, membrane lipids metabolism, membrane proteins metabolism,
oligonucleotides, antisense pharmacology, proteolipids antagonists and
inhibitors, proteolipids genetics, proteolipids immunology, rats, rats, wistar,
transfection.
Purchase, H.G. (1989). Practical application of
nucleic acid techniques to avian disease problems. Avian Diseases
33(4): 609-14. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: A workshop in which 17 practicing scientists
participated was intended to address primarily people who use or could use
biotechnology in their work and was confined to five techniques. Endonuclease
fingerprinting and mapping involved cleaving nucleic acid with a specific
restriction enzyme and separating the nucleic acid fragments by electrophoresis.
Field and vaccine isolates of Pasteurella multocida could be
distinguished; Salmonella enteritidis could be divided into three
groups; chlamydia could be grouped into seven groups; and vaccinia, quail pox,
and fowl pox could be clearly distinguished. Preparation of nucleic acid probes
involved producing large amounts of labeled oligonucleotides, usually of
unknown sequence. Successful probes had been made for infectious bursal disease
virus, avian influenza virus, Newcastle disease virus, and infectious
bronchitis virus. In Southern, Northern, and dot blotting, either DNA or RNA
fragments were placed on or transferred to a solid substrate and probed. The
procedure was able to detect infectious bursal disease virus, infectious
bronchitis virus, Mycoplasma gallisepticum, and Marek's disease virus.
In situ hybridization involved applying a labeled probe to frozen or fixed
sections or to intact cells. In Polymerase chain reaction, two primers, some
distance apart, were annealed to a denatured target DNA. Repeated cycles of DNA
synthesis with a thermostable polymerase, denaturing, and reannealing resulted
in great amplification of a rare sequence. After 30 cycles, a rare gene
sequence could be amplified more than 10(6) times. It was used successfully to
detect minute quantities of influenza virus and infectious bursal disease
virus, and the process was used to facilitate DNA sequencing of coccidiosis
gene segments.
Descriptors: poultry diseases diagnosis, blotting,
northern, blotting, Southern, DNA restriction enzymes genetics, nucleic acid
hybridization, nucleic acid probes, peptide mapping, polymerase chain reaction.
Pushkarskaia, N.L., Z.h.A. Shakarian, S.C. Lavrov,
and G.A. Galegov (1972). Kombinirovannoe deistvie amantadina i DL-etionina
na reproduktsiiu virusa grippa v kul'ture tkani. [Combined effect of amantadine
and DL-ethionine on the reproduction of influenza virus in tissue culture].
Voprosy Virusologii 17(3): 267-9.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: amantadine pharmacology, ethionine
pharmacology, influenza A virus avian drug effects, antiviral agents
pharmacology, chickens, fibroblasts, tissue culture, virus replication drug
effects.
Qiao ChuanLing, Jiang YongPing, Yu KangZhen, Tian
GuoBin, and Chen HuaLan (2004). Immune efficacy of a recombinant fowlpox
virus co-expressing HA and NA genes of avian influenza virus in SPF chickens.
Agricultural Sciences in China 3(9): 716-720. ISSN: 1671-2927.
NAL
Call Number: S417.C6Z462
Descriptors: antibodies, experimental infections, gene
expression, immunity, potency, recombinant vaccines, vaccine development, viral
hemagglutinins, avian influenza virus, fowl pox virus, chickens, poultry, fowl,
mortality.
Qiao ChuanLing, Yu KangZhen, Deng GuoHua, Wang
XiuRong, Meng QingWen, Tian GuoBin, and Tang XiuYing (2003). Cloning of NA
gene of avian influenza virus A/Goose/Guangdong/3/96(H5N1) and construction of
transfer vector of recombinant fowlpox virus. Chinese Journal of
Veterinary Science 23(2): 111-114.
ISSN: 1005-4545.
NAL
Call Number: SF604.C58
Descriptors: complementary DNA, DNA cloning, genes,
nucleotide sequences, avian influenza virus, fowl pox virus, poultry, geese,
China, Guangdong.
Ramalho Santos, J., S. Nir, N. Duzgunes, A.P. de
Carvalho, and M.C. de Lima (1993). A common mechanism for influenza virus
fusion activity and inactivation. Biochemistry 32(11): 2771-9. ISSN: 0006-2960.
NAL
Call Number: 381 B523
Abstract: The fusion of influenza virus (A/PR/8/34
strain) with PC-12 cells was monitored by a fluorescence assay, and the results
were analyzed with a mass-action model which could explain and predict the
kinetics of fusion. The model accounted explicitly for the reduction in the
fusion rate constant upon exposure of the virus to low pH, either for the virus
alone in suspension or for the virus bound to the cells. When the pH was
lowered without previous viral attachment to cells, an optimal fusion activity
was detected at pH 5.2. When the virus was prebound to the cells, however,
reduction of pH below 5.2 resulted in enhanced fusion activity at the initial
stages. These results were explained by the fact that the rate constants of
both fusion and inactivation increased severalfold at pH 4.5 or 4, compared to
those at pH 5.2. At pH 5.2, lowering the temperature from 37 to 20 or 4 degrees
C resulted in a decrease in the fusion rate constant by more than 30- or
1000-fold, respectively. Inactivation of the virus when preincubated in the
absence of target membranes at pH 5 was found to be rapid and extensive at 37
degrees C, but was also detected at 0 degrees C. Our results indicate a strong
correlation between fusion and inactivation rate constants, suggesting that the
rate-limiting step in viral hemagglutinin (HA)-mediated fusion, that is,
rearrangement of viral glycoproteins at the contact points with the target
membrane, is similar to that involved in fusion inactivation.
Descriptors: influenza A virus avian physiology, chick
embryo, hydrogen-ion concentration, kinetics, mathematics, membrane fusion,
PC-12 cells, rats, temperature.
Ratner, L.S., D. Omirzhanov, G.N. Pershin, and N.S.
Bogdanova (1971). Izuchenie antivirusnogo deistviia khlozameshchennykh
benzokhinona i gidrokhinona. [Study of antiviral effect of chlorine-substituted
benzoquinine and hydroquinine]. Farmakologiia i Toksikologiia 34(1):
80-3. ISSN: 0014-8318.
Descriptors: antiviral agents therapeutic use, chlorides
administration and dosage, DNA viruses drug effects, hydroquinones
administration and dosage, quinones administration and dosage, RNA viruses drug
effects, virus diseases prevention and control, aphthovirus drug effects, chick
embryo, cytopathogenic effect, viral drug effects, depression, chemical,
herpesviridae drug effects, hydroquinones therapeutic use, influenza A virus
avian drug effects, mice, quinones therapeutic use, tissue culture, viruses
pathogenicity.
Rees, P.J. and N.J. Dimmock (1982). Kinetics of
synthesis of influenza virus ribonucleoprotein structures. Journal of
General Virology 59(Pt. 2): 403-8.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The synthesis of influenza virus
ribonucleoprotein structures (RNPs) in infected chick embryo cells was analysed
by polyacrylamide gel electrophoresis (PAGE) in the presence of sodium
deoxycholate which resolves the RNPs into five size classes. A relatively small
proportion of total RNPs accumulated in the nucleus but free NP protein was
found there in large amounts over the period 1.5 to 4 h post-infection. In
contrast, by 4 h post-infection, all cytoplasmic NP was complexed into RNP
structures. At early times, during at 15 min pulse of (35S]methionine, nearly
all the newly synthesized NP was incorporated into RNPs but by 4 h the majority
of pulse-labelled NP was present as free protein. However, the proportion of
free NP: NP in RNPs remained constant over the 1.5 to 4 h post-infection
period, indicating that there was a delay before the NP synthesized later in
infection was assembled into RNP structures. Individual RNP size classes were
predominantly cytoplasmic and accumulated at similar rates but were not
produced in equimolar amounts. The rates of synthesis of individual RNPs were
in general agreement with their rates of accumulation with the remarkable
exception of RNP d (containing RNA 7, the matrix protein gene). This was
synthesized nearly 10-fold faster but accumulated at the same rate as the other
RNPs. Possibly RNP d is more rapidly degraded than the other RNPs.
Descriptors: bacterial proteins biosynthesis, influenza A
virus avian metabolism, nucleoproteins biosynthesis, ribonucleoproteins biosynthesis,
cell nucleus metabolism, cultured cells, chick embryo, cytoplasm metabolism,
influenza A virus avian growth and development, kinetics.
Reid, A.H., T.G. Fanning, T.A. Janczewski, R.M.
Lourens, and J.K. Taubenberger (2004). Novel origin of the 1918 pandemic
influenza virus nucleoprotein gene. Journal of Virology 78(22):
12462-70. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The nucleoprotein (NP) gene of the 1918
pandemic influenza A virus has been amplified and sequenced from archival material.
The NP gene is known to be involved in many aspects of viral function and to
interact with host proteins, thereby playing a role in host specificity. The
1918 NP amino acid sequence differs at only six amino acids from avian
consensus sequences, consistent with reassortment from an avian source shortly
before 1918. However, the nucleotide sequence of the 1918 NP gene has more than
170 differences from avian strain consensus sequences, suggesting substantial
evolutionary distance from known avian strain sequences. Both the gene and
protein sequences of the 1918 NP fall within the mammalian clade upon
phylogenetic analysis. The evolutionary distance of the 1918 NP sequences from
avian and mammalian strain sequences is examined, using several different
parameters. The results suggest that the 1918 strain did not retain the
previously circulating human NP. Nor is it likely to have obtained its NP by
reassortment with an avian strain similar to those now characterized. The
results are consistent with the existence of a currently unknown host for
influenza, with an NP similar to current avian strain NPs at the amino acid
level but with many synonymous nucleotide differences, suggesting evolutionary
isolation from the currently characterized avian influenza virus gene pool.
Descriptors: nucleoproteins genetics, RNA binding proteins
genetics, viral core proteins genetics, amino acid sequence, base sequence,
influenza epidemiology, molecular sequence data, nucleoproteins chemistry,
orthomyxoviridae classification, phylogeny, RNA binding proteins chemistry,
regression analysis, swine, time factors, viral core proteins chemistry.
Reina, J. (2002). Factores de virulencia y
patogenicidad en las cepas gripales (virus influenza tipo A) aviares y humanas.
[Factors affecting the virulence and pathogenicity of avian and human viral
strains (influenza virus type A)]. Enfermedades Infecciosas y
Microbiologia Clinica 20(7): 346-53.
ISSN: 0213-005X.
Abstract: Most studies performed in avian viral strains
seem to indicate that virulence is a polygenic phenomenon. However,
hemagglutinin and neuraminidase and the genes codifying these substances (genes
4 and 6) play an essential role in viral pathogenesis. Avian strains can be
classified as avirulent or virulent according to the ability of hemagglutinin
to be activated by endoproteases of the respiratory tract only or by proteases
from other tissues. This ability is based on the progressive development of
mutations that lead to the substitution of the normal amino acids at the point
of hemagglutinin hydrolysis by the other basic amino acids that determine the
amplification of the spectrum of hydrolysis and activation. Neuraminidase
participates in the acquisition of virulence through its capacity to bind to
plasminogen and by increasing the concentration of activating proteases.
Adaptation to the host, through recognition of the cell receptor, is another
factor determining the virulence and interspecies transmission of avian
strains. From an epidemiological point of view, viral strains should be
subtyped and the activating capacity of hemagglutinin should be determined to
identify their degree of virulence.
Descriptors: influenza A virus avian pathogenicity,
influenza A virus human pathogenicity, hemagglutinins, neuraminidase, peptide
hydrolases, virulence.
Reinacher, M. (1974). Intracellular maturation of
fowl plague virus in chicken-embryo cell monolayers. Naturwissenschaften
61(3): 135. ISSN: 0028-1042.
NAL
Call Number: 474 N213
Descriptors: influenza A virus avian growth and
development, cell membrane, chick embryo, microscopy, electron, virus
cultivation.
Reinacher, M., J. Bonin, O. Narayan, and C.
Scholtissek (1983). Pathogenesis of neurovirulent influenza A virus
infection in mice. Route of entry of virus into brain determines infection of
different populations of cells. Laboratory Investigation a Journal of
Technical Methods and Pathology 49(6): 686-92. ISSN: 0023-6837.
NAL
Call Number: 448.8 L11
Abstract: Coinfection of a cell culture with a human
and avian influenza A virus had yielded a recombinant virus with high
neurovirulence for mice. This study reports on the comparative pathogenesis of
central nervous system infection in mice between the parental human and the
recombinant virus using the immunohistologic peroxidase-antiperoxidase method
and virus assay of tissue suspensions. The human virus replicated poorly in
mice and did not replicate in the brain even after intracerebral inoculation.
In contrast, the recombinant virus replicated to high titer in the lung and
brain with resulting viremia after inoculation of young mice by the
intracerebral, intraperitoneal, or intranasal routes. Different populations of
cells in the brain became infected after inoculation by each of the three
routes: choroid plexus, and ependymal and subependymal cells after
intracerebral inoculation; cells in perivenous areas, neurons in the olfactory
bulbs and trigeminal ganglia and nuclear groups in the brainstem and midbrain
after intranasal inoculation. Intraperitoneal inoculation resulted almost
exclusively in the perivenous spread of the virus. The intranasal inoculation
suggested that virus entry into the brain both by spread along nerve cell
processes from the nasal mucosa to the brain and trigeminal ganglia and
subsequent perivenous spread after viremia developed following virus
replication in the lung. To dissect these two mechanisms we inoculated neonatal
mice that had acquired high levels of serum antibody by nursing from actively
immunized mothers. Intraperitoneal inoculation of these mice failed to cause
infection, whereas intranasal inoculation resulted in the same pattern of
cellular spread through the olfactory and trigeminal pathways as noted
previously. This proved that this recombinant influenza virus could invade the
central nervous system after infection via a natural route of infection. This
highly neuroinvasive agent provides one example of the extent of virulence
which can be acquired by recombination of apathogenic influenza viruses and
raises a note of caution for adequate control of those agents generated in the
laboratory.
Descriptors: brain diseases microbiology, influenza
microbiology, influenza A virus avian pathogenicity, influenza A virus human
pathogenicity, antigens, viral analysis, birds, brain microbiology, brain
pathology, brain diseases immunology, brain diseases pathology, immunization,
influenza immunology, influenza pathology, influenza A virus avian genetics,
influenza A virus avian immunology, influenza A virus human genetics, influenza
A virus human immunology, lung microbiology, lung pathology, mice, plaque
assay, recombination, genetic, virulence, virus replication.
Reinacher, M. and E. Weiss (1975). Electron
microscopical study of initial and final stages of fowl plague
virus-replication in chick embryo cells. Archives of Virology
49(2-3): 187-97. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Cellular uptake of fowl plague virus occurs
10-30 minutes after inoculation of chick embryo cells. The penetration of the
virions is by pinocytosis (viropexis); fusion with the cellular membrane has
not been observed. After pinocytosis the virions become gradually
disintegrated. Budding of newly formed virions from the cellular membrane
starts 3 hours post inoculation (p.i.) and reaches its maximum 8 hours p.i. At
the same time budding takes place into electron microscopically empty and
autophagic vacuoles. Eight hours p.i. about 3 per cent of the infected cells
show budding of virions from the surface and into cytoplasmic vacuoles.
Labelling of the cellular membrane with ruthenium red demonstrated that these
cytoplasmic vacuoles are not simple cross-sections of invaginations of the
cellular membrane. Cluster-like structures were found at 6 hours p.i. in the
nuclei of infected cells; however, the suggestion that the clusters develop
from nucleoli could not be confirmed.
Descriptors: influenza A virus avian ultrastructure, virus
replication, cell membrane microbiology, cell membrane ultrastructure, chick
embryo, influenza A virus avian growth and development, pinocytosis, time
factors, tissue culture, vacuoles microbiology, vacuoles ultrastructure.
Reinhardt, J. and T. Wolff (2000). The influenza A
virus M1 protein interacts with the cellular receptor of activated C kinase
(RACK) 1 and can be phosphorylated by protein kinase C. Veterinary
Microbiology 74(1-2): 87-100. ISSN:
0378-1135.
NAL
Call Number: SF601.V44
Abstract: The M1 protein of influenza A virus has
multiple regulatory functions during the infectious cycle, which include
mediation of nuclear export of viral ribonucleoproteins, inhibition of viral
transcription and a crucial role in virus assembly and budding. The only known
modification of the M1 protein is by phosphorylation through
yet-to-be-identified kinases. We postulated that at least some of the M1
functions are exerted or regulated through interactions with cellular
components. In a screen for such cellular mediators, the protein receptor of
the activated C-kinase (RACK 1) was identified by its interaction with the
viral M1 protein in the yeast two hybrid system. The physical M1-RACK 1
interaction was confirmed in glutathione-S-transferase-based coprecipitation
assays for the diverged M1 proteins of avian, swine and human influenza A virus
strains. This conservation suggests that the M1-RACK 1 interaction is of
general importance during influenza A virus infections. RACK 1 has previously
been identified to specifically bind the activated form of protein kinase C
(PKC) and is assumed to anchor the kinase at membranes in the vicinity of its
substrates. Since the M1 protein becomes phosphorylated during influenza virus
infection, we examined if PKC could catalyze the phosphate transfer. We
demonstrate that virion-derived and recombinant M1 protein can indeed be
efficiently phosphorylated by purified PKC. Moreover, in cell extracts, we
detected M1 phosphorylation activity that was strongly reduced in the presence
of the PKC-specific inhibitor compound GF109203X. These data suggest that PKC
is the main M1-phosphorylating activity in the cell. Since both, the M1 protein
and PKC have been shown to interact with RACK 1, we suggest that the M1-RACK 1
interaction is involved in M1 phosphorylation.
Descriptors: ion channels metabolism, peptides metabolism,
protein kinase c metabolism, viral matrix proteins metabolism, binding
sites, chick embryo, electrophoresis,
polyacrylamide gel, enzyme inhibitors pharmacology, indoles pharmacology,
influenza A virus avian, influenza A
virus human, influenza A virus, porcine, maleimides pharmacology,
phosphorylation, recombinant proteins metabolism, serine metabolism, software,
structure activity relationship, threonine metabolism.
Rimmelzwaan, G.F., T. Kuiken, A.G. van, T.M.
Bestebroer, R.A.M. Fouchier, and A.D.M.E. Osterhaus (2003). A primate model
to study the pathogenesis of influenza A (H5N1) virus infection. Avian
Diseases 47(Special Issue): 931-933.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Cynomolgus macaques (Macaca fascicularis)
infected with influenza virus A/HongKong/156/97 (H5N1) developed acute
respiratory distress syndrome (ARDS) with fever. Reverse
transcriptase/polymerase chain reaction (RT/PCR) and virus isolation showed
that the respiratory tract is the major target of the virus. The main lesion
observed upon necropsy, performed 4 or 7 days postinfection, was a necrotizing
bronchointerstitial pneumonia, similar to that found in primary influenza pneumonia
in human beings. By immunohistochemistry, influenza virus antigen proved to be
limited to pulmonary tissue and tonsils. The data indicate that ARDS and
multiple organ dysfunction syndrome (MODS), observed in both humans and monkeys
infected with this virus, are caused by diffuse alveolar damage from virus
replication in the lungs alone.
Descriptors: infection, acute respiratory distress
syndrome (ARDS), respiratory system disease, avian influenza, infectious
disease, respiratory system disease, viral disease, bronchointerstitial
pneumonia, respiratory system disease, multiple organ dysfunction syndrome
(MODS), disease miscellaneous, immunohistochemistry immunologic techniques,
laboratory techniques, necropsy clinical techniques, reverse transcriptase polymerase
chain reaction (RT PCR) genetic techniques, laboratory techniques, viral
isolation laboratory techniques, influenza pathogenesis viral replication.
Robertson, J.S. (1979). 5' and 3' terminal
nucleotide sequences of the RNA genome segments of influenza virus. Nucleic
Acids Research 6(12): 3745-57. ISSN:
0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: EXtensive nucleotide sequence analysis of the
5' and the 3' terminal of the RNA segments of the genome of fowl plague virus,
an avian strain of influenza virus, confirms the presence of a common sequence
at the 5' terminus of each segment and a common sequence at the 3' terminus of
each segment. Between the ends of each individual segment there is a
complementary sequence which may be important in the control of transcription
and replication of the genome. In addition, the probable sites of initiation of
translation of fowl plague virus mRNA are indicated along with the
corresponding NH2-terminal amino acid sequences of the virus polypeptides.
Descriptors: influenza A virus avian analysis, RNA viral
analysis, base sequence, electrophoresis, polyacrylamide gel, genes viral.
Robertson, J.S. (1980). Nucleotide sequences from
the terminal regions of fowl plague virus genome RNA. Philosophical
Transactions of the Royal Society of London. Series B Biological Sciences
288(1029): 371-4. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Descriptors: influenza A virus, RNA viral genetics, base
sequence.
Robertson, J.S., E. Robertson, I. Roditi, J.W.
Almond, and S.C. Inglis (1983). Sequence analysis of fowl plague virus
mutant ts47 reveals a nonsense mutation in the NS1 gene. Virology
126(1): 391-4. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: A mutant of fowl plague virus, ts47, induces
the synthesis in infected cells of a truncated NS1 polypeptide at both
permissive and restrictive temperatures. Nucleotide sequence analysis of the
segment coding for the NS1 polypeptide, segment 8, indicates that this
aberration is due to a nonsense mutation. This mutation occurs in the region of
the NS1 gene which overlaps with the NS2 gene and there is a corresponding
amino acid substitution in the NS2 polypeptide. While it is not clear which
polypeptide is responsible for the thermal instability of ts47, the loss of the
COOH-terminal 28 amino acid residues from the NS1 polypeptide does not affect
replication of the virus at permissive temperatures.
Descriptors: genes viral, influenza A virus avian
genetics, RNA viral genetics, viral proteins genetics, base sequence, codon,
mutation, RNA, messenger, temperature, viral nonstructural proteins.
Roditi, I.J. and J.S. Robertson (1984). Nucleotide
sequence of the avian influenza virus A/Fowl Plague/Rostock/34 segment 1
encoding the PB2 polypeptide. Virus Research 1(1): 65-71. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Descriptors: avian influenza virus, nucleotide sequence,
RNA, polypeptide.
Roepke, D.C., S.M. Goyal, C.J. Kelleher, D.A.
Halvorson, A.J. Abraham, R.F. Freitas, and E.L. Cussler (1987). Use of
temperature-sensitive gel for concentration of influenza virus from infected
allantoic fluids. Journal of Virological Methods 15(1): 25-31. ISSN: 0166-0934.
NAL
Call Number: QR355.J6
Abstract: Cross-linked, poly(N-isopropylacrylamide) gel
was used to concentrate avian influenza virus from allantoic fluid. Placing the
gel in virus-infected allantoic fluid at 4 degrees C caused the gel to swell
and absorb small molecular weight solutes, while excluding avian influenza
virus and other large particles. Warming the gel to 37 degrees C or more caused
the gel to collapse. The gel remained functional after sterilization in an
autoclave and could be reused to concentrate other samples of allantoic fluid.
Using a combined concentration and elution technique, we were able to achieve
an average of 84.2% virus recovery, while reducing the fluid volume from 90 ml
to 7.6 ml.
Descriptors: allantois microbiology, fetal membranes
microbiology, influenza A virus avian isolation and purification, acrylic
resins, chick embryo, hydrogen-ion concentration, temperature.
Rogers, G.N. and B.L. D'Souza (1989). Receptor
binding properties of human and animal H1 influenza virus isolates. Virology
173(1): 317-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: It has been previously reported that several
human H1 influenza viruses isolated prior to 1956, in contrast to human H3
isolates which are quite specific for SA alpha 2,6Gal sequences, apparently
recognize both SA alpha 2,3Gal and SA alpha 2,6Gal sequences (Rogers, G.N., and
Paulson, J.C., Virology 127, 361-373, 1983). In this report human H1 isolates
representative of two epidemic periods, from 1934 to 1957 and from 1977 to
1986, and H1 influenza isolated from pigs, ducks, and turkeys were compared for
their ability to utilize sialyloligosaccharide structures containing terminal
SA alpha 2,3Gal or SA alpha 2,6Gal sequences as receptor determinants. Five of
the eight human isolates from the first epidemic period recognize both SA alpha
2,3Gal and SA alpha 2,6Gal linkages, in agreement with our previous results. Of
the remaining three strains, all isolated towards the end of the first
epidemic, two appear to prefer SA alpha 2,6Gal sequences while the third
preferentially binds SA alpha 2,3Gal sequences. In contrast to the early
isolates, 11 of 13 human strains isolated during the second epidemic period
preferentially bind SA alpha 2,6Gal containing oligosaccharides. On the basis
of changes in receptor binding associated with continued passage in the
laboratory for some of these later strains, it seems likely that human H1
isolates preferentially bind SA alpha 2,6Gal sequences in nature, and that
acquisition of SA alpha 2,3Gal-binding is associated with laboratory passage.
Influenza H1 viruses isolated from pigs were predominantly SA alpha
2,6Gal-specific while those isolated from ducks were primarily SA alpha
2,3Gal-specific. Thus, as has been previously reported for H3 influenza
isolates, receptor specificity for influenza H1 viruses appears to be
influenced by the species from which they were isolated, human isolates binding
preferentially to SA alpha 2,6Gal-containing oligosaccharides while those
isolated from ducks prefer SA alpha 2,3Gal-containing oligosaccharides.
However, unlike the SA alpha 2,6Gal-specific H3 isolates, binding to cell
surface receptors by the H1 influenza viruses is not sensitive to inhibition by
horse serum glycoproteins, regardless of their receptor specificity. These
results suggest that, while the H1 and H3 hemagglutinins appear to be subject
to similar host-derived selective pressures, there appear to be certain
fundamental differences in the detailed molecular interaction of the two
hemagglutinins with their sialyloligosaccharide receptor determinants.
Descriptors: influenza A virus avian metabolism, influenza
A virus human metabolism, influenza A virus, porcine metabolism, influenza A
virus metabolism, orthomyxoviridae metabolism, receptors, virus metabolism,
ducks, hemagglutination inhibition tests, hemagglutination tests, species
specificity, swine, turkeys.
Rogers, G.N. and J.C. Paulson (1983). Receptor
determinants of human and animal influenza virus isolates: differences in
receptor specificity of the H3 hemagglutinin based on species of origin. Virology
127(2): 361-73. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The binding of influenza virus to
erythrocytes and host cells is mediated by the interaction of the viral
hemagglutinin (H) with cell surface receptors containing sialic acid (SA). The
specificity of this interaction for 19 human and animal influenza isolates was
examined using human erythrocytes enzymatically modified to contain cell surface
sialyloligosaccharides with the sequence SA alpha 2,6Gal beta 1,4GlcNAc; SA
alpha 2,3Gal beta 1,4(3)GlcNAc; SA alpha 2,3Gal beta 1,3GalNAc; or SA alpha
2,6GalNAc. Although none of the viruses agglutinated cells containing the SA
alpha 2,6GalNAc linkage, differential agglutination of cells containing the
other three sequences revealed at least three distinct receptor binding types.
Several virus isolates exhibited marked receptor specificity, binding only to
cells containing the SA alpha 2,6Gal or the SA alpha 2,3Gal linkage, while
others bound equally well to cells containing either linkage. Moreover, some
viruses could distinguish between two oligosaccharide receptor determinants
containing the terminal SA alpha 2,3Gal linkage when present in the SA alpha
2,3Gal beta 1,4(3)GlcNAc sequence or the SA alpha 2,3Gal beta 1,3GalNAc
sequence binding cells containing only the former. The observed receptor
specificities were not significantly influenced by the viral neuraminidases as
shown by the use of the potent neuraminidase inhibitor
2-deoxy-2,3-dehydro-N-acetylneuraminic acid. Receptor specificity appeared, to
some extent, to be dependent on the species from which the virus was isolated.
In particular, human isolates of the H3 serotype all agglutinated cells
containing the SA alpha 2,6Gal linkage, but not cells bearing the SA alpha
2,3Gal beta 1,3GalNAc sequence. In contrast, antigenically similar (H3)
isolates from avian and equine species preferentially bound erythrocytes
containing the SA alpha 2,3Gal linkage. This is of particular interest in view
of the identification of the avian virus H3 hemagglutinin as the progenitor of
the H3 hemagglutinin present on the current human Hong Kong viruses.
Descriptors: hemagglutinins viral, influenza A virus
immunology, oligosaccharides metabolism, receptors, virus metabolism,
hemagglutination, viral, hemagglutinin glycoproteins, influenza virus,
influenza A virus avian immunology, influenza A virus human immunology,
influenza A virus, porcine immunology, neuraminidase metabolism, species
specificity.
Rogers, G.N., T.J. Pritchett, J.L. Lane, and J.C.
Paulson (1983). Differential sensitivity of human, avian, and equine
influenza A viruses to a glycoprotein inhibitor of infection: selection of
receptor specific variants. Virology 131(2): 394-408. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Human and animal (avian and equine) influenza
A virus isolates of the H3 serotype exhibit marked differences in their ability
to bind specific sialyloligosaccharide sequences that serve as cell surface
receptor determinants (G. Rogers and J. Paulson, 1983, Virology 127, 361-373).
Whereas human isolates of this subtype strongly agglutinate enzymatically
modified human erythrocytes containing the terminal SA alpha 2,6Gal sequence,
avian and equine isolates preferentially agglutinate erythrocytes bearing the
SA alpha 2, 3Gal sequence. As shown in this report, a glycoprotein found in
horse serum, alpha 2-macroglobulin, is a potent inhibitor of viral adsorption
to the cell surface for human H3 isolates. In contrast, avian and equine
isolates are poorly inhibited suggesting a correlation between receptor
specificity and inhibitor sensitivity. Growth of a human H3 isolate
(A/Memphis/102/72) on MDCK cells in the presence of horse serum resulted in an
overall shift in the virus receptor specificity from preferential binding of
the SA alpha 2,6Gal linkage to preferential binding of the SA alpha 2,3Gal
linkage characteristic of avian and equine isolates. Clonally isolated variants
of A/Memphis/102/72 grown in the presence or absence of horse serum exhibited
binding properties that account for those observed in the field isolates.
Clones which preferentially bound the SA alpha 2,6Gal linkage, like the parent
human virus, were very sensitive to inhibition of hemagglutination by horse
serum and equine alpha 2-macroglobulin. In contrast, receptor variants which
preferentially bound the SA alpha 2,3Gal linkage, like the avian and equine
isolate, were insensitive to such inhibitors. None of the variants was very
sensitive to inhibition of hemagglutination by human alpha 2-macroglobulin.
These results suggest that the presence, in vivo, of a glycoprotein inhibitor
such as equine alpha 2-macroglobulin could suppress infection of influenza
viruses bearing an H3 hemagglutinin with a SA alpha 2,6Gal specific, inhibitor
sensitive phenotype, allowing growth to predominance of a virus which is SA
alpha 2,3Gal specific and inhibitor insensitive as found in avian and equine
isolates.
Descriptors: glycoproteins antagonists and inhibitors,
influenza A virus avian drug effects, influenza A virus human drug effects,
influenza A virus drug effects, receptors, virus drug effects, viral proteins
antagonists and inhibitors, adsorption, chick embryo, ducks, erythrocytes
immunology, erythrocytes microbiology, hemagglutination inhibition tests,
hemagglutination tests, hemagglutinins viral analysis, horses, alpha
macroglobulins pharmacology.
Rohde, W., C.B. Boschek, E. Harms, R. Rott, and C.
Scholtissek (1979). Characterization of virus-like particles produced by an
influenza A virus. Archives of Virology 62(4): 291-302. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The influenza strain 413 1,1 segregated as a
stable recombinant during passage of the isolate 19/N which was obtained after
double infection of chick embryo fibroblasts by virus N and the fowl plague
virus (FPV) mutant ts 19. Its gene constellation was determined by molecular
hybridization. Upon infection of chick embryo cells by this recombinant strain,
two particle populations of high (H) and low (L) buoyant densities were
produced. By biological and biochemical parameters, the H-population (delta =
1.22 g/cm3) cannot be distinguished from standard infectious influenza virus.
In contrast, the noninfectious L-particles (delta = 1.14 g/cm3) lack all
virus-specific glycoproteins (HA, NA) as well as the matrix protein M and are
visualized by electron microscopy as spikeless particles. Significant changes
in the quantitative composition of the phospholipid bilayer are evident as
compared to the H-particles. In addition to the previously characterized eight
genes both populations contain a variety of smaller RNA fragments which
hybridize with complementary RNA and presumably represent degradation products
of full-length genes.
Descriptors: influenza A virus avian ultrastructure,
phospholipids analysis, RNA viral analysis, viral proteins analysis, virion
ultrastructure, chick embryo, fibroblasts, genes viral, influenza A virus avian
genetics, influenza A virus avian growth and development, mutation,
recombination, genetic, tissue culture, virus replication.
Rohde, W., E. Harms, and C. Scholtissek (1977). Biochemical
studies on influenza viruses. I. Comparative analysis of equine 2 virus and
virus N genes and gene products. Virology 79(2): 393-404. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus analysis, RNA viral
analysis, translation, genetic, base sequence,
electrophoresis, polyacrylamide gel, horses, influenza A virus avian,
influenza A virus isolation and purification, nucleic acid hybridization,
recombination, genetic, viral proteins analysis.
Rohde, W. and C. Scholtissek (1980). On the origin
of the gene coding for an influenze A virus nucleocapsid protein. Archives
of Virology 64(3): 213-23. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The gene coding for the nucleocapsid protein
NP of the influenza A virus recombinant strain 413 1,1 was characterized
biochemically by molecular hybridization and fingerprint analysis. The data
presented suggest that this NP gene has evolved by intracistronic recombination
between NP genes of virus N and the fowl plague virus temperature-sensitive
mutants ts 19.
Descriptors: capsid genetics, genes viral, influenza A virus
avian genetics, RNA viral genetics, viral proteins genetics, avian analysis,
mutation, nucleic acid hybridization, oligonucleotides analysis, peptides
analysis, viral analysis, recombination, genetic, temperature, viral proteins
analysis.
Rohm, C., T. Horimoto, Y. Kawaoka, J. Suss, and R.G.
Webster (1995). Do hemagglutinin genes of highly pathogenic avian influenza
viruses constitute unique phylogenetic lineages? Virology 209(2):
664-670. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Avian influenza A viruses of the H5 and H7
subtypes periodically cause severe outbreaks of disease in poultry. The
question we wished to address in this study is whether these highly pathogenic
strains constitute unique lineages or whether they and related nonpathogenic
viruses are derived from common ancestors in the wild bird reservoir. We
therefore compared the nucleotide and amino acid sequences of the hemagglutinin
(HA) genes of 15 H5 and 26 H7 influenza A viruses isolated over 91 years from a
variety of host species in Eurasia, Africa, Australia, and North America.
Phylogenetic analysis indicated that the HA genes of H5 and H7 viruses that
cause severe disease in domestic birds do not form unique lineages but share
common ancestors with nonpathogenic H5 and H7 viruses. These findings predict
that highly pathogenic avian H5 and H7 influenza A viruses will continue to
emerge from wild bird reservoirs. Another important question is whether H7
influenza viruses found in mammalian species are derived from avian strains. We
included eight equine influenza viruses and one seal isolate in the
phylogenetic analysis of H7 HA genes. We could show that the HA genes of both,
the equine and the seal viruses, shared ancestors with avian H7 HA genes. This
indicates that currently circulating H7 viruses with an avian HA gene may have
the potential to adapt to mammalian species and to cause an influenza outbreak
in the new host.
Descriptors: avian influenza virus, agglutinins, genes,
pathogenicity, phylogeny, nucleotide sequence, chemical composition, biological
properties, cell structure, chromosomes, evolution, genomes, influenza virus,
microbial properties, nucleus, orthomyxoviridae, proteins, viruses, viral
hemagglutinins, structural genes, amino acid sequences.
Rohm, C., J. Suss, V. Pohle, and R.G. Webster (1996).
Different hemagglutinin cleavage site variants of H7N7 in an influenza
outbreak in chickens in Leipzig, Germany. Virology 218(1):
253-7. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The hemagglutinin (HA) genes from four avian
H7N7 influenza A isolates, from a single outbreak, were shown to possess
different cleavage sites that contain varying numbers of basic amino acid
residues (KKKKR, KRKKR, KKRKKR, KKKKKKR). All four variants are highly pathogenic
in chickens and share an immediate common ancestral HA with
A/tern/Potsdam/342-6/79 (H7N7) and A/swan/Potsdam/63-6/81 (H7N7). These viruses
are nonpathogenic and contain no extra basic amino acids at the cleavage site
of their HA. During evolution a common precursor virus acquired different
sequences at the cleavage site of the HA and became highly pathogenic in
chickens. In vitro assays revealed that the HA from A/chicken/Leipzig/79 with
KKKKR at the cleavage site was only partially cleaved (41%), compared to
93-100% cleavage of the other HAs. Since all four viruses were highly
pathogenic in chickens, these findings confirm that the degree of pathogenicity
in vivo is not exclusively determined by the degree of HA cleavability.
Descriptors: chickens, disease outbreaks veterinary, fowl
plague virology, hemagglutinins viral metabolism, influenza A virus avian
metabolism, amino acid sequence, base sequence, DNA, viral, fowl plague
epidemiology, geese, Germany epidemiology, hemagglutinin glycoproteins, influenza
virus, hemagglutinins viral genetics, avian genetics, molecular sequence data,
phylogeny.
Rohm, C., N. Zhou, J. Suss, J. Mackenzie, and R.G. Webster (1996). Characterization
of a novel influenza hemagglutinin, H15: criteria for determination of influenza
A subtypes. Virology 217(2):
508-16. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Two viruses with a novel hemagglutinin (HA),
A/duck/Australia/341/83 and A/shearwater/West Australia/2576/79, have been
isolated from a duck and a shorebird in Australia. Hemagglutination inhibition
and double immunodiffusion assays failed to reveal cross-reactivity with any of
the known subtypes (H1 to H14). We therefore propose that these viruses
constitute a new HA subtype, H15. Sequence analysis of the HA genes confirmed
the serologic findings. When compared at the amino acid level, the HA1 region
of the H15 subtype differs from those of the other subtypes by 30% and more.
This degree of heterogeneity is also found among HA genes of other subtypes. Thus
we propose that amino acid sequence data should be evaluated when determining
the HA subtypes of influenza A viruses. Sequence comparison and phylogenetic
analysis suggested that the HA subtype H15 is most closely related to the H7.
Compared to the H7 HA, the H15 acquired a 30-nucleotide insertion within HA1 at
position 253 which is located in the globular head of the molecule. This
finding suggests that RNA recombination, although a rare event in nature, may
play an important role in the evolution of influenza viruses.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian classification, influenza A virus classification, amino acid
sequence, antigens, viral genetics, genes, structural, viral, hemagglutinins
viral genetics, avian immunology, influenza A virus immunology, molecular
sequence data, phylogeny, RNA viral genetics, sequence homology, amino acid,
sequence homology, nucleic acid.
Romanos, M.A. and A.J. Hay (1984). Identification
of the influenza virus transcriptase by affinity-labeling with pyridoxal
5'-phosphate. Virology 132(1): 110-7. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Pyridoxal 5'-phosphate (PLP), a reversible
inhibitor of in vitro transcription by fowl plaque virus, has been used to
identify the transcriptase. Kinetic analyses showed that PLP competitively
inhibits the addition of each nucleoside triphosphate in ApG-primed reactions,
suggesting that both initiation and elongation are affected. The irreversible
inhibition by PLP following reduction with borohydride was prevented by
preincubation with the first substrate: GTP in unprimed reactions or CTP in the
presence of ApG. On reaction of FPV proteins with PLP and [3H]borohydride the
core protein PB1 was preferentially labeled and the labeling was selectively
blocked by GTP or ApG + CTP. These data suggest that PB1 has the
nucleotide-binding site of the transcriptase, is responsible for both
initiation and elongation, and is apparently associated with the 3' ends of
template RNAs in virions.
Descriptors: influenza A virus avian enzymology, pyridoxal
phosphate pharmacology, reverse transcriptase inhibitors, affinity labels,
chick embryo, kinetics, transcription, genetic, viral core proteins, viral
proteins metabolism.
Romero, P.A., R. Datema, and R.T. Schwarz (1983). N-methyl-1-deoxynojirimycin,
a novel inhibitor of glycoprotein processing, and its effect on fowl plague
virus maturation. Virology 130(1): 238-42. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The glucose analogue
N-methyl-1-deoxynojirimycin was found to be a specific inhibitor of the
trimming of the outermost glucose residue of the N-linked
precursor-oligosaccharide Glc3Man9GlcNAc2, and therefore of oligosaccharide
processing, in fowl plague virus-infected chicken-embryo cells. The fowl plague
virus glycoproteins in N-methyl-1-deoxynojirimycin-treated cells contain
oligosaccharides of the composition Glc3ManxGlcNAc2 (x = 7, 8, and 9).
Inhibition of trimming of the outermost glucose residues does not prevent
release of infectious virus with oligosaccharides of the composition
Glc3Man7(GlcNAc)2. On the other hand inhibition of the trimming of the
innermost glucose residue does inhibit release of infectious virus (Datema, R.,
Romero, P. A., Legler, G., and Schwarz, R. T. Proc. Nat. Acad. Sci. USA 79,
6787-6791 (1982) ).
Descriptors: 1 deoxynojirimycin analogs and derivatives,
anti bacterial agents pharmacology, antiviral agents pharmacology, glucosamine
analogs and derivatives, glycoproteins antagonists and inhibitors, influenza A
virus avian drug effects, viral proteins antagonists and inhibitors, chick
embryo, glucosamine pharmacology, avian metabolism, oligosaccharides
antagonists and inhibitors, virion drug effects, virion metabolism.
Ronda, E., A. Garcia Gancedo, L. Alonso, P. Vilas,
and L. Lucas (1966). Killed fowl plague virus vaccine obtained from chick
embryo cells. Microbiologia Espanola 19(3): 257-80. ISSN: 0026-2595.
NAL
Call Number: 448.3 M583
Descriptors: influenza A virus avian, viral vaccines,
virus cultivation, chick embryo, chickens, HeLa cells, orthomyxoviridae
infections immunology, tissue culture, vaccination.
Rosenbergova, M., E. Matisova, and S. Pristasova
(1971). Endonuclease activities of myxo- and paramyxoviruses. Acta
Virologica 15(6): 515-8. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: influenza A virus avian enzymology, Newcastle
disease virus enzymology, orthomyxoviridae enzymology, parainfluenza virus 1,
human enzymology, centrifugation, density gradient, chick embryo, chlorides,
hydrogen-ion concentration, avian metabolism, magnesium, Newcastle disease
virus metabolism, orthomyxoviridae metabolism, parainfluenza virus 1, human
metabolism, perchloric acid, phosphorus isotopes, precipitation, RNA, ribosomal
analysis, ribosomal metabolism, ribonucleases metabolism, solubility, sucrose,
temperature.
Rosenbergova, M. and S. Pristasova (1972). Nuclease
activity of large RNA viruses. Acta Virologica 16(1): 1-8. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: leukosis virus, avian enzymology,
orthomyxoviridae enzymology, ribonucleases metabolism, carcinoma, ehrlich
tumor, cattle, chick embryo, DNA metabolism, deoxyribonucleases metabolism,
influenza A virus avian enzymology, leukosis virus, avian isolation and
purification, Newcastle disease virus enzymology, nucleic acid denaturation,
orthomyxoviridae isolation and purification, parainfluenza virus 1, human
enzymology, paramyxoviridae enzymology, paramyxoviridae isolation and
purification, polynucleotides metabolism, RNA, neoplasm isolation and
purification, neoplasm metabolism, species specificity, temperature, thymus
gland, tissue culture, virus cultivation.
Rott, R. (1980). Genetic determinants for infectivity
and pathogenicity of influenza viruses. Philosophical Transactions of
the Royal Society of London. Series B Biological Sciences 288(1029):
393-9. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Abstract: The objective of the studies presented was to
define a molecular basis for infectivity and pathogenicity of influenza virus.
It is demonstrated that activation of the HA glycoprotein by post-translational
proteolytic cleavage is indispensable for the formation of infectious influenza
virus. There are two preconditions for influenza virus to be pathogenic: (1)
the presence on the virus particle of a cleaved HA molecule essential for the
infectivity, and (2) an optimal genome composition. In naturally occurring
avian influenza viruses there is a direct correlation between the cleavability
of the haemagglutinin, the potential of the virus to be produced in infectious
form in a wide range of host cells, and the viruses' pathogenicity for chicken.
It is concluded that Nature selects an optimal gene constellation for each
individual field strain. In these viruses the structure of the haemagglutinin
is the determining factor for pathogenicity.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, avian pathogenicity, protein precursors metabolism,
structure activity relationship, viral proteins genetics.
Rott, R. (1985). In vitro Differenzierung von
pathogenen und apathogenen aviaren Influenzaviren. [In vitro differentiation of
pathogenic and nonpathogenic avian influenza viruses]. Berliner Und
Munchener Tierarztliche Wochenschrift 98(2): 37-9. ISSN: 0005-9366.
NAL
Call Number: 41.8 B45
Descriptors: influenza A virus avian classification,
microbiological techniques veterinary, chick embryo, fibroblasts,
hemagglutination tests, avian pathogenicity, plaque assay veterinary, tissue
culture, virulence, virus cultivation.
Rott, R. (1992). The pathogenic determinant of
influenza virus. Veterinary Microbiology 33(1-4): 303-10. ISSN: 0378-1135.
NAL
Call Number: SF601.V44
Abstract: Influenza viruses, like other viruses, must
exhibit a genome constellation, which permits optimal virus reproduction in a
given host. Besides this prerequisite the influenza virus haemagglutinin
glycoprotein (HA) has been shown to be an essential determinant for
pathogenicity. HA, which is synthesized as a precursor molecule, is activated
by posttranslational cleavage by host proteases to obtain its full biological
properties. Proteolytic activation is therefore indispensable for effective
virus spread in the infected host and thus for pathogenicity. HA of the highly
pathogenic avian influenza viruses inducing a systemic infection in birds is
cleaved in a broad range of different host cells. On the other hand, HA of all
mammalian viruses and the nonpathogenic avian strains, which cause local
infection, exhibit a restricted cleavability. The prime determinant for these
differences has been found to be the structure of the cleavage site. This
concept was corroborated on virus mutants adapted in vitro to a new host.
Descriptors: hemagglutinins viral immunology,
orthomyxoviridae pathogenicity, viral envelope proteins immunology, amino acid
sequence, base sequence, hemagglutinin glycoproteins, influenza virus,
hemagglutinins viral chemistry, hemagglutinins viral genetics, molecular
sequence data, mutagenesis, insertional, orthomyxoviridae genetics,
orthomyxoviridae immunology, RNA, ribosomal, 28S chemistry, viral envelope
proteins chemistry, viral envelope proteins genetics.
Rott, R. (1977). The structural basis of the
function of influenza virus glycoproteins. Medical Microbiology and
Immunology 164(1-3): 23-33. ISSN:
0300-8584.
Descriptors: hemagglutinins viral analysis, neuraminidase
analysis, neuraminidase immunology, orthomyxoviridae enzymology, glycopeptides
analysis, influenza A virus avian enzymology, avian immunology, avian
ultrastructure.
Rott, R., H. Becht, and Orlich (1975). Antigenic
relationship between the surface antigens of avian and equine influenze
viruses. Medical Microbiology and Immunology 161(4): 253-61. ISSN: 0300-8584.
Abstract: Influenza virus Equine 1 (A/equine/Prague/56)
has a hemagglutinin which is antigenically related to the hemagglutinin of fowl
plague virus strain Rostock (FPV) and a neuraminidase which cross-reacts with
the enzyme of virus N (A/chick/Germany/49). After a single injection of
chickens with Equine 1 virus no hemagglutination inhibiting (HI) and
neutralizing antibodies against FPV can be demonstrated, although the birds are
fully protected against a lethal dose of FPV. HI and neutralizing antibodies
against FPV appear after a second injection of Equine 1 virus several weeks
after the first one. Liberation of newly sunthesized FPV from the host cell is
ingibited by antibodies cross-reacting with any antigen of virus surface.
Descriptors: antigens, viral administration and
dosage, arteritis virus, equine
immunology, influenza A virus avian immunology, RNA viruses immunology, binding
sites, antibody, epitopes, fluorescent antibody technique, hemadsorption,
hemagglutination inhibition tests, hemagglutination tests, hemagglutinins viral
isolation and purification, injections, intravenous, neuraminidase analysis,
neutralization tests, plaque assay.
Rott, R., H. Becht, and M. Orlich (1974). The
significance of influenza virus neuraminidase in immunity. Journal of
General Virology 22(1): 35-41. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: antibody formation, antigens, viral, fowl
plague immunology, influenza A virus avian immunology, neuraminidase analysis,
orthomyxoviridae immunology, chickens immunology, hemagglutination inhibition
tests, hemagglutinins viral analysis, immune sera, immunization, influenza
veterinary, avian enzymology, neutralization tests, orthomyxoviridae
enzymology, rabbits immunology, swine, swine diseases microbiology.
Rott, R. and H.D. Klenk (1973). Biosynthese des
Hamagglutinins eines Influenzavirus (Virus der Klassischen Geflugelpest.
[Hemagglutinin biosynthesis in an influenza virus (fowl plague virus)]. Zentralblatt
Fur Veterinarmedizin. Reihe B Journal of Veterinary Medicine. Series B
20(7): 509-21. ISSN: 0514-7166.
NAL
Call Number: 41.8 Z52
Descriptors: antibodies, viral biosynthesis,
hemagglutination tests, influenza A virus avian immunology, chickens, tissue
culture, virus cultivation.
Rott, R., H.D. Klenk, and C. Scholtissek (1984). Bedeutung
des Hamagglutinins fur die Pathogenitat aviarer Influenzaviren. [Significance
of hemagglutinins for the pathogenicity of avian influenza viruses]. Zentralblatt
Fur Bakteriologie, Mikrobiologie, Und Hygiene. Series A, Medical Microbiology,
Infectious Diseases, Virology, Parasitology 258(2-3): 337-49. ISSN: 0176-6724.
NAL
Call Number: 448.3 C33 (1)
Abstract: In addition to acute viral diseases,
persistent infections have attained considerable interest in recent years. Such
persistent infections are characterized by extended time periods in which the
infecting virus remains within the organism before the eventual appearance of
manifest symptoms. These infections may be evoked by a variety of virus species
resulting in a diversity of pathogenic reactions and clinical manifestations.
The mechanisms of viral persistence, where known, also appear to be quite
diverse. As far as space permits, some examples of persistent infections will be
presented and the mechanisms of the pathogenesis of the resulting diseases will
be discussed.
Descriptors: hemagglutinins viral analysis, hemagglutinins
viral genetics, hemagglutinins viral immunology, influenza A virus avian
pathogenicity, amino acid sequence, cell membrane microbiology, chick embryo,
fetal membranes microbiology, genes viral, avian genetics, avian growth and
development, avian ultrastructure, models, molecular, mutation, virulence.
Rott, R., M. Orlich, and C. Scholtissek (1976). Attenuation
of pathogenicity of fowl plague virus by recombination with other influenza A
viruses nonpathogenic for fowl: nonexculsive dependence of pathogenicity on
hemagglutinin and neuraminidase of the virus. Journal of Virology
19(1): 54-60. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: A number of antigenic hybrids of influenza A
viruses were produced possessing either the hemagglutinin or the neuraminidase
of fowl plague virus and the corresponding antigen derived from another
influenza A virus. Other recombinants were obtained carrying both surface
antigens of fowl plague virus but differing from the parent in certain
biological properties. None of the recombinants isolated were pathogenic for
adult chickens. Most recombinants obtained after crosses between reciprocal
recombinants carrying both fowl plague virus surface antigens were also
apathogenic for chickens. Using the same parent recombinants for double
infection some of the progeny "back-recombinants" were pathogenic,
whereas others were not. From these results it is concluded that the surface
components do not by themselves determine the pathogenicity of influenza A
viruses.
Descriptors: hemagglutinins viral analysis, influenza A
virus avian pathogenicity, neuraminidase immunology, orthomyxoviridae
pathogenicity, recombination, genetic, chick embryo, crosses, genetic, avian
enzymology, avian immunology, neuraminidase analysis, orthomyxoviridae
enzymology, orthomyxoviridae immunology.
Rott, R., M. Orlich, and C. Scholtissek (1979). Correlation
of pathogenicity and gene constellation of influenza A viruses. III.
Non-pathogenic recombinants derived from highly pathogenic parent strains. Journal
of General Virology 44(2): 471-7.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: We have demonstrated by recombination of two
highly pathogenic avian influenza viruses [A/FPV/Rostock (Hav1N1) x
A/turkey/England/63 (Hav1Nav3)] that recombinants can be isolated which are
pathogenic as well as non-pathogenic for chickens. They carried the glycoproteins
of either parent strains, and all are produced in infectious form in chick
embryo cells. Genetic analysis revealed that the non-pathogenic recombinants
possess a mixed RNA polymerase complex, consisting of pol 1, pol 2, ptra and NP
gene products, while, with one exception, the pathogenic recombinants have the
genes coding for the polymerase activity from one or other parent virus. The
biological properties of the recombinant viruses did not correlate with their
pathogenicity for chickens.
Descriptors: genes viral, influenza A virus avian
genetics, recombination, genetic, chickens, DNA directed RNA polymerases
genetics, fowl plague microbiology, avian pathogenicity, neuraminidase
genetics, turkeys.
Rott, R., M. Orlich, and C. Scholtissek (1982). Differences
in the multiplication at elevated temperature of influenza virus recombinants
pathogenic and nonpathogenic for chicken. Virology 120(1):
215-24. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: chickens microbiology, influenza A virus
avian pathogenicity, recombination, genetic, cell line, chick embryo, DNA
directed RNA polymerases genetics, genes viral, avian genetics, avian growth
and development, plaque assay, temperature.
Rott, R., M. Orlich, and C. Scholtissek (1981). Intrinsic
interference between swine influenza and fowl plague virus. Archives of
Virology 69(1): 25-32. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Multiplication of swine influenza (SW) virus
is inhibited by fowl plaque virus (FPV) at the level of RNA synthesis when host
cells are infected with both viruses at a high multiplicity of infection. Under
these conditions reassortment between the two viruses cannot be detected. The
inhibitory effect of FPV is highly reduced and recombinants between the two
viruses could be obtained when the cells were superinfected with FPV 1--2 hours
after infection with SW virus, or after simultaneous infection with a low
multiplicity of infection. The phenomenon is compatible with the intrinsic
interference.
Descriptors: influenza A virus avian growth and
development, porcine growth and development, influenza A virus growth and
development, viral interference, antigens, viral genetics, cell line, chick
embryo, dogs, hybridization, genetic, avian genetics, porcine genetics, kidney,
tissue culture, virus replication.
Rott, R., M. Reinacher, M. Orlich, and H.D. Klenk
(1980). Cleavability of hemagglutinin determines spread of avian influenza
viruses in the chorioallantoic membrane of chicken embryo. Archives of Virology 65(2):
123-33. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The spread of infection in the
chorioallantoic membrane (CAM) has been analysed with pathogenic and
non-pathogenic avian influenza A viruses. After allantoic inoculation of
pathogenic strains, high titers of infectious virus were found in the allantoic
fluid, and virus growth could be demonstrated by immunohistology and electron
microscopy in the allantoic epithelium, the mesenchyma, and in the chorionic
epithelium. By the same route of inoculation, non-pathogenic strains yielded
also higher titers of infectious virus in the allantoic fluid, but virus
replication was restricted to the allantoic epithelium and did not occur in the
other cell layers. After chorionic inoculation of pathogenic strains,
replication occurred in all layers of the CAM, and infectious virus was
released into the allantoic fluid. However, when the chorionic epithelium was
infected with a non-pathogenic strain, infection did not spread beyond the site
of inoculation. These differences in virus spread are based on differential
activation of the hemagglutinin by proteolytic cleavage. The hemagglutinin of
pathogenic strains is cleaved in cells of each layer, whereas the hemagglutinin
of non-pathogenic strains is cleaved only in the allantoic epithelium. In
epithelial cells, virus budding occurred nearly exclusively at the apical side
of the cell surface, but this polarization of virus maturation was found with
both pathogenic and nonpathogenic strains, indicating that it does not account
for the differences in virus spread and, thus, in pathogenicity.
Descriptors: fetal membranes microbiology, hemagglutinins
viral, influenza A virus avian growth and development, virus replication,
allantois microbiology, chick embryo, chorion microbiology, epithelium
microbiology, avian immunology, avian pathogenicity, tissue culture, virulence.
Rott, R. and C. Scholtissek (1968). Biochemical
studies on influenza virus multiplication at reduced temperatures. Journal
of General Virology 3(2): 239-45.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian, virus replication,
carbon isotopes, complement fixation tests, cycloheximide pharmacology,
cytopathogenic effect, viral, neuraminidase metabolism, RNA biosynthesis,
temperature, tissue culture, uridine metabolism.
Rott, R. and C. Scholtissek (1967). Multiplication
of myxoviruses. Modern Trends in Medical Virology 1(0): 25-48. ISSN: 0544-6856.
Descriptors: orthomyxoviridae growth and development,
virus replication, antigens, viral, chick embryo, DNA biosynthesis,
dactinomycin pharmacology, defective viruses, hemagglutinins viral, inclusion
bodies, viral, influenza A virus avian growth and development, neuraminidase
biosynthesis, neuraminidase pharmacology, Newcastle disease virus growth and
development, phagocytosis, RNA viral biosynthesis, viral proteins biosynthesis.
Rott, R. and C. Scholtissek (1970). Specific
inhibition of influenza replication by alpha-amanitin. Nature
228(5266): 56. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: mycotoxins pharmacology, orthomyxoviridae
drug effects, virus replication drug effects, depression, chemical, influenza A
virus avian, leucine metabolism, Newcastle disease virus, orthomyxoviridae
metabolism, RNA viral biosynthesis, tritium, uridine metabolism, viral proteins
biosynthesis.
Rousset, J., M. Cherbonnel, M.O. Le Bras, and V.
Jestin (2003). Experimental challenge model with low pathogenic H7N1 avian
influenza virus to assess protection against infection by these viruses. British
Poultry Science 44(5): 830-1. ISSN:
0007-1668.
NAL
Call Number: 47.8 B77
Descriptors: avian influenza virus, low pathogenic H7N1,
experimental challenge, model, protection.
Rovnova, Z.I., E.I. Isaeva, A.L. Platonova, and P.N.
Kosiakov (1989). Antigenno-geneticheskie sviazi virusov grippa cheloveka i
zhivotnykh. [Antigenic-genetic connections between human and animal influenza
viruses]. Voprosy Virusologii 34(5): 553-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A comparative immunological analysis of the
composition of antigenic determinants (AGD) in hemagglutinins of human
influenza A virus (HIAV) of the serosubtypes H1, H2, H3, and in hemagglutinins
of animal influenza viruses (AIV) of the serosubtypes H1, H3-H6, H8-H11 with 25
polyclonal highly active sera was demonstrated. Using original monospecific mon
AGD in HIAV and AIV hemagglutinins was demonstrated. Using original
monospecific antibodies to individual AGD, those AGD contributing to similarity
and differences between HIAV and AIV were determined. It was found that
influenza A. virus strains isolated from man in the USSR in 1986 were identical
in the antigenic structure of hemagglutinin with that isolated from a tern in
1973 (A/tern/Turkmenistan/18/73).
Descriptors: epitopes, genes viral, influenza A virus
avian immunology, human immunology, antigens, viral immunology, cross
reactions, hemagglutination tests, hemagglutinins viral genetics,
hemagglutinins viral immunology, avian genetics, human genetics, neuraminidase
genetics, neuraminidase immunology, species specificity.
Rudneva, I.A., V.P. Kovaleva, N.L. Varich, V.R.
Farashyan, L.V. Gubareva, S.S. Yamnikova, I.A. Popova, V.P. Presnova, and N.V.
Kaverin (1993). Influenza A virus reassortants with surface glycoprotein
genes of the avian parent viruses: effects of HA and NA gene combinations on
virus aggregation. Archives of Virology 133(3-4): 437-50. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A series of 33 human-avian and human-mammalian
influenza virus reassortant clones possessing either HA or both HA and NA genes
of the avian or mammalian virus was obtained by crosses of A/USSR/90/77 (H1N1)
human virus with 5 avian and 1 mammalian influenza virus strains. All of the
reassortants possessing NA genes of the H1N1 human parent virus and HA gene of
an avian or mammalian parent virus had high values of infectivity/HA activity
ratio. Since this feature could result from a limited virion aggregation,
several reassortants were analyzed by velocity sucrose gradient centrifugation.
In all cases tested, the reassortants of H3N1, H4N1, H10N1 and H13N1
composition were shown to be aggregated, whereas the preparations of the parent
H1N1 virus and the reassortants possessing both HA and NA genes from the avian
parents were represented mostly by single virions. The aggregates were formed
at 4 degrees C and dissociated at 37 degrees C. The dissociation was blocked by
an inhibitor of neuraminidase activity (2-deoxy-2,3-dehydro-N-acetyl-neuraminic
acid). The dissociation was reversible since the virions reaggregated at 4
degrees C; however, treatment with bacterial neuraminidase led to an
irreversible dissociation of the aggregates. The tendency of the reassortants
to aggregate correlates with an increased infectivity/HA ratio. No regular
decrease in the neuraminidase activity in the virions of reassortants as
compared to the parent H1N1 virus was revealed. The most likely explanation of
the observed phenomenon seems to be an inefficient removal of sialic acid
residues from the avian virus hemagglutinin by the human virus N1
neuraminidase.
Descriptors: influenza A virus genetics, membrane
glycoproteins genetics, reassortant viruses genetics, viral proteins genetics,
chick embryo, chickens, ducks, electrophoresis, polyacrylamide gel, genes
viral, hemagglutination, viral, hemagglutinins viral genetics, avian genetics,
avian physiology, human genetics, human physiology, influenza A virus
physiology, neuraminidase genetics, neuraminidase pharmacology, RNA viral
analysis, reassortant viruses physiology, recombination, genetic drug effects,
temperature, whales.
Rudneva, I.A., N.L. Varich, N.V. Makarova, E.A.
Kropotkina, and S.S. Iamnikova (2000). Gennyi analiz i fenotipicheskaia
kharakteristika vysokoreproduktivnykh reassortantov, soderzhashchikh gen
gemaggliutinina virusa grippa ptits podtipa H2. [Gene analysis and phenotypic
characteristic of highly-reproductive reassortants, containing the gene for
bird influenza virus subtype H2 hemagglutinin]. Voprosy Virusologii
45(1): 20-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A series of reassortant clones with antigenic
formulae H2N1 and H2N3 were produced by genetic reassortment performed with the
use of an avian influenza virus, A/Pintail Duck/Primorie/695/76 (H2N3) and a
high-yield reassortant strain X-67. Preliminary identification of the parent
origin of NP and NS genes for 5 reassortants was performed by comparison of the
mobilities of virus-specific proteins in polyacrylamide gel electrophoresis.
The parent origin of genes of internal and nonstructural proteins for 3
reassortants was identified by partial sequencing. Although the genes of
internal and nonstructural proteins of the reassortants originated from
high-yield X-67 virus, only H2N3 reassortants were similar to the high-yield
parent virus as concerns the level of the virus accumulation evaluated by
hemagglutination titration and measurement of the virus protein content.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian genetics, reassortant viruses genetics,
birds, electrophoresis, polyacrylamide gel, phenotype.
Rudneva, I.A., N.L. Varich, N.V. Makarova, Y.A.
Kropotkina, and S.S. Yamnikova (2000). Gene analysis and phenotypical
characteristics of highly productive reassortants containing hemagglutinin gene
of subtype H2 avian influenza virus. Voprosy Virusologii 45(1):
20-24. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A series of reassortant clones with antigenic
formulae H2N1 and H2N3 were produced by genetic reassortment performed with the
use of an avian influenza virus, A/Pintail Duck/Primorie/695/76 H2N3) and a
high-yield reassortant strain X-67. Preliminary identification of the parent
origin of NP and NS genes for 5 reassortants was performed by comparison of the
mobilities of virus-specific proteins in polyacrylamide gel electrophoresis.
The parent origin of genes of internal and nonstructural proteins for 3
reassortants was identified by partial sequencing. Although the genes of
internal and nonstructural proteins of the reassortants originated from
high-yield X-67 virus, only H2N3 reassortants were similar to the high-yield
parent virus as concerns the level of the virus accumulation evaluated by
hemagglutination titration and measurement of the virus protein content.
Descriptors: molecular genetics, gene analysis analytical
method, genetic reassortment phenotypes, viral genetics.
Russell, R.J., S.J. Gamblin, L.F. Haire, D.J.
Stevens, B. Xiao, Y. Ha, and J.J. Skehel (2004). H1 and H7 influenza
haemagglutinin structures extend a structural classification of haemagglutinin
subtypes. Virology 325(2):
287-96. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Comparing the structures of H3, H5 and H9
subtype haemagglutinins, we deduced a structural basis for including all 15
influenza subtypes in four clades. H3, H5 and H9 represent three of these
clades; we now report the structure of an H7 HA as a representative of the
fourth clade. We confirm the structure of the turn at the N-terminus of the
conserved central alpha-helix of HA2, and the combination of ionisable residues
near the "fusion peptide" as clade-specific features. We compare the
structures of three H1 HAs with H5 HA in the same clade, to refine our previous
classification and we confirm the division of the clades into two groups of
two. We also show the roles of carbohydrate side chains in the esterase-fusion
domain boundaries in the formation of clade-specific structural markers.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, hemagglutinin glycoproteins, influenza virus classification,
influenza A virus chemistry, influenza A virus classification, amino acid
sequence, carbohydrates chemistry, crystallography, x-ray, hemagglutinin glycoproteins,
influenza virus genetics, influenza A virus genetics, models, molecular,
molecular sequence data, phylogeny, protein structure, quaternary, protein
structure, tertiary, sequence homology, amino acid.
Russi Cahill, J.C., M.C. Mogdasy, R.E. Somma Moreira,
and M.H. de Peluffo (1975). Counterimmunoelectrophoresis with influenza
antigens. I. Use of avian plague virus to detect type-specific antibodies to
influenza A in human sera. Journal of Infectious Diseases 131(1):
64-6. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: Avian plague virus was used as antigen in a
counterimmunoelectrophoresis technique. This virus was selected because it
detects only type-specific influenza A antibodies in human sera, avoiding the
possible interference of other antigens with anodic migration. The results with
reference sera, as well as the correlation of positive sera found by
counterimmunoelectrophoresis and complement fixation with the proposed antigen,
in the absence of other types of antibodies to fowl plague virus antigen,
support the conclusion that the counterimmunoelectrophoresis technique reveals
type-specific antibodies. The test is more sensitive than immunodiffusion but
less sensitive than complement fixation. Its sensitivity, simplicity, and
rapidity make it suitable for serologic surveys of human influenza A.
Descriptors: antibodies, viral analysis, antigens, viral,
immunoelectrophoresis, influenza immunology, influenza A virus avian
immunology, antibody specificity, chick embryo, complement fixation tests,
guinea pigs immunology, immune sera,
immunodiffusion.
Ruttkayova Nedecka, S. and G. Russ (1977). Effect
of a proteolytic enzyme inhbitor on influenza virus replication. Acta
Virologica 21(1): 79-81. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: N-tosyl-L-phenylalanyl chloromethane patially
inhibited the multiplicatiion of fowl plague virus (FPV) in infected cells. The
capacity of the inhibitor to suppress the muliplication of FPV depended on the
host cell system.
Descriptors: influenza A virus avian drug effects, virus
replication drug effects, cultured cells, avian growth and development,
tosylphenylalanyl chloromethyl ketone pharmacology.
Sadykhova, F.E. (1982). Antitela k virusam grippa
u ptits. [Antibodies to influenza viruses in poultry]. Voprosy
Virusologii 27(2): 218-20. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Determination of antibodies to influenza
viruses in chicken sera by radial hemolysis technique using normal horse serum
as the source of complement is described. This test was shown to be also very
sensitive and standard with mammal sera when some strains, including the
A/Khabarovsk/77, were tested.
Descriptors: antibodies, viral analysis, chickens
immunology, influenza A virus immunology, hemolytic plaque technique, influenza
A virus avian immunology, Newcastle disease virus immunology.
Saito, T., Y. Kawaoka, and R.G. Webster (1993). Phylogenetic
analysis of the N8 neuraminidase gene of influenza A viruses. Virology
193(2): 868-76. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Phylogenetic analysis of the N8 neuraminidase
(NA) genes from 18 influenza A viruses, representing equine and avian hosts in
different geographic locations, revealed three major lineages: (i) currently
circulating equine 2 viruses; (ii) avian viruses isolated in the Eurasian
region, including A/Equine/Jilin/1/89, a recent avian-like N8 isolate found in
horses in China; and (iii) avian viruses isolated in North America. Comparison
of mutation rates indicated that avian N8 genes have evolved more slowly than
their equine counterparts. That is, in both avian lineages, 72% of the
nucleotide changes were silent in the terminal branches of the phylogenetic
tree, whereas in equine 2 viruses, 59% of the nucleotide changes were silent.
This suggests greater selective pressure on the NA gene from the mammalian
immune system, leading to progressive evolution. Alternatively, the slower
mutation rate for avian N8 genes could reflect a selective advantage gained
from a longer, continuous span of evolution. The shape of the phylogenetic
tree, the evolutionary rate, and the calculated date of origin for the N8
equine 2 virus lineage were comparable to findings for the equine 2 virus
hemagglutinin (HA) gene (Bean et al., J. Virol. 66, 1129-1138, 1992). This
suggests that both viral membrane glycoproteins of equine 2 viruses have
evolved together and have been subjected to similar levels of selective
pressure. Several amino acid residues were found to differ among the three
host-specific lineages, but they may not be involved in host restriction of the
NA, as they are shared by EQ/Jilin/1/89 and viruses of avian origin. The
present findings complement detailed structural information on the N2 and N9
subtypes and should prove valuable in understanding future X-ray diffraction
studies of N8 crystals.
Descriptors: genes, structural, viral, influenza A virus
genetics, neuraminidase genetics, phylogeny, amino acid sequence, base
sequence, cloning, molecular, ducks, Escherichia coli genetics, horses,
influenza A virus avian classification, avian enzymology, avian genetics,
influenza A virus classification, influenza A virus enzymology, models,
molecular, molecular sequence data, mutation, neuraminidase chemistry, protein
structure, secondary, RNA viral genetics, RNA viral isolation and purification,
sequence homology, amino acid, sequence homology, nucleic acid.
Saito, T., W. Lim, and M. Tashiro (2004). Attenuation
of a human H9N2 influenza virus in mammalian host by reassortment with an avian
influenza virus. Archives of Virology 149(7): 1397-407. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: In order to develop a surrogate virus strain
for production of an inactivated influenza vaccine against a human H9N2 virus,
A/Hong Kong/1073/99 (HK1073: H9N2) was co-infected in embryonated chicken eggs
with an apathogenic avian influenza virus, A/Duck/Czechoslovakia/56 (Dk/Cz:
H4N6), for gene segment reassortment. Multiple-gene reassortants obtained were
examined for replication in mammalian hosts in vitro and in vivo by infecting
MDCK cells and by intranasal administration to hamsters, respectively. A 2-6
gene reassortant with both surface glycoproteins of HK1073 origin and the rest
of Dk/Cz origin, HK/CZ-13, was shown to replicate poorly in the mammalian hosts
both in vivo and in vitro comparing with HK1073, although this reassortant
replicated as efficiently as each parental strain in embryonated eggs. No
sequence difference was observed in the HA1 region between HK1073 and HK/CZ-13,
indicating that the reassortant would be equivalent in its immunogenicity to
the parental HK1073 strain when it is used as an inactivated vaccine. A virus
strain with attenuation in mammalian hosts is preferable for production of an
H9 vaccine, since it should reduce the risk of manufacturing-related infections
of employees during the vaccine production. HK/CZ-13 can therefore be a
surrogate strain for production of an inactivated vaccine as well as diagnostic
antigens in case of a possible future pandemic caused by an HK1073-like H9
influenza virus.
Descriptors: influenza A virus, avian genetics, human
genetics, influenza vaccines, reassortant viruses genetics, reassortant viruses
physiology, administration, intranasal, cell line, chick embryo, DNA
complementary chemistry, DNA complementary isolation and purification,
hamsters, hemagglutinin glycoproteins, influenza virus immunology, avian
pathogenicity, avian physiology, human pathogenicity, human physiology,
mesocricetus, neuraminidase immunology, RNA, viral isolation and purification,
viral metabolism, reassortant viruses immunology, reassortant viruses
pathogenicity, reverse transcriptase polymerase chain reaction, sequence
analysis, specific pathogen free organisms, vaccines, attenuated, virus
replication.
Saito, T., G. Taylor, W.G. Laver, Y. Kawaoka, and
R.G. Webster (1994). Antigenicity of the N8 influenza A virus neuraminidase:
existence of an epitope at the subunit interface of the neuraminidase. Journal
of Virology 68(3): 1790-6. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: To locate antigenic epitopes on the N8
neuraminidase (NA), we generated a panel of 97 monoclonal antibodies (MAbs), 66
of which inhibited NA activity (NI antibodies). Three groups of NI MAbs were
identified from their different reactivities with escape mutants. Group 1
antibodies recognized the peptide loop containing residues 344 to 346, which
appears to be an immunodominant region on the rim of the enzyme center of the
N8 NA. Group 2 antibodies recognized a novel epitope containing residues 150,
199, 367, 399, and 400 (N2 numbering). From the location of these residues on
the three-dimensional structure of the N8 NA, the epitope appears to be located
at the interface of two adjacent monomers in the tetrameric NA, one
contributing residues 150 and 199 and the other contributing residues 367 and
399 to 400. The available evidence indicates that the MAbs of this group react
with the NA only after it is fully assembled. The third group of antibodies
recognized the peptide loops containing residues 367 and 399 to 400. All of the
amino acid substitutions in N8 escape mutants which affect the NI activity of
antibodies were located in the peptide loops known to form epitopes in the N2
and N9 subtypes, indicating that antigenic regions in the NA head inducing NI
antibodies appear to be similar among different subtypes of influenza A
viruses. The MAbs used in this study will be valuable in studying the role of each
N8 NA epitope in host immune defense systems and in the kinetics analysis of
the biosynthesis of the enzyme.
Descriptors: antibodies, viral immunology, epitopes
immunology, influenza A virus avian immunology, neuraminidase immunology,
amidohydrolases metabolism, antibodies, monoclonal, antibodies, viral
classification, base sequence, avian enzymology, avian genetics, models,
molecular, molecular sequence data, mutation genetics, precipitin tests,
sequence analysis, structure activity relationship.
Saito, T., G. Taylor, and R.G. Webster (1995). Steps
in maturation of influenza A virus neuraminidase. Journal of Virology
69(8): 5011-7. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract:
We have studied the maturation of the
influenza A virus neuraminidase (NA), using monoclonal antibodies (MAbs) with
different conformational specificities against the head domains of the N8 NA.
The results obtained with radioimmunoprecipitation, together with previously
published information, suggest the following steps in maturation of this
molecule. First, the folding of the nascent NA leads to formation of the
epitope recognized by MAb N8-10, a step that depends on the formation of
intramolecular disulfide bonds. Second, monomers form dimers by an
intermolecular disulfide linkage in the stalk, with a t1/2 of 2.5 min. Third,
the epitope recognized by MAb N8-82 appears after dimerization, suggesting that
oligomeric NAs may undergo conformational change with a t1/2 of 8 min. Finally,
a tetramer-specific epitope recognized by MAb N8-4 appears on the NA with a
t1/2 of 13 min. Epitope detection by MAb N8-4 was inhibited by tunicamycin
treatment, suggesting that glycosylation of this molecule is required for proper
tetramerization. Each of these proposed steps occurs in the endoplasmic
reticulum of host cells, as demonstrated by treatment of virus-infected cells
with brefeldin A or carbonyl cyanide m-chlorophenylhydrazine; subsequently,
tetrameric NA is transported to the Golgi apparatus, where oligosaccharide
processing is completed. Our findings also provide a possible explanation--lack
of a functionally active conformation--for the absence of enzymatic function by
NA monomers.
Descriptors: influenza A virus avian enzymology,
neuraminidase metabolism, protein processing, post translational, antibodies,
monoclonal immunology, antibody specificity, cell line, disulfides metabolism,
dogs, epitopes immunology, glycosylation, kinetics, neuraminidase immunology,
protein folding, temperature.
Sambhara, S., A. Kurichh, R. Miranda, T. Tumpey, T.
Rowe, M. Renshaw, R. Arpino, A. Tamane, A. Kandil, O. James, B. Underdown, M.
Klein, J. Katz, and D. Burt (2001). Heterosubtypic immunity against human
influenza A viruses, including recently emerged avian H5 and H9 viruses,
induced by FLU-ISCOM vaccine in mice requires both cytotoxic T-lymphocyte and
macrophage function. Cellular Immunology 211(2): 143-53. ISSN: 0008-8749.
NAL
Call Number: QR180.C4
Descriptors: iscoms immunology, influenza prevention and
control, influenza A virus avian immunology, human immunology, influenza
vaccine immunology, macrophages immunology, T lymphocytes, cytotoxic
immunology, antibodies, viral immunology, cross reactions, fowl plague
prevention and control, influenza immunology, mice inbred BALB c, mice, inbred
c57bl, mice, inbred DBA, mice, knockout, time factors.
Sanchez Fauquier, A., M. Guillen, J. Martin, A.P.
Kendal, and J.A. Melero (1991). Conservation of epitopes recognized by
monoclonal antibodies against the separated subunits of influenza hemagglutinin
among type A viruses of the same and different subtypes. Archives of
Virology 116(1-4): 285-92. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Monoclonal antibodies raised against the
separated hemagglutinin subunits (HA1 and HA2) of influenza A/Vic/3/75 (H3N2)
virus were tested against a large panel of human and avian strains. The
epitopes recognized by most antibodies were conserved among subtype H3 viruses,
but reactivity of some antibodies with members of other subtypes was also
observed. Particularly, the H4 virus reacted with most antibodies directed
against the HA2 subunit. These results are discussed in terms of sequence
similarities between subtypes and application of these antibodies as subtyping
reagents.
Descriptors: antibodies, viral immunology, epitopes
immunology, hemagglutinins viral immunology, influenza A virus immunology,
antibodies, monoclonal immunology, cross reactions immunology, electrophoresis,
polyacrylamide gel, hemagglutinin glycoproteins, influenza virus, avian
classification, avian immunology, human classification, human immunology,
influenza A virus classification.
Sander Wewer, M., R. Schauer, and A.P. Corfield
(1982). Substrate specificity of viral, bacterial and mammalian sialidases
with regard to different N,O-acetylated sialic acids and GM1. Advances
in Experimental Medicine and Biology 152: 215-22. ISSN: 0065-2598.
NAL
Call Number: 448.3 AC85
Descriptors: bacteria enzymology, gm1 ganglioside
metabolism, gangliosides metabolism, influenza A virus avian enzymology,
neuraminidase metabolism, paramyxoviridae enzymology, sialic acids metabolism,
acetylation, species specificity, substrate specificity, time factors.
Sanger, C., E. Muhlberger, H.D. Klenk, and S. Becker
(2001). Adverse effects of MVA-T7 on the transport of Marburg virus
glycoprotein. Journal of Virological Methods 91(1): 29-35. ISSN: 0166-0934.
NAL
Call Number: QR355.J6
Abstract: Expression of glycoproteins has been carried
out successfully using recombinant vaccinia virus vectors. Especially
attractive is the use of recombinant vaccinia viruses which express the
DNA-dependent RNA polymerase of the phage T7 (T7-polymerase). The T7-polynerase
drives the transcription of plasmid-based genes under the control of the T7 RNA
polymerase promoter transfected into the infected cell. Comparison of two
different recombinant vaccinia viruses, vTF7-3 and MVA-T7, revealed that
post-translational processing of Marburg virus surface glycoprotein (GP) is
impaired in the MVA-T7 but not in the vTF7-3 system. Influenza virus
hemagglutinin, however, was transported and processed like the authentic
protein in both systems. It is shown that transport of GP in the MVA-T7 system
is not completely blocked, but the vast majority of molecules remained Endo
H-sensitive. Only trace amounts evaded the endoplasmatic reticulum and reached
the plasma membrane. Thus, the adverse effects of MVA-T7 on the processing of
recombinant glycoproteins cannot be predicted, and correct processing has to be
investigated for every expressed glycoprotein.
Descriptors: genetic vectors, vaccinia virus genetics,
viral envelope proteins metabolism, cell membrane metabolism, endoplasmic
reticulum metabolism, HeLa cells, hemagglutinins viral genetics, hemagglutinins
viral metabolism, influenza A virus avian genetics, avian metabolism, protein
processing, post translational, protein transport, viral envelope proteins
genetics.
Sansom, M.S. and I.D. Kerr (1993). Influenza virus
M2 protein: a molecular modelling study of the ion channel. Protein
Engineering 6(1): 65-74. ISSN:
0269-2139.
NAL
Call Number: TP248.P77P763
Abstract: The influenza A M2 protein forms
cation-selective ion channels which are blocked by the anti-influenza drug
amantadine. A molecular model of the M2 channel is presented in which a bundle
of four parallel M2 transbilayer helices surrounds a central ion-permeable
pore. Analysis of helix amphipathicity was used to aid determination of the
orientation of the helices about their long axes. The helices are tilted such
that the N-terminal mouth of the pore is wider than the C-terminal mouth. The
channel is lined by residues V27, S31 and I42. Residues D24 and D44 are located
at opposite mouths of the pore, which is narrowest in the vicinity of I42.
Energy profiles for interaction of the channel with Na+, amantadine-H+ and
cyclopentylamine-H+ are evaluated. The interaction profile for Na+ exhibits
three minima, one at each mouth of the pore, and one in the region of residue
S31. The amantadine-H+ profile exhibits a minimum close to S31 and a barrier
near residue I42. This provides a molecular model for amantadine-H+ block of M2
channels. The profile for cyclopentylamine-H+ does not exhibit such a barrier.
It is predicted that cyclopentylamine-H+ will not act as an M2 channel blocker.
Descriptors: influenza A virus avian chemistry, ion
channels chemistry, protein structure, tertiary, viral matrix proteins
chemistry, amantadine chemistry, amantadine metabolism, computer simulation,
cyclopentanes chemistry, cyclopentanes metabolism, ion channels metabolism,
models, molecular, protein structure, secondary, protons, receptors, nicotinic
chemistry, receptors, nicotinic metabolism, sodium chemistry, sodium metabolism,
viral matrix proteins metabolism.
Sauter, C., U. Baumberger, S. Ekenbark, and J.
Lindenmann (1973). Replication of an avian myxovirus in primary cultures of
human leukemic cells. Cancer Research 33(11): 3002-7. ISSN: 0008-5472.
NAL
Call Number: 448.8 C16
Descriptors: influenza A virus avian, leukemia
microbiology, virus replication, cultured cells, leukemia, lymphocytic,
leukemia, myelocytic, acute, leukemia, myeloid, virus cultivation.
Sauter, C., M. Ellison, and J. Lindenmann (1978). Association
of carcinoembryonic antigen (CEA) and influenza antigen. European
Journal of Cancer 14(6): 623-8.
ISSN: 0014-2964.
Descriptors: carcinoembryonic antigen, hemagglutinins
viral, influenza A virus avian immunology, bronchial neoplasms immunology, cell
line, cell membrane immunology, virus replication.
Schafer, J., M.L. Khristova, T.L. Busse, R.
Sinnecker, I.G. Kharitonenkov, C. Schrader, J. Suss, and D. Bucher (1992). Analysis
of internal proteins of influenza A (H2N2) viruses isolated from birds in East
Germany in 1983. Acta Virologica 36(2): 113-20. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Proteins and RNAs of influenza A (H2N2)
viruses isolated from birds in 1983 in East Germany were compared antigenically
with those of H2N2 human strains. The electrophoretic mobility of the viral
proteins and of the S1-treated double-stranded RNAs from two human and six
avian strains, as well as the results of EIA-tests using monoclonal antibodies
to their matrix protein and nucleoproteins indicate an antigenic relationship
between the avian isolates and human strains of H2N2 subtype. One of the avian
strains had a reduced amount of matrix protein.
Descriptors: antigens, viral analysis, epitopes analysis,
influenza A virus avian chemistry, human chemistry, RNA viral analysis, viral
matrix proteins analysis, antibodies, monoclonal, ducks, enzyme linked
immunosorbent assay, East Germany.
Schefer, J., M.L. Khristova, T.L. Busse, R.
Sinnecker, and I.G. Kharitonenkov (1990). Standartizatsiia uslovii
vyiavleniia vnutrennikh belkov virusa grippa pri issledovanii ikh antigennykh
svoistv v tverdofaznom immunofermentnom analize. [Standardization of conditions
for detecting the internal proteins of the influenza virus in studying their
antigenic properties in solid-phase immunoenzyme analysis]. Voprosy
Virusologii 35(2): 105-8. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The influence of the conditions of adsorption
and virion destruction by freezing-thawing and detergents on the detection of
M1 and NP proteins of different influenza virus strains by solid-phase enzyme
immunoassay with direct virion adsorption on polystyrene was studied. It was
found that for the detection of M1 protein the optimal conditions included
virion disruption with detergent and adsorption to polystyrene at 4 degrees C,
and for NP protein disruption by freezing-thawing at adsorption to polystyrene
at 37 degrees C. In the study of the antigenic properties of protein M1 of
different influenza virus strains using monoclonal antibodies it was shown to
be necessary, first, to achieve maximum detection of proteins and, second, to
standardize the amount of the adsorbed antigen with polyclonal antibodies.
Descriptors: antigens, viral analysis, capsid analysis,
influenza A virus avian analysis, human analysis, viral core proteins analysis,
viral matrix proteins analysis, adsorption, antibodies, monoclonal diagnostic
use, antigens, viral immunology, capsid immunology, enzyme linked immunosorbent
assay methods, enzyme linked immunosorbent assay standards, avian immunology,
human immunology, temperature, viral core proteins immunology, viral matrix
proteins immunology, virion analysis, virion immunology.
Scheiffele, P., A. Rietveld, T. Wilk, and K. Simons
(1999). Influenza viruses select ordered lipid domains during budding from
the plasma membrane. Journal of Biological Chemistry 274(4):
2038-44. ISSN: 0021-9258.
NAL
Call Number: 381 J824
Abstract: During the budding of enveloped viruses from
the plasma membrane, the lipids are not randomly incorporated into the
envelope, but virions seem to have a lipid composition different from the host
membrane. Here, we have analyzed lipid assemblies in three different viruses:
fowl plague virus (FPV) from the influenza virus family, vesicular stomatitis
virus (VSV), and Semliki Forest virus (SFV). Analysis of detergent
extractability of proteins, cholesterol, phosphoglycerolipids, and
sphingomyelin in virions showed that FPV contains high amounts of
detergent-insoluble complexes, whereas such complexes are largely absent from
VSV or SFV. Cholesterol depletion from the viral envelope by
methyl-beta-cyclodextrin results in increased solubility of sphingomyelin and
of the glycoproteins in the FPV envelope. This biochemical behavior suggests
that so-called raft-lipid domains are selectively incorporated into the influenza
virus envelope. The "fluidity" of the FPV envelope, as measured by
the fluorescence polarization of diphenylhexatriene, was significantly lower
than compared with VSV or SFV. Furthermore, influenza virus hemagglutinin
incorporated into the envelope of recombinant VSV was largely
detergent-soluble, indicating the depletion of raft-lipid assemblies from this
membrane. The results provide a model for lipid selectivity during virus
budding and support the view of lipid rafts as cholesterol-dependent, ordered
domains in biological membranes.
Descriptors: influenza A virus avian physiology, membrane
lipids metabolism, Semliki Forest virus physiology, vesicular stomatitis
Indiana virus physiology, cell line, cell membrane virology, detergents,
fluorescence polarization, hamsters, solubility.
Schettler, C.H. (1972). Immunologische Studien mit
Tween-Ather Spaltprodukten von drei serologisch verschiedenen aviaren Influeza
A Viren. [Immunological studies with Tween-ether fission products of three
serologically different avian influenza A viruses]. Tierarztliche
Umschau 27(10): 494-496. ISSN:
0049-3864.
NAL
Call Number: 41.8 T445
Descriptors: avian influenza, strains, vaccines,
immunology, ducks.
Schild, G.C., R.W. Newman, R.G. Webster, D. Major,
and V.S. Hinshaw (1980). Antigenic analysis of influenza A virus surface
antigens: considerations for the nomenclature of influenza virus. Brief review.
Archives of Virology 63(3-4): 171-84.
ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Descriptors: antigens, surface analysis, antigens, viral
analysis, hemagglutinins viral analysis, influenza A virus immunology,
antigens, viral classification, hemagglutinins viral classification, influenza
A virus avian immunology, human immunology, porcine immunology, neuraminidase
immunology, terminology.
Schild, G.C., R.W. Newman, R.G. Webster, D. Major,
and V.S. Hinshaw (1980). Antigenic analysis of influenza A virus surface
antigens: considerations for the nomenclature of influenza virus. Comparative
Immunology, Microbiology and Infectious Diseases 3(1-2): 5-18. ISSN: 0147-9571.
NAL
Call Number: QR180.C62
Descriptors: antigens, viral analysis, influenza A virus
avian immunology, human immunology, influenza A virus immunology,
hemagglutinins viral analysis, horses, porcine immunology, influenza A virus
classification, neuraminidase immunology, serotyping, terminology.
Schild, G.C. and H.G. Pereira (1969). Characterization
of the ribonucleoprotein and neuraminidase of influenza A viruses by
immunodiffusion. Journal of General Virology 4(3): 355-63. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: neuraminidase analysis, orthomyxoviridae
analysis, RNA viral analysis, antigens analysis, bile acids and salts
pharmacology, complement fixation tests, detergents pharmacology,
hemagglutinins viral analysis, immunochemistry, immunodiffusion,
immunoelectrophoresis, influenza A virus avian analysis, neuraminidase
antagonists and inhibitors, orthomyxoviridae drug effects.
Schlesinger, R.W., P.J. Husak, G.L. Bradshaw, and
P.P. Panayotov (1998 ). Mechanisms involved in natural and experimental
neuropathogenicity of influenza viruses: evidence and speculation. Advances
in Virus Research 50: 289-379. ISSN:
0065-3527.
NAL
Call Number: 448.3 AC85
Descriptors: central nervous system diseases virology,
influenza A virus avian pathogenicity, human pathogenicity, influenza B virus
pathogenicity, peripheral nervous system diseases virology, central nervous
system diseases pathology, peripheral nervous system diseases pathology.
Schmidt, M.F. (1982). Acylation of viral spike
glycoproteins: a feature of enveloped RNA viruses. Virology 116(1):
327-38. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: fatty acids metabolism, glycoproteins
metabolism, RNA viruses metabolism, viral proteins metabolism, acylation,
alphavirus metabolism, hemagglutinins viral, influenza A virus avian
metabolism, human metabolism, murine hepatitis virus metabolism, Newcastle
disease virus metabolism.
Schmidt, M.F., R.T. Schwarz, and H. Ludwig (1976). Fluorosugars
inhibit biological properties of different enveloped viruses. Journal of
Virology 18(3): 819-23. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Both 2-deoxy-2-fluoro-D-glucose and
2-deoxy-2-fluoro-D-mannose were found to be potent inhibitors of the synthesis
of infectious Semliki forest and fowl plague virus in chicken embryo cells and
also of pseudorabies virus grown in rabbit kidney cells. It was found that the
pseudorabies virus-mediated cell fusion and the synthesis of functional
hemagglutinin of fowl plague virus were blocked. In all cases the
2-deoxy-2-fluoro-D-mannose-caused inhibition was stronger than the
2-deoxy-2-fluoro-D-glucose- or 2-deoxy-D-glucose-mediated blocks. Studies on
the virus-specified proteins from Semiliki forest virus-infected cells grown in
the presence of the inhibitors show that the target of the fluorosugar action,
parallel to the well-studied effects of 2-deoxy-D-glucose, is the glycoprotein
biosynthesis.
Descriptors: deoxy sugars analogs and derivatives,
deoxyglucose analogs and derivatives, herpesviridae drug effects, herpesvirus
1, suid drug effects, influenza A virus avian drug effects, rhamnose analogs
and derivatives, Semliki Forest virus drug effects, cell fusion drug effects,
cell line, deoxyglucose pharmacology, fluorine, glycoproteins biosynthesis,
hemagglutinins viral, herpesvirus 1, suid growth and development, herpesvirus
1, suid metabolism, avian growth and development, avian metabolism, rhamnose
pharmacology, Semliki Forest virus growth and development, Semliki Forest virus
metabolism, viral proteins biosynthesis, virus replication drug effects.
Schmidt, R.C., H.F. Maassab, and F.M. Davenport
(1974). Infection by influenza A viruses of tracheal organ cultures derived
from homologous and heterologous hosts. Journal of Infectious Diseases
129(1): 28-36. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Descriptors: influenza A virus, tracheal tissue culture,
pathogenesis, human, swine, equine, chicken, ferret.
Schofield, D.J., J.R. Stephenson, and N.J. Dimmock
(1997). High and low efficiency neutralization epitopes on the
haemagglutinin of type A influenza virus. Journal of General Virology
78(Pt. 10): 2441-6. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The relationship between the efficiency of
the neutralization process and the affinity of five monoclonal IgG antibodies
specific for the haemagglutinin of type A influenza virus has been investigated
by determining their neutralization rate constants (Kneut.) and affinities
(Kdissoc.). We addressed the hypothesis that if antibody affinity alone
determined the efficiency of neutralization, then the Kneut.:Kdissoc. ratio
would be the same for all antibodies. However, we found that the
Kneut.:Kdissoc. ratio varied by up to 125-fold, suggesting that properties
unique to the epitope are of major importance in determining the efficiency of
neutralization. These data suggest that vaccines should preferentially
stimulate antibodies to epitopes that mediate the most efficient
neutralization, and that a high Kdissoc. should be an important but secondary
consideration.
Descriptors: antibodies, viral immunology, antigens, viral
immunology, hemagglutinin glycoproteins, influenza virus immunology, influenza
A virus avian immunology, antibodies, monoclonal immunology, antibody affinity,
antigen antibody reactions, chickens, epitope mapping, kinetics, neutralization
tests.
Schofield, D.J., J.R. Stephenson, and N.J. Dimmock
(1997). Variations in the neutralizing and haemagglutination-inhibiting
activities of five influenza A virus-specific IgGs and their antibody
fragments. Journal of General Virology 78(Pt. 10): 2431-9.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Neutralization and
haemagglutination-inhibition (HI) of a type A influenza virus by a panel of
five monoclonal IgGs, their F(ab')2s, Fabs and Fabs+ anti-mouse Fab were
compared. The MAbs were specific for antigenic sites A, B and D of the haemagglutinin.
Activities of the IgGs varied by up to 6-fold on a molar basis, apart from the
HI activity of HC58 which was > 100-fold lower. This was not due to low
functional affinity as HC58 had the second highest value (nM) as determined by
an equilibrium method with whole virions. Conversion to the F(ab')2 reduced
neutralization and HI by only 2- to 6-fold, indicating that the Fc region had
little involvement in these processes. However, all Fabs had low neutralization
and HI activity compared with their IgGs, neutralization being reduced by 86 to
> 1912-fold, and HI by 13 to > 69-fold. Although decreased, their
affinities remained high, in the nM range. Neutralization and HI by three of
the Fabs (HC2, HC3W and HC61) were restored by the addition of anti-Fab IgG;
however, HC10 Fab+anti-Fab IgG still had no detectable neutralization activity
but gave HI, and HC58 Fab+anti-Fab IgG had no detectable HI activity but
neutralized to the same extent as its IgG. The different properties of the
antibodies are discussed in the light of their known mechanisms of action: HI
by steric blocking of attachment of virus to the red cell receptor, and
neutralization by the inhibition of post-attachment events (HC2, HC10 and
HC61). The data demonstrate just how variable are the antiviral properties of
individual IgGs.
Descriptors: antibodies, monoclonal immunology,
antibodies, viral immunology, hemagglutinin glycoproteins, influenza virus
immunology, influenza A virus avian immunology, adult, antibodies, anti
idiotypic immunology, antigen antibody reactions, cell membrane immunology,
chickens, dose response relationship, immunologic, hemagglutination inhibition
tests, immunoglobulin g immunology, immunoglobulins, Fab immunology, membrane
glycoproteins immunology, neutralization tests.
Scholtissek, C. (1979). The genes coding for the
surface glycoproteins of influenza A viruses contain a small conserved and a
large variable region. Virology 93(2): 594-7. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes, structural, genes viral, glycoproteins
genetics, influenza A virus genetics, viral proteins genetics, base sequence,
hemagglutinins viral genetics, influenza A virus avian genetics, neuraminidase
genetics, nucleic acid hybridization, RNA viral genetics.
Scholtissek, C. (1976). Inhibition of influenza
RNA synthesis by virazole (ribavirin). Archives of Virology 50(4):
349-52. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Virazole (ribavirin) inhibits the RNA
synthesis of an influenza A virus (fowl plague). Neither virion RNA nor
complementary RNA are produced. Although the effect of virazole can be
counteracted by guanosine the inhibitor does not interfere with the uptake or
incorporation of labelled guanosine into chick embryo cells, nor does replacement
of glucose by mannose amplify the effect of virazole. Thus virazole seems not
to act via an interference with the GTP pool. Synthesis of Semliki Forest virus
RNA is not affected by virazole.
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, ribavirin pharmacology, ribonucleosides pharmacology, DNA
directed RNA polymerases biosynthesis, depression, chemical, hemagglutinins
viral, avian drug effects, neuraminidase biosynthesis, Semliki Forest virus
metabolism, tissue culture, viral proteins biosynthesis.
Scholtissek, C. (1985). Stability of infectious
influenza A viruses at low pH and at elevated temperature. Vaccine
3(3 Suppl.): 215-8. ISSN: 0264-410X.
NAL
Call Number: QR189.V32
Abstract: After treatment of different strains of
influenza A at low pH, the threshold pH, at which the infectivity was lost,
depended on the haemagglutinin (HA) subtype of the virus strain. Strains with
noncleaved HA were much more stable when compared to strains with cleaved HA.
These observations might explain why duck influenza viruses spread well by lake
water, while highly pathogenic strains with cleaved HA do not. There were also
significant differences in heat stability of infectivity among influenza A
strains, which do not correlate with differences in stability at low pH.
Descriptors: influenza A virus pathogenicity, chick
embryo, heat, hemagglutinins viral, hydrogen-ion concentration, influenza A
virus avian pathogenicity, human pathogenicity, species specificity.
Scholtissek, C. (1985). Stability of infectious
influenza A viruses to treatment at low pH and heating. Archives of
Virology 85(1-2): 1-11. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: We have measured the infectivity of influenza
A virus strains grown either in embryonated eggs or in chick embryo cells in
culture after treatment at low pH. At pH values at which hemolysis occurs there
was an irreversible loss of infectivity. The threshold pH, at which the
infectivity was lost, depended on the hemagglutinin subtype of the virus
strain. All H5 and H7 strains tested were extremely labile at low pH. In
contrast, all H3 strains were relatively stable, independent of the species
from which the viruses were isolated. With several H1 viruses the
hemagglutination (HA) activity was irreversibly lost at intermediate pH values
causing inactivation of infectivity. Strains with noncleaved hemagglutinins
were much more stable. These observations might explain why duck influenza
viruses can easily survive in lake water and wet faeces, and multiply in the
intestinal tract, where trypsin is present. There are also significant
differences in heat stability exhibited by influenza A strains. In contrast to
pH stability this is not a specific trait of the hemagglutinin, since it can be
influenced by reassortment. There is no correlation between the stability of
infectivity at low pH and heat.
Descriptors: heat, influenza A virus pathogenicity,
cultured cells, chick embryo, hemagglutination, viral, hydrogen-ion
concentration, influenza A virus avian growth and development, influenza A
virus classification, influenza A virus growth and development.
Scholtissek, C., H. Becht, and R. Drzeniek (1967). Biochemical
studies on the cytopathic effect of influenza viruses. Journal of
General Virology 1(2): 219-25. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: antiviral agents pharmacology, cytopathogenic
effect, viral, influenza A virus avian drug effects, avian pathogenicity,
carbon isotopes, ethylenes pharmacology, imines pharmacology, leucine
metabolism, quinones pharmacology, RNA viral metabolism, tritium, uridine
metabolism, virus cultivation.
Scholtissek, C., H. Becht, and I. Macpherson (1970). The
effect of mithramycin on the multiplication of myxoviruses. Journal of
General Virology 8(1): 11-9. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: antibiotics, antineoplastic pharmacology,
influenza A virus avian drug effects, Newcastle disease virus drug effects,
virus inhibitors, virus replication drug effects, antigens metabolism, chick
embryo, dactinomycin pharmacology, fibroblasts, hemagglutination inhibition
tests, hemagglutination tests, avian enzymology, avian growth and development,
avian immunology, avian metabolism, leucine metabolism, neuraminidase
metabolism, Newcastle disease virus growth and development, proteins
biosynthesis, RNA biosynthesis, RNA nucleotidyltransferases metabolism, RNA
viral biosynthesis, tritium, uridine metabolism.
Scholtissek, C., H. Burger, P.A. Bachmann, and C.
Hannoun (1983). Genetic relatedness of hemagglutinins of the H1 subtype of
influenza A viruses isolated from swine and birds. Virology 129(2):
521-3. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The hemagglutinin (HA) gene of the influenza
virus subtype H1N1 isolated from pigs and birds has been analyzed by the
hybridization technique. According to the RNase protection data the HA genes of
recent isolates from pigs in Northern Europe are genetically more closely
related to those of isolates from birds in Europe and North America than to
those of isolates from pigs in the United States, Taiwan, and Italy. Thus, two
different H1N1 subtypes are circulating in the pig population. The results are
consistent with the view that H1N1 viruses can be transmitted from birds to pigs
and/or vice versa.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, porcine genetics, genetics, birds microbiology, genes
viral, avian immunology, avian isolation and purification, porcine
classification, porcine immunology, porcine isolation and purification, nucleic
acid hybridization, swine microbiology.
Scholtissek, C., H. Burger, O. Kistner, and K.F.
Shortridge (1985). The nucleoprotein as a possible major factor in
determining host specificity of influenza H3N2 viruses. Virology
147(2): 287-94. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: In an attempt to assess the importance of the
nucleoprotein (NP) in the determination of host specificity, a series of
experiments was performed on influenza A viruses of the H3N2 subtype. We have
examined rescue of mutants of A/FPV/Rostock/34 with temperature-sensitive (ts)
lesions in the nucleoprotein (NP) gene by double infection of chick embryo
cells with H3N2 strains isolated from different species. The ts mutants could
be rescued by all avian H3N2 strains but not by any of the human H3N2 isolates.
Only two of the swine H3N2 strains tested were able to rescue our mutants. The
NP gene of these two swine isolates resembled the NP gene of the avian strains
genetically in the hybridization test. However, their NPs reacted differently
with a set of monoclonal antibodies when compared with NPs of avian H3N2
strains. Concerning multiplication in ducks they behaved like the other swine
and human strains. The phosphopeptide fingerprints of all swine isolates tested
were alike and were different from those of human or avian origin. Our
observations are compatible with the idea that human H3N2 strains might not be
able to cross the species barrier to birds directly, and possibly also not the
other way around, without prior reassortment in pigs, which seem to have a
broader host range concerning the compatibility of the NP gene in reassortants.
Descriptors: capsid physiology, influenza A virus avian
physiology, human physiology, porcine physiology, influenza A virus physiology,
viral core proteins physiology, antibodies, viral analysis, capsid analysis,
capsid genetics, capsid immunology, cultured cells, chick embryo, ducks,
electrophoresis, polyacrylamide gel, epitopes, fowl plague immunology, fowl
plague microbiology, avian genetics, avian immunology, human genetics, human
immunology, porcine genetics, porcine immunology, mutation, nucleic acid
hybridization, phosphopeptides analysis, recombination, genetic, temperature,
viral core proteins analysis, viral core proteins genetics, viral core proteins
immunology.
Scholtissek, C. and J. Damgen (1974). Proceedings:
Specific inhibition of influenza and Semliki Forest virus RNA synthesis by
glucosamine. Hoppe Seyler's Zeitschrift Fur Physiologische Chemie
355(10): 1252-3. ISSN: 0018-4888.
NAL
Call Number: 384 Z38
Descriptors: glucosamine pharmacology, influenza A virus
avian metabolism, RNA viral biosynthesis, Semliki Forest virus metabolism,
chick embryo, depression, chemical.
Scholtissek, C. and G.P. Faulkner (1979). Amantadine-resistant
and -sensitive influenza A strains and recombinants. Journal of General
Virology 44(3): 807-15. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Several influenza A strains and recombinants
of fowl plague virus (FPV) with a known gene constellation were tested for
amantadine sensitivity under two different experimental conditions. In a
haemagglutinin yield analysis of a single growth cycle experiment FPV was found
to be highly sensitive to amantadine, while in the plaque reduction and
inhibition test it was highly resistant. With the A3 Hong Kong and equi 2
strains the opposite observation was made. The A2 Singapore strain was
sensitive while Ao PR8 was resistant in both tests. In the haemagglutinin yield
analysis of a single growth cycle all recombinants carrying segment 4 (HA) of
the resistant strain were resistent against amantadine, independent of the
derivation of the other genes. In the plaque reduction and inhibition test
recombinants carrying the haemagglutinin of the sensitive strain were either
resistant or sensitive depending on the gene constellation. Drug sensitivity
was transferred by the combination of segments 5 (NP) and 6 (NA). Segment 7 (M)
of certain sensitive strains seems to counteract this effect. The results are
compatible with the concept that amantadine resistance or sensitivity is not
confined to a single gene product or a single mechanism.
Descriptors: amantadine pharmacology, influenza A virus
drug effects, recombination, genetic, drug resistance, microbial,
hemagglutinins viral analysis, influenza A virus avian drug effects, human drug
effects, influenza A virus genetics, influenza A virus immunology, mutation,
plaque assay.
Scholtissek, C., E. Harms, W. Rohde, M. Orlich, and
R. Rott (1976). Correlation between RNA fragments of fowl plague virus and
their corresponding gene functions. Virology 74(2): 332-44. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes, influenza A virus avian metabolism,
RNA viral metabolism, base sequence, nucleic acid denaturation, nucleic acid
hybridization, plaque assay, recombination, genetic.
Scholtissek, C., G. Kaluza, and R. Rott (1972). Stability
and precursor relationships of virus RNA. Journal of General Virology
17(2): 213-9. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian metabolism, Newcastle
disease virus metabolism, protein precursors, RNA viral metabolism, Semliki
Forest virus metabolism, base sequence, centrifugation, density gradient, chick
embryo, culture media, dactinomycin pharmacology, fibroblasts, glucosamine
pharmacology, hemagglutination tests, avian growth and development, Newcastle
disease virus growth and development, nucleic acid hybridization, plaque assay,
RNA biosynthesis, viral biosynthesis, Semliki Forest virus growth and
development, tissue culture, tritium, uracil nucleotides metabolism, uridine
metabolism, virus replication.
Scholtissek, C., I. Koennecke, and R. Rott (1978). Host
range recombinants of fowl plague (influenza A) virus. Virology
91(1): 79-85. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian genetics,
recombination, genetic, cell line, chickens microbiology, genes viral,
hemagglutinins viral analysis, avian growth and development, avian
pathogenicity, human genetics, influenza A virus genetics, RNA viral
biosynthesis.
Scholtissek, C., R. Kruczinna, R. Rott, and H.D.
Klenk (1974). Characteristics of an influenza mutant temperature-sensitive
for viral RNA synthesis. Virology 58(2): 317-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, mutation,
RNA viral biosynthesis, temperature, amino acids metabolism, antigens, viral
analysis, chick embryo, DNA directed RNA polymerases metabolism,
electrophoresis, polyacrylamide gel, fibroblasts, fluorouracil, hemagglutinins
viral analysis, avian enzymology, avian growth and development, avian immunology,
mutagens, neuraminidase analysis, peptide synthesis, tissue culture,
tritium, uridine metabolism, viral
proteins biosynthesis, virus replication.
Scholtissek, C., S. Ludwig, and W.M. Fitch (1993). Analysis
of influenza A virus nucleoproteins for the assessment of molecular genetic
mechanisms leading to new phylogenetic virus lineages. Archives of
Virology 131(3-4): 237-50. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The nucleoprotein (NP) gene of influenza A
viruses is decisive for separating two large individually evolving reservoirs
in birds and humans. A phylogenetic analysis of the NP gene revealed that all
mammalian influenza viruses originated--directly or indirectly--from an avian
ancestor. The stable introduction of an avian influenza A virus into a
mammalian species seems to be a relatively rare event, the latest one occurred
in 1979 when such an avian virus was introduced into pigs in Northern Europe
which gave rise to a new lineage. At least two concomitant events are required
for such a new and stable introduction: (1) The new species has to become
infected, and (2) a mutation in the polymerase complex has to establish a
labile variant, which is prone to provide a large number of different variants,
from which some can adapt rapidly to the new host (or to any unusual
environments). Since such mutator mutations might be advantageous only during
stress periods, variants with a less error prone polymerase might emerge again
after adaptation. Examples for such fluctuations in terms of mutational and
evolutionary rates are discussed in this brief review.
Descriptors: influenza A virus genetics, nucleoproteins
chemistry, phylogeny, viral core proteins chemistry, genes viral, influenza A
virus chemistry, mutation, nucleoproteins genetics, sequence homology, amino
acid, viral core proteins genetics.
Scholtissek, C. and K. Muller (1988). Effect of
dimethylsulfoxide (DMSO) on virus replication and maturation. Archives
of Virology 100(1-2): 27-35. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: At intermediate concentrations of DMSO the
yields of infectious virus and biologically active hemagglutinin and
neuraminidase of an influenza A virus (fowl plague virus) and of reassortants
therefrom are enhanced severalfold, even though viral protein synthesis is not
significantly affected. A corresponding enhancing effect was also found with
New castle disease and Semliki Forest viruses. At elevated concentrations of
DMSO virus yield decreases, and under these conditions the synthesis of the
late influenza virus proteins is specifically inhibited. The results indicate
that DMSO can facilitate the assembly of virus particles, and viral components,
which are normally produced in surplus amounts, now contribute to the maturation
of infectious particles.
Descriptors: dimethyl sulfoxide pharmacology, virus
replication drug effects, hemagglutination, viral drug effects, influenza A
virus avian drug effects, avian growth and development, Newcastle disease virus
drug effects, Newcastle disease virus growth and development, plaque assay,
Semliki Forest virus drug effects, Semliki Forest virus growth and development,
viral proteins biosynthesis, virus cultivation.
Scholtissek, C. and K. Muller (1991). Failure to
obtain drug-resistant variants of influenza virus after treatment with
inhibiting doses of 3-deazaadenosine and H7. Archives of Virology
119(1-2): 111-8. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: 3-Deazaadenosine and H7 specifically inhibit
influenza virus replication under conditions at which they have no effect on
other tested RNA viruses. This effect can be significantly potentiated by
concomitant application of both compounds. Even under the most stringent
conditions we failed to obtain any drug resistant variants. A possible
explanation for this failure is that these compounds presumably do not act on a
viral component like amantadine which was used as a control, but they interfere
with cellular enzymes (factors) absolutely essential for influenza virus replication
but more or less dispensable for the survival of the cell.
Descriptors: influenza A virus avian drug effects,
isoquinolines pharmacology, piperazines pharmacology, tubercidin pharmacology,
1 5 isoquinolinesulfonyl 2 methylpiperazine, cultured cells, chick embryo, drug
combinations, drug resistance, microbial, virus replication drug effects.
Scholtissek, C. and K. Muller (1988). Interference
between influenza A viruses with a cleavable and a noncleavable hemagglutinin;
pH-stability after mixed infection. Archives of Virology 101(1-2):
119-23. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The infectivity of influenza A viruses like
fowl plague virus (FPV) with a cleaved hemagglutinin (HA) is highly sensitive
to treatment at pH 5, while strains like PR 8 or virus N with a noncleaved HA
survive under this condition. After double infection of chick embryo cells with
FPV and PR 8 or virus N, the yield of virus with the HA gene of FPV is greatly
reduced. However, it can now survive treatment at pH 5, and the surviving FPV
particles form plaques only in the presence of trypsin, indicating that they
were coated by the HA of PR 8 or virus N, depending on the coinfecting virus.
The results are discussed with respect to the build-up and maintenance of a
large reservoir of nonpathogenic influenza A viruses with noncleavable HA in
water fowl.
Descriptors: fowl plague microbiology, hemagglutinins
viral physiology, influenza A virus avian pathogenicity, cultured cells,
fibroblasts microbiology, fowl plague enzymology, hemagglutinins viral
metabolism, hydrogen-ion concentration, avian enzymology, plaque assay, trypsin
physiology, viral interference, water microbiology.
Scholtissek, C. and K. Muller (1983). Temperature-sensitive
mutants of fowl plague virus (influenza A) generated by undiluted passages at
33 degrees C. Journal of General Virology 64(Pt. 12): 2621-9. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Temperature-sensitive (ts) mutants obtained
by undiluted passages of fowl plague virus at 33 degrees C have their defects
located mainly in RNA segments 3, 4 and 8 as determined by rescue to wild-type
with standard ts mutants. This result is different from that obtained after
treatment of virus with mutagens, where the frequency of mutations follows
roughly the target size of the RNA segments. Many isolates generated after
undiluted passages at 33 degrees C, which seem to have mutations in RNA
segments 3 and 4, can be rescued to wild-type. This occurs, however, with
certain defined standard ts mutants having a defect in RNA segment 4, but not
by other segment 4 mutants. One such mutant, ts 1/93 (ts defect in segment 3),
interferes with the multiplication of ts 227 (ts defect in segment 4) at the
permissive temperature, presumably at the level of vRNA synthesis, preventing
reassortment to wild-type. Similarly, ts 263 (ts defect in segment 3)
interferes with the multiplication of ts 1/1 (ts defect in segment 4). For
other such interfering mutants, the mechanism preventing reassortment to wild-type
is different from that of ts 1/93 or ts 1/1, but is not yet understood. Thus,
the number of mutations as determined by rescue with standard ts mutants in
isolates obtained by undiluted passages is overestimated due to intrinsic
interference.
Descriptors: genes viral, influenza A virus avian
genetics, cultured cells, chick embryo, fluorouracil pharmacology, avian growth
and development, mutation, plaque assay, RNA viral genetics, temperature, viral
interference.
Scholtissek, C., K. Muller, and S. Herzog (1986). Influence
of insulin and 12-O-tetradecanoylphorbol-13-acetate (TPA) on influenza virus
multiplication. Virus Research 6(3): 287-94. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Insulin and
12-O-tetradecanoylphorbol-13-acetate (TPA) interfere with the multiplication of
fowl plague virus, an influenza A virus, in primary chick embryo cells.
Specifically the production of the viral glycoproteins hemagglutinin and
neuraminidase are affected by the drugs. A decrease or omission of glucose from
the culture medium enhances this effect, which is in agreement with the idea
that these drugs act on virus replication via a shortage of glucose in the host
cell. Virus replication in cells of different organs is affected to different
extents by insulin and TPA.
Descriptors: glucose metabolism, influenza A virus avian
drug effects, insulin pharmacology, tetradecanoylphorbol acetate pharmacology,
virus replication drug effects, cell line, cultured cells, chick embryo,
electrophoresis, polyacrylamide gel, avian physiology.
Scholtissek, C. and B.R. Murphy (1978). Host range
mutants of an influenza A virus. Archives of Virology 58(4):
323-33. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Temperature-sensitive (ts) mutants of fowl
plague virus with a ts-lesion in segment 1 (ts 3, polymerase 1 gene) or segment
2 (ts 90, transport gene) do not form plaques on MDCK cells at the permissive
temperature, while the wild type and ts-mutants of other groups are able to do
so. This property is correlated with the ts-lesion, since revertants for the
ts-lesion of ts 3 and ts 90 again form plaques on MDCK cells. The block on MDCK
cells--at least for ts3--may be located in a late function, since viral RNA
polymerase and hemagglutinin are formed in almost normal yields. MDCK cells
infected with ts 3 or ts 90 exhibit a retarded cytopathic effect at 33 degrees
C, but no cytopathic effect at 39 degrees C, at which temperature the infected
cells can be passaged and super-infected with the wild type strain. Cells
surviving the infection with ts 90 at 33 degrees C sometimes grow out again to
a normal monolayer. It is suggested that the spread of virus is inhibited under
these conditions.
Descriptors: genes viral, influenza A virus avian growth
and development, cell line, cytopathogenic effect, viral, DNA directed RNA
polymerases biosynthesis, hemagglutinins viral, avian genetics, mutation,
plaque assay, temperature.
Scholtissek, C., W. Rohde, E. Harms, and R. Rott
(1977). Correlation between base sequence homology of RNA segment 4 and
antigenicity of the hemagglutinin of influenza viruses. Virology
79(2): 330-6. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: base sequence, biochemistry, hemagglutinins
viral analysis, influenza A virus analysis, influenza A virus immunology, RNA
viral analysis, influenza A virus avian analysis, avian immunology, human
analysis, human immunology, porcine analysis, porcine immunology, nucleic acid
hybridization.
Scholtissek, C., W. Rohde, E. Harms, R. Rott, M.
Orlich, and C.B. Boschek (1978). A possible partial heterozygote of an
influenza A virus. Virology 89(2): 506-16. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus avian
genetics, influenza A virus genetics, recombination, genetic, base sequence,
heterozygote, avian analysis, influenza A virus analysis, mutation,
neuraminidase analysis, nucleic acid conformation, RNA viral analysis.
Scholtissek, C. and R. Rott (1984). Correlation
between loss of the temperature-sensitive phenotype and pathogenicity of fowl
plague virus mutants in the chicken. Virus Research 1(2):
117-31. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The reversion of temperature-sensitive (ts)
mutants of fowl plague virus to the ts+ phenotype was correlated with
pathogenicity for chicken. Two types of ts mutants were investigated: those
obtained by mutagenesis with 5-fluorouracil and those obtained by undiluted
passages at 33 degrees C. The reversion frequency of the former mutants
depended on the RNA segment in which the ts defect was located, mutations in
RNA segments 1 and 2 having the highest reversion frequency, those in the RNA
segments coding for the glycoproteins the lowest. ts mutants obtained by
undiluted passages behaved differently in this respect. There was an
approximate correlation between frequency of reversion and pathogenicity for
chicken. Double mutants induced by 5-fluorouracil, having one tight and one
leaky mutation, reverted easily without loss of the leaky mutation. These
double mutants were still to a limited extent pathogenic for the chicken. Only
one double mutant with two tight mutations (ts 293) was completely
nonpathogenic after intramuscular inoculation. Two ts mutants with multiple
tight defects (ts 1/1 and ts 3/18) obtained by undiluted passage did not revert
to wild-type after injection into embryonated eggs and incubation at 33 degrees
C, but they were still slightly pathogenic for the chicken. There was no obvious
correlation between the shut-off temperature and pathogenicity of mutants
carrying a single ts defect. However, for mutants with multiple tight mutations
a high shut-off temperature seemed to be essential for reversion during serial
passages as well as for pathogenicity in the chicken, when different routes of
inoculation were examined. ts mutants seem to be safe as live vaccines only,
(1) if they carry at least two tight ts defects, (2) if they have a relatively
low shut-off temperature, and (3) if they could be administered other than via
the respiratory tract.
Descriptors: influenza A virus avian genetics, mutation,
temperature, chickens microbiology, fluorouracil pharmacology, avian
pathogenicity.
Scholtissek, C. and R. Rott (1969). Effect of temperature
on the multiplication of an Influenza virus. Journal of General Virology
5(2): 283-90. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian growth and
development, fibroblasts, hemagglutination, viral, avian enzymology, leucine,
neuraminidase metabolism, nucleosides, RNA nucleotidyltransferases metabolism,
temperature, tissue culture, tritium.
Scholtissek, C. and R. Rott (1967). Failure of
function of the "early protein" induced by an influenza virus in
cells infected by Newcastle disease virus. Nature 213(72): 186. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: dactinomycin pharmacology, influenza A virus
avian, Newcastle disease virus, phenylalanine pharmacology, proteins, RNA viral
biosynthesis, uridine metabolism, carbon isotopes, chick embryo.
Scholtissek, C. and R. Rott (1969). Ribonucleic
acid nucleotidyl transferase induced in chick fibroblasts after infection with
an influenza virus. Journal of General Virology 4(1): 125-37. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian, RNA
nucleotidyltransferases, tissue culture, chickens, dactinomycin pharmacology,
dextrans pharmacology, enzyme induction, fibroblasts, guanine nucleotides
metabolism, magnesium pharmacology, nucleotides pharmacology, phenylalanine
pharmacology, protamines pharmacology, RNA pharmacology, ribonucleases
pharmacology, tritium.
Scholtissek, C. and R. Rott (1970). Synthesis in
vivo of influenza virus plus and minus strand RNA and its preferential
inhibition by antibiotics. Virology 40(4): 989-96. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cycloheximide pharmacology, dactinomycin pharmacology,
influenza A virus avian metabolism, RNA viral biosynthesis, chickens,
depression, chemical, fibroblasts, avian pathogenicity, phosphates metabolism,
phosphorus isotopes, precipitation, RNA viral isolation and purification,
tissue culture, tritium, uridine metabolism.
Scholtissek, C., R. Rott, and H.D. Klenk (1975). Two
different mechanisms of the inhibition of the multiplication of enveloped
viruses by glucosamine. Virology 63(1): 191-200. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: antiviral agents pharmacology, glucosamine
pharmacology, influenza A virus avian drug effects, Newcastle disease virus
drug effects, Semliki Forest virus drug effects, vesicular stomatitis Indiana
virus drug effects, virus replication drug effects, culture media, cytidine
pharmacology, DNA directed RNA polymerases metabolism, dose response
relationship, drug, fructose metabolism, glucose metabolism, glycoproteins
biosynthesis, guanosine pharmacology, avian growth and development, Newcastle
disease virus growth and development, RNA viral biosynthesis, Semliki Forest
virus growth and development, tritium, uracil nucleotides metabolism, uridine
pharmacology, vesicular stomatitis Indiana virus growth and development, virus
cultivation.
Scholtissek, C., R. Rott, D.K. Lvov, and I.A.
Myasnikova (1980). Genetic relatedness of the neuramindase of influenza A
strains Nav2, Nav3, and Nav6. Archives of Virology 65(3-4):
325-8. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: By molecular hybridization and by
neuraminidase inhibition tests it is shown that all influenza A strains tested
carrying an Nav3 or Nav2 neuraminidase (NA) are genetically highly related in
their NA genes and cross-react serologically with specific antineuraminidase
sera. The Nav6 strains exhibit a very low RNase protection after hybridization
and do not cross-react serologically with Nav2 or Nav3 strains. Thus, the Nav2
and Nav3 strains comprise one group which is distinct from that of Nav6
strains.
Descriptors: genes viral, influenza A virus genetics,
neuraminidase genetics, cross reactions, influenza A virus avian enzymology,
avian genetics, influenza A virus enzymology, neuraminidase immunology, nucleic
acid hybridization.
Scholtissek, C., R. Rott, M. Orlich, E. Harms, and W.
Rohde (1977). Correlation of pathogenicity and gene constellation of an
influenza A virus (fowl plague). I. Exchange of a single gene. Virology
81(1): 74-80. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes, influenza A virus avian pathogenicity,
recombination, genetic, antibodies, viral biosynthesis, chickens, fluorouracil,
avian analysis, avian immunology, influenza A virus pathogenicity, mutagens,
mutation, RNA viral analysis.
Scholtissek, C., R.T. Schwarz, W. Keil, and H.D.
Klenk (1984). A mutant of fowl plague virus (influenza A) with an altered
glycosylation pattern in its hemagglutinin. Virology 136(1):
1-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: A temperature-sensitive mutant (ts 1/1) with
a defect in the hemagglutinin (HA) gene, which was obtained by undiluted
passage of fowl plague virus (FPV) at 33 degrees, is described. At 33 degrees
proteolytic cleavage of the abnormal HA yielded an altered HA2 (XHA2) which
migrated ahead of the NS1 protein and lacked the complex oligosaccharide side
chain. At the nonpermissive temperature of 40 degrees, the migration of the HA
of ts 1/1 from the rough endoplasmic reticulum (RER) via the Golgi apparatus to
the cell surface was rate limiting for virus maturation. The HA was only slowly
cleaved and migrated during polyacrylamide gel electrophoresis ahead of the HA
of wild type FPV. Some revertants of ts 1/1 exhibited the same protein pattern
as the mutant, others resembled wild type FPV, while one revertant gave rise to
a mixture of HA2 and XHA2 at 40 degrees. These results suggest that (1) the
loss of the complex oligosaccharide side chain is not responsible for the ts
phenotype, (2) the mutation is presumably not at the site where the
oligosaccharide side chain is linked to the protein backbone, and (3) ts 1/1
presumably carries a mutation located in RNA segment 4, which by
pseudoreversion (suppressor mutation) in the same gene leads to different ts+
phenotypes.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian genetics, oligosaccharides analysis, cell membrane
metabolism, cultured cells, chick embryo, endoplasmic reticulum metabolism,
Golgi apparatus metabolism, hemagglutinins viral analysis, avian growth and
development, avian immunology, mutation, phenotype, temperature.
Scholtissek, C. and S.B. Spring (1982). Extragenic
suppression of temperature-sensitive mutations in RNA segment 8 by replacement
of different rna segments with those of other influenza A virus prototype
strains. Virology 118(1): 28-34.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian genetics, mutation,
RNA viral genetics, suppression, genetic, crosses, genetic, genes viral,
genetic markers, recombination, genetic, virus activation.
Scholtissek, C., J. Stech, S. Krauss, and R.G.
Webster (2002). Cooperation between the hemagglutinin of avian viruses and
the matrix protein of human influenza A viruses. Journal of Virology
76(4): 1781-6. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: To analyze the compatibility of avian
influenza A virus hemagglutinins (HAs) and human influenza A virus matrix (M)
proteins M1 and M2, we doubly infected Madin-Darby canine kidney cells with
amantadine (1-aminoadamantane hydrochloride)-resistant human viruses and
amantadine-sensitive avian strains. By using antisera against the human virus
HAs and amantadine, we selected reassortants containing the human virus M gene
and the avian virus HA gene. In our system, high virus yields and large,
well-defined plaques indicated that the avian HAs and the human M gene products
could cooperate effectively; low virus yields and small, turbid plaques
indicated that cooperation was poor. The M gene products are among the primary
components that determine the species specificities of influenza A viruses.
Therefore, our system also indicated whether the avian HA genes effectively
reassorted into the genome and replaced the HA gene of the prevailing human
influenza A viruses. Most of the avian HAs that we tested efficiently
cooperated with the M gene products of the early human A/PR/8/34 (H1N1) virus;
however, the avian HAs did not effectively cooperate with the most recently
isolated human virus that we tested, A/Nanchang/933/95 (H3N2). Cooperation between
the avian HAs and the M proteins of the human A/Singapore/57 (H2N2) virus was
moderate. These results suggest that the currently prevailing human influenza A
viruses might have lost their ability to undergo antigenic shift and therefore
are unable to form new pandemic viruses that contain an avian HA, a finding
that is of great interest for pandemic planning.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, influenza A virus avian genetics, human genetics, reassortant
viruses, viral matrix proteins metabolism, amantadine pharmacology, antiviral
agents pharmacology, cell line, dogs, drug resistance, viral, fowl plague
virology, hemagglutinin glycoproteins, influenza virus genetics, influenza
virology, avian drug effects, avian growth and development, avian metabolism,
human drug effects, human growth and development, human metabolism, kidney
cytology, kidney virology, plaque assay, poultry, viral matrix proteins
genetics.
Scholtissek, C., A. Vallbracht, B. Flehmig, and R.
Rott (1979). Correlation of pathogenicity and gene constellation of
influenza A viruses. II. Highly neurovirulent recombinants derived from
non-neurovirulent or weakly neurovirulent parent virus strains. Virology
95(2): 492-500. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus pathogenicity,
recombination, genetic, brain microbiology, chickens, influenza A virus avian
genetics, human genetics, influenza A virus genetics, lung microbiology, mice,
tissue culture, virulence.
Scholtissek, C. and V. von Hoyningen Huene (1980). Genetic
relatedness of the gene which codes for the nonstructural (NS) protein of
different influenza A strains. Virology 102(1): 13-20. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes, structural, genes viral, influenza A
virus genetics, viral proteins genetics, base sequence, influenza A virus avian
genetics, human genetics, porcine, nucleic acid hybridization, RNA viral
analysis, RNA viral genetics.
Schroeder, C., H. Heider, B. Hegenscheid, M.
Schoffel, V.I. Bubovich, and H.A. Rosenthal (1985). The anticholinergic
anti-Parkinson drug Norakin selectively inhibits influenza virus replication.
Antiviral Research (Suppl. 1): 95-9.
ISSN: 0166-3542.
NAL
Call Number: QR355.A5
Descriptors: antiviral agents, biperiden pharmacology,
influenza A virus avian drug effects, human drug effects, piperidines
pharmacology, amantadine pharmacology, cell line, chick embryo, drug
interactions, drug resistance, microbial, genes viral drug effects, hemagglutination,
viral drug effects, hemolysis drug effects, avian physiology, human growth and
development, human physiology, interferon type I biosynthesis, interferons
pharmacology, measles virus drug effects, mutation, virus replication drug
effects.
Schultz, C.S., M. Koci, E. Thompson, and T.M. Tumpey
(2003). Examining the cellular pathways involved in influenza virus induced
apoptosis. Avian Diseases 47(Special Issue): 968-971. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Apoptosis is essential in many physiological
processes including wound healing and development of the immune response.
Apoptosis also plays an important role in the pathogenesis of many infectious
diseases including those caused by viruses. Influenza viruses induce apoptosis
in cells that are permissive for viral replication and cells that do not
support viral replication. The cellular pathways involved in influenza virus
induced apoptosis are currently ill defined. Previous studies suggest that
influenza virus infection increased the expression of the Fas antigen in HeLa
cells, and that Fas antigen is partially involved in apoptosis. In these
studies we examined the cellular pathways involved in avian influenza virus
induced apoptosis in two cell lines that support productive viral replication:
Madin-Darby canine kidney cells (MDCK) and mink lung epithelial (Mv1Lu) cells.
Descriptors: cell biology, infection, cellular pathways,
immune response, physiological processes, viral replication, virally induced apoptosis,
wound healing.
Schultz, U., W.M. Fitch, S. Ludwig, J. Mandler, and
C. Scholtissek (1991). Evolution of pig influenza viruses. Virology
183(1): 61-73. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: There is evidence that the nucleoprotein (NP)
gene of the classical swine virus (A/Swine/1976/31) clusters with the early
human strains at the nucleotide sequence level, while at the level of the amino
acid sequence, as defined by consensus amino acids and in functional tests, its
NP is clearly "avian like." Therefore it was suggested that the Sw/31
NP had been recently under strong selection pressure, possibly caused by
reassortment with other avian influenza genes, whose gene products have to
cooperate intimately with NP (Gammelin et al., 1989. Virology 170, 71-80). This
suggestion has been investigated by sequencing the genes of internal and
nonstructural proteins of Sw/31. The data on these sequences and on the
phylogenetic trees are not in accordance with that suggestion: all these genes cluster
with the early human strains at the nucleotide level while, at the level of the
amino acid sequence, most of them are more closely related to the avian
strains, thus resembling NP in this respect. This indicates that these genes
rather evolved concomitantly with the NP gene. Our data are in agreement with
the suggestion that, at about the time of the Spanish Flu (1918/19), a human
influenza A (H1N1) virus entered the pig population. Furthermore, it is known
that the NP of the human influenza A viruses--in contrast to that of the avian
and swine strains--has been under strong selection pressure to change (Gammelin
et al., 1990. Mol. Biol. Evol. 7, 194-200. Gorman et al., 1990a. J. Virol. 64,
1487-1497). Thus, after transfer of a human strain into pigs, the selection
pressure might be released, enabling the NP and the other genes of the swine
virus to evolve back to the optimal avian sequences, especially at the
functionally important consensus positions. The swine influenza viruses
circulating since 1979 in Northern Europe--represented by A/Swine/Germany/2/81
(H1N1)--have all genes, so far examined, derived from an avian influenza virus
pool and are different from the classical swine viruses.
Descriptors: influenza A virus, porcine genetics,
phylogeny, RNA replicase, viral proteins genetics, chick embryo, consensus sequence, genes
viral, nucleoproteins genetics, swine, viral core proteins genetics.
Schuy, W., C. Will, K. Kuroda, C. Scholtissek, W.
Garten, and H.D. Klenk (1986). Mutations blocking the transport of the
influenza virus hemagglutinin between the rough endoplasmic reticulum and the
Golgi apparatus. EMBO Journal 5(11): 2831-6. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: Mutants ts1 and ts227 of fowl plague virus
have a temperature-sensitive defect in the transport of the hemagglutinin from
the rough endoplasmic reticulum to the Golgi apparatus. The primary structure
of the hemagglutinin of the mutants and of a number of revertants derived from
them has been analysed by nucleotide sequencing. The transport block of the
hemagglutinin of ts227 can be attributed to a single amino acid exchange. It
involves the replacement of aspartic acid at position 457 by asparagine thereby
introducing a new glycosylation site which appears to be located in a cryptic
position in the lower part of the hemagglutinin stalk. Attachment of
carbohydrate to this site is temperature-dependent. At permissive temperature
only a small fraction of the monomers (approximately 30%) is glycosylated in
this position, whereas at nonpermissive temperature this is the case with all
subunits. The data suggest that under the latter conditions the new
oligosaccharide interferes by steric hindrance with the trimerization of the
hemagglutinin. The hemagglutinin of ts1 has an essential amino acid exchange at
position 275 where serine is replaced by glycine. This substitution may
increase the flexibility of the molecule in the hinge region between the
globular domain and the stalk. The exchange of a conserved glutamic acid residue
at position 398 that is involved in the interaction between different monomers
contributes also to the structural instability of the ts1 hemagglutinin. These
observations support the notion that the transport of the hemagglutinin from
the rough endoplasmic reticulum to the Golgi apparatus depends on trimer
assembly.
Descriptors: endoplasmic reticulum metabolism, Golgi
apparatus metabolism, hemagglutinins viral genetics, influenza A virus avian
genetics, mutation, base sequence, chick embryo, cloning, molecular, DNA
analysis, DNA restriction enzymes, glycoproteins genetics, glycoproteins
isolation and purification, models, molecular, protein conformation, RNA viral
genetics, RNA viral isolation and purification.
Schwarz, R.T., B. Fournet, J. Montreuil, R. Rott, and
H.D. Klenk (1978). The carbohydrates of influenza virus. II. Gas
chromatographic analysis of glycopeptides derived from viral glycoproteins and
mucopolysaccharides. Archives of Virology 56(3): 251-5. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Two carbohydrate fractions can be obtained
from egg-grown influenza virus after Pronase digestion followed by gel
chromatography. One fraction contains glycopeptides (MW ca. 2000--2600) which
represent the carbohydrate side chains of the viral glycoproteins. The
constituent sugars of this material are fucose, galactose, glucosamine, and
mannose, and their position within the side chain has been partially elucidated
by methylation studies. The other fraction (MW greatest than 6000) appears to
be mucopolysaccharide and is composed of fucose, galactose, glucose,
galactosamine, and glucosamine.
Descriptors: glycopeptides analysis, glycoproteins
analysis, glycosaminoglycans analysis, influenza A virus avian analysis,
influenza A virus analysis, chromatography, gas, fucose analysis, galactosamine
analysis, galactose analysis, glucosamine analysis, glucose analysis, mannose
analysis.
Schwarz, R.T. and H.D. Klenk (1981). Carbohydrates
of influenza virus. IV. Strain-dependent variations. Virology 113(2):
584-93. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: glycoproteins analysis, hemagglutinins viral
analysis, influenza A virus analysis, oligosaccharides analysis, viral
proteins analysis, influenza A virus avian analysis, human analysis, porcine
analysis, influenza A virus classification, serotyping, species specificity.
Schwarz, R.T. and H.D. Klenk (1974). Proceedings:
Inhibition of glycosylation of the influenza virus hemagglutinin. Hoppe
Seyler's Zeitschrift Fur Physiologische Chemie 355(10): 1254. ISSN: 0018-4888.
NAL
Call Number: 384 Z38
Descriptors: glycoproteins biosynthesis, hemagglutinins
viral metabolism, influenza A virus avian metabolism, viral proteins
biosynthesis, deoxyglucose pharmacology, depression, chemical, glucosamine
pharmacology.
Schwarz, R.T., J.M. Rohrschneider, and M.F. Schmidt
(1976). Suppression of glycoprotein formation of Semliki Forest, influenza,
and avian sarcoma virus by tunicamycin. Journal of Virology 19(3):
782-91. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Tunicamycin, a new antibiotic, halts the formation
of physical particles of Semliki forest and fowl plague virus, whereas avian
oncornavirus particles which show a reduction in infectivity and do not contain
detectable labeled glycoprotein are released in the presence of the drug. In
Semliki forest virus-infected cells only the protein moieties of the
glycoproteins could be labeled. In cells infected with fowl plague and avian
sarcoma virus neither intact glycoproteins nor their protein moieties could be
detected. By using a protease inhibitor (N-alpha-p-tosyl-L-lysin chloromethyl
ketone, TLCK) it could be shown, however, that the carbohydrate-free
hemagglutinin precursor of influenza virus is synthesized but is presumably
degraded by intracellular proteases in the absence of TLCK as a consequence of the
lack of carbohydrate.
Descriptors: anti bacterial agents pharmacology,
glycoproteins biosynthesis, influenza A virus avian drug effects, sarcoma
viruses, avian drug effects, Semliki Forest virus drug effects, viral proteins
biosynthesis, chick embryo, glucosamine analogs and derivatives, glucosamine metabolism, glucosamine
pharmacology, hemagglutinins viral analysis, avian metabolism, mannose
metabolism, sarcoma viruses, avian metabolism, Semliki Forest virus metabolism,
tissue culture, tosyllysine chloromethyl ketone pharmacology.
Schwarz, R.T. and C. Scholtissek (1973). Purification
and properties of the RNA polymerase-template complex of an influenza virus.
Zeitschrift Fur Naturforschung. Teil C Biochemie, Biophysik, Biologie,
Virologie 28(3): 202-7. ISSN:
0341-0471.
NAL
Call Number: QH301.Z4
Descriptors: DNA directed RNA polymerases analysis,
influenza A virus avian enzymology, adenosine triphosphate, chick embryo, RNA
viral biosynthesis, templates, genetic.
Sears, S.D., M.L. Clements, R.F. Betts, H.F. Maassab,
B.R. Murphy, and M.H. Snyder (1988). Comparison of live, attenuated H1N1 and
H3N2 cold-adapted and avian-human influenza A reassortant viruses and
inactivated virus vaccine in adults. Journal of Infectious Diseases
158(6): 1209-19. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: The infectivity, immunogenicity, and efficacy
of live, attenuated influenza A/Texas/1/85 (H1N1) and A/Bethesda/1/85 (H3N2)
avian-human (ah) and cold-adapted (ca) reassortant vaccines were compared in
252 seronegative adult volunteers. The immunogenicity and efficacy of the H1N1
reassortant vaccine were also compared with those of the trivalent inactivated
virus vaccine. Each reassortant vaccine was satisfactorily attenuated. The 50%
human infectious dose was 10(4.9) for ca H1N1, 10(5.4) for ah H1N1, 10(6.4) for
ca H3N2, and 10(6.5) TCID50 for ah H3N2 reassortant virus. Within a subtype,
the immunogenicities of ah and ca vaccines were comparable. Five to seven weeks
after vaccination, volunteers were challenged with homologous wild-type
influenza A virus. The magnitude of shedding of virus after challenge was
greater than 100-fold less in H1N1 vaccinees and greater than 10-fold less in
H3N2 vaccinees compared with unimmunized controls. The vaccines were equally
efficacious, as indicated by an 86%-100% reduction in illness. Thus, the ah
A/Mallard/New York/6750/78 and the ca A/Ann Arbor/6/60 reassortant viruses are
comparable.
Descriptors: influenza prevention and control, influenza A
virus avian immunology, human immunology, influenza vaccine, adult, antibodies,
viral biosynthesis, cold, double blind method, enzyme linked immunosorbent
assay, hemagglutination inhibition tests, avian pathogenicity, avian
physiology, human pathogenicity, human physiology, random allocation, vaccines,
attenuated, vaccines, synthetic, virus replication.
Sekellick, M.J., S.A. Carra, A. Bowman, D.A. Hopkins,
and P.I. Marcus (2000). Transient resistance of influenza virus to
interferon action attributed to random multiple packaging and activity of NS
genes. Journal of Interferon and Cytokine Research the Official Journal
of the International Society for Interferon and Cytokine Research 20(11):
963-70. ISSN: 1079-9907.
Abstract: Interferon (IFN) action survival curves for
an avian influenza virus (AIV) in chicken or quail cells showed that 40-60% of
the virions in a stock of virus were highly sensitive to the inhibitory effects
of chicken IFN-alpha (ChIFN-alpha), whereas the rest were up to 100 times less
sensitive. This greater resistance to IFN was transient, that is, was not a
stable characteristic, in that virus stocks grown from plaques that formed in
the presence of 50-800 U/ml IFN gave rise to virus populations that contained
both sensitive and resistant virions. If AIV was serially passaged several
times in the presence of IFN, the proportion of transiently IFN-resistant virus
was greater. We propose a model to account for this transient resistance of AIV
to IFN action based on the reported inactivation of the dsRNA-dependent protein
kinase (PKR) and its activator dsRNA by the NS1 protein of influenza virus and
also on the increase in the survival of AIV in IFN-treated cells exposed to
2-aminopurine, a known inhibitor of PKR. We suggest that IFN-resistant AIV is generated
from a random packaging event that results in virions that contain two or more
copies of RNA segment 8, the gene segment that encodes the NS1 protein of AIV,
and that these virions will produce correspondingly elevated levels of NS1. The
experimental data fit well to theoretical curves based on this model and
constructed from the fraction of virus in the population expected by chance to
contain one, two, or three copies of the NS gene when packaging an average of
12 influenza gene segments that include the 8 segments essential for
infectivity.
Descriptors: influenza A virus avian genetics, avian
physiology, interferon alpha pharmacology, viral nonstructural proteins
genetics, virus assembly, 2 aminopurine pharmacology, chick embryo, genes viral
, half life, avian growth and development, interferon alpha administration and
dosage, plaque assay, serial passage, viral nonstructural proteins metabolism,
EIF 2 kinase antagonists and inhibitors.
Sekellick, M.J., D. Hopkins, A. Bowman, and P.I.
Marcus (1997). IFN sensitivity of avian influenza. Journal of
Interferon and Cytokine Research the Official Journal of the International
Society for Interferon and Cytokine Research 17(Suppl. 2): S73. ISSN: 1079-9907.
Descriptors: endocrine system, infection, avian influenza,
viral disease, interferon resistance interferon sensitivity (IFN sensitivity)
viral sensitivity, meeting abstract, meeting poster.
Semenova, N.P., E.N. Kantorovich Prokudina, I.A.
Miasnikova, and O.N. Berezina (1978). Ispol'zovanie metoda bliashek dlia
vyiavleniia fenomena autointerferentsii u virusa grippa. [Use of the plaque
method to reveal the phenomenon of autointerference in influenza virus]. Voprosy
Virusologii (6): 709-13. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The paper describes a simple and convenient
method for qualitative and quantitative evaluation of the capacity of influenza
virus for autointerference consisting in the lack or considerable reduction of
the cytolytic effect of the virus under agar overlay at a high multiplicity of
infection. Some experimental and theoretical arguments assuming the role of
defective interfering particles in the formation of the observed phenomenon. It
is assumed that the detection of autointerference under agar may be used as an
additional criterion for detection of non-plaque-forming strains of influenza
virus, tentative determination of their interfering capacity as well as for the
establishment of biological relationships of viruses.
Descriptors: influenza A virus physiology, viral
interference, defective viruses, influenza A virus avian, plaque assay.
Semenova, N.P., E.N. Prokudina, V.M. Chumakov, I.A.
Rudneva, I.G. Fediakina, and S.S. Iamnikova (2000). Zavisimost'
oligomerizatsii nukleoproteina virusa grippa ot vidovoi prinadlezhnosti
virusa. [Dependence of oligomerization
of influenza virus nucleoprotein on the species affiliation of the virus]. Voprosy
Virusologii 45(6): 12-7. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Comparison of human and avian influenza virus
nucleoprotein (NP) oligomerization showed that the efficiency of NP
oligomerization is different in influenza viruses of different origin. NP
oligomerization is virtually complete in avian influenza viruses, while in
human influenza viruses only part of monomeric NP is oligomerized. The authors
discuss the utilization of NP oligomerization efficiency as a sign for
identification of the origin of influenza virus.
Descriptors: influenza A virus metabolism, nucleoproteins
metabolism, biopolymers, birds virology, cell line, dogs, influenza A virus
classification, species specificity.
Semenova, N.P., Y.N. Prokudina, V.M. Chumakov, I.A.
Rudneva, I.G. Fedyakina, and S.S. Yamnikova (2000). Relationship between
influenza virus nucleoprotein oligomerization and species appurtenance of the
virus. Voprosy Virusologii (6): 12-17. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Comparison of human and avian influenza virus
nucleoprotein (NP) oligomerization showed that the efficiency of NP
oligomerization is different in influenza viruses of different origin. NP
oligomerization is virtually complete in avian influenza viruses, while in
human influenza viruses only part of monomeric NP is oligomerized. The authors
discuss the utilization of NP oligomerization efficiency as a sign for
identification of the origin of influenza virus.
Descriptors: biochemistry and molecular biophysics,
infection, virology.
Senne, D.A., B. Panigrahy, Y. Kawaoka, J.E. Pearson,
J. Suss, M. Lipkind, H. Kida, and R.G. Webster (1996). Survey of the
hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses:
amino acid sequence at the HA cleavage site as a marker of pathogenicity
potential. Avian Diseases 40(2): 425-437. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The deduced amino acid sequence at the
hemagglutinin (HA) cleavage site of 76 avian influenza (AI) viruses, subtypes
H5 and H7, was determined by reverse transcription-polymerase chain reaction
and cycle sequencing techniques to assess pathogenicity. Eighteen of the 76
viruses were isolated in 1993 and 1994 from various sources in the United
States. In addition, 34 H5 (4 highly pathogenic [HP] and 30 non-highly
pathogenic [nonHP]) and 24 H7 (3 HP and 21 non-HP) repository viruses, isolated
between 1927 and 1992, were sequenced and the sequences compared to those in
recent isolates. All repository HP H5 and H7 viruses studied had multiple basic
amino acids adjacent to the HA cleavage site and most had basic amino acids in
excess of the proposed minimum motif B-X-B-R (B = basic amino acids arginine or
lysine, X = nonbasic amino acid, R = arginine) that has been associated with
high pathogenicity. Of the non-HP viruses studied, 35 of 38 for H5 and 30 of 31
for H7 conformed to the motif B-X-X-R and B-X-R, respectively. Two nonHP HS
viruses had the motif X-X-X-R at the cleavage site and a third had the motif
B-X-X-K (K = basic amino acid lysine). One non-HP H7 (A/Pekin
robin/CA/30412-5/94) had four basic amino acids (K-R R-R) adjacent to the
cleavage site. Although the Pekin robin isolate did not produce disease in
chickens under the conditions of the study it did have the amino acid sequence
compatible with that in HP AI viruses and, therefore, is considered potentially
HP. This is the first account of an H7 virus that is non-HP in chickens but
meets the molecular criterion to be classified as HP.
Descriptors: United States, avian influenza virus,
chemical composition, nucleotide sequence, agglutinins, pathogenicity, PCR,
DNA, acids, America, biological properties, genomes, influenza virus, microbial
properties, North America, nucleic acids, nucleic compounds, organic
acids, orthomyxoviridae, proteins,
viruses, molecular sequence data, characterization, DNA sequencing.
Seo, S.H., E. Hoffmann, and R.G. Webster (2004). The
NS1 gene of H5N1 influenza viruses circumvents the host anti-viral cytokine
responses. Virus Research 103(1-2): 107-13. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The H5N1 influenza viruses transmitted to
humans in 1997 were highly virulent, but the mechanism of their virulence in humans
is largely unknown. Here we show that lethal H5N1 influenza viruses, unlike
other human, avian, and swine influenza viruses, are resistant to the
anti-viral effects of interferons and tumor necrosis factor alpha The
nonstructural (NS) gene of H5N1 viruses is associated with this resistance.
Pigs infected with recombinant human H1N1 influenza virus that carried the H5N1
NS gene experienced significantly greater and more prolonged viremia, fever,
and weight loss than did pigs infected with wild-type human H1N1 influenza
virus. These effects required the presence of glutamic acid at position 92 of
the NS1 molecule. These findings may explain the mechanism of the high
virulence of H5N1 influenza viruses in humans and provide insight into the
virulence of 1918 Spanish influenza.
Descriptors: cytokines pharmacology, drug resistance,
multiple, viral genetics, influenza immunology, avian influenza A virus
pathogenicity, human influenza A virus pathogenicity, viral nonstructural
proteins genetics, cell line, cytokines metabolism, influenza physiopathology,
influenza virology, avian influenza A virus genetics, interferons metabolism,
interferons pharmacology, mutation, recombination, genetic, swine virology,
tumor necrosis factor alpha metabolism, tumor necrosis factor alpha
pharmacology.
Seo, S.H. and R.G. Webster (2001). Cross-reactive,
cell-mediated immunity and protection of chickens from lethal H5N1 influenza
virus infection in Hong Kong poultry markets. Journal of Virology
75(6): 2516-25. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: In 1997, avian H5N1 influenza virus
transmitted from chickens to humans resulted in 18 confirmed infections.
Despite harboring lethal H5N1 influenza viruses, most chickens in the Hong Kong
poultry markets showed no disease signs. At this time, H9N2 influenza viruses
were cocirculating in the markets. We investigated the role of H9N2 influenza
viruses in protecting chickens from lethal H5N1 influenza virus infections.
Sera from chickens infected with an H9N2 influenza virus did not cross-react
with an H5N1 influenza virus in neutralization or hemagglutination inhibition
assays. Most chickens primed with an H9N2 influenza virus 3 to 70 days earlier
survived the lethal challenge of an H5N1 influenza virus, but infected birds
shed H5N1 influenza virus in their feces. Adoptive transfer of T lymphocytes or
CD8(+) T cells from inbred chickens (B(2)/B(2)) infected with an H9N2 influenza
virus to naive inbred chickens (B(2)/B(2)) protected them from lethal H5N1
influenza virus. In vitro cytotoxicity assays showed that T lymphocytes or
CD8(+) T cells from chickens infected with an H9N2 influenza virus recognized
target cells infected with either an H5N1 or H9N2 influenza virus in a
dose-dependent manner. Our findings indicate that cross-reactive cellular
immunity induced by H9N2 influenza viruses protected chickens from lethal
infection with H5N1 influenza viruses in the Hong Kong markets in 1997 but
permitted virus shedding in the feces. Our findings are the first to suggest that
cross-reactive cellular immunity can change the outcome of avian influenza
virus infection in birds in live markets and create a situation for the
perpetuation of H5N1 influenza viruses.
Descriptors: chickens, fowl plague immunology, fowl plague
virology, influenza A virus avian immunology, T lymphocytes, cytotoxic
immunology, adoptive transfer, cross reactions, fowl plague prevention and
control, hemagglutination inhibition tests, Hong Kong, immunity, cellular,
immunization, avian classification, avian pathogenicity.
Seo, S.H. and R.G. Webster (2002). Tumor necrosis
factor alpha exerts powerful anti-influenza virus effects in lung epithelial
cells. Journal of Virology 76(3): 1071-6. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Previous studies have associated influenza
virus-induced expression of inflammatory cytokines, including tumor necrosis
factor alpha (TNF-alpha), with influenza pathogenesis in the human respiratory
tract and have suggested that alpha and beta interferons are the first cytokines
recruited to counteract such infection. However, we report here that TNF-alpha
has powerful anti-influenza virus activity. When infected with influenza virus,
cultured porcine lung epithelial cells expressed TNF-alpha in a dose-dependent
manner. Expression of TNF-alpha was induced only by replicating virus.
TNF-alpha showed strong antiviral activity against avian, swine, and human
influenza viruses, and the antiviral effect of TNF-alpha was greater than that
of gamma or alpha interferon. These findings suggest that TNF-alpha serves as
the first line of defense against influenza virus infection in the natural
host.
Descriptors: antiviral agents immunology, influenza A
virus avian immunology, human immunology, porcine immunology, influenza B virus
immunology, tumor necrosis factor immunology, antiviral agents pharmacology,
cell line, chick embryo, gene expression, avian drug effects, avian physiology
, human drug effects, human physiology,
porcine drug effects, porcine physiology, influenza B virus drug effects,
influenza B virus physiology, interferon type II immunology, interferon type II
pharmacology, interferon alpha immunology, interferon alpha pharmacology,
interferon beta immunology, interferon beta pharmacology, swine, tumor necrosis
factor biosynthesis, tumor necrosis factor genetics, tumor necrosis factor
pharmacology, virus replication drug effects.
Serkedjieva, J. (2000). Combined antiinfluenza
virus activity of Flos verbasci infusion and amantadine derivatives.
Phytotherapy Research PTR 14(7): 571-4.
ISSN: 0951-418X.
NAL
Call Number: RS164.P59
Descriptors: amantadine pharmacology, antiviral agents
pharmacology, influenza A virus avian drug effects, plant extracts
pharmacology, amantadine administration and dosage, amantadine analogs and
derivatives, antiviral agents administration and dosage, cultured cells, chick
embryo, drug therapy, combination, fibroblasts drug effects, hemagglutination,
influenza prevention and control, avian classification, phytotherapy, plants,
medicinal therapeutic use.
Serkedjieva, J. (1995). Inhibition of influenza
virus protein synthesis by a plant preparation from Geranium sanguineum L.
Acta Virologica 39(1): 5-10.
ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: A polyphenolic complex (PC) with antiviral
properties has been isolated from the Bulgarian medicinal plant Geranium
sanguineum L. A study was undertaken to investigate the effect of PC on
virus-specific protein synthesis in influenza virus-infected cells. The
expression of viral glycoproteins on the surface of chick embryo fibroblasts
infected with virus A/FPV, strain Rostock (H7N1) was suppressed. Virus protein
synthesis was selectively inhibited as shown by SDS polyacrylamide gel
electrophoresis of 35S-methionine-labelled proteins and proteins
immunoprecipitated with monoclonal antibodies. The inhibitory effect was
dose-dependent and better pronounced when PC was applied after virus infection.
Two variants of influenza virus FPV/Rostock with reduced drug susceptibility
were selected. PC affected to a lesser extent the synthesis of viral proteins
in cells infected with the variants as compared to the sensitive parental
virus.
Descriptors: antiviral agents pharmacology, influenza A
virus avian drug effects, phenols pharmacology, plants medicinal chemistry,
viral proteins biosynthesis, cultured cells, chick embryo, plant roots
chemistry, protein synthesis inhibitors pharmacology.
Serkedjieva, J., M. Konaklieva, S. Dimitrova
Konaklieva, V. Ivanova, K. Stefanov, and S. Popov (2000). Antiinfluenza
virus effect of extracts from marine algae and invertebrates. Zeitschrift
Fur Naturforschung. C, Journal of Biosciences 55(1-2): 87-93. ISSN: 0341-0382.
NAL
Call Number: QH301.Z4
Abstract: Sixty products, derived from marine
organisms, typical of the Bulgarian Black Sea coast, were examined for
inhibitory activity on the reproduction of influenza viruses in tissue
cultures. The antiviral effect was investigated by the reduction of virus infectivity.
Using representative strains of influenza virus it was shown that apparently
the inhibitory effect was strain-specific. The most effective products were
further studied in fertile hen's eggs and in experimental influenza infection
in white mice.
Descriptors: algae chemistry, antiviral agents
pharmacology, influenza drug therapy, influenza A virus avian drug effects,
human drug effects, plant extracts pharmacology, tissue extracts pharmacology,
antiviral agents isolation and purification, chick embryo, hemagglutination
inhibition tests, invertebrates, mice, seawater, species specificity.
Serkedjieva, J. and M. Velcheva (2003). In vitro
anti-influenza virus activity of the pavine alkaloid (-)-thalimonine isolated
from Thalictrum simplex L. Antiviral Chemistry and Chemotherapy
14(2): 75-80. ISSN: 0956-3202.
Abstract: The pavine alkaloid (-)-thalimonine (Thl),
isolated from the Mongolian plant Thalictrum simplex inhibited markedly
the reproduction of influenza virus A/Germany/27, str. Weybridge (H7N7) and
A/Germany/34, str. Rostock (H7N1) in cell cultures of chicken embryo
fibroblasts. In a number of assays at a non-toxic concentration range of
0.1-6.4 microM the alkaloid inhibited viral reproduction in a selective and
specific way (selectivity index = 640, 106.6, respectively). Expression of
viral glycoproteins haemagglutinin (HA), neuraminidase (NA) and nucleoprotein
(NP) on the surface of infected cells, virus-induced cytopathic effect,
infectious virus yields, HA production and virus-specific protein synthesis
were all reduced. The inhibition was dose-related and depended on virus
inoculum. The time of addition experiments indicated that viral reproduction
was markedly inhibited when Thl was added at 4-5 h of infection. No inactivating
effect on extracellular virus was found.
Descriptors: alkaloids pharmacology, antiviral agents
pharmacology, benzylisoquinolines pharmacology, influenza A virus avian drug
effects, Thalictrum chemistry, alkaloids isolation and purification, benzylisoquinolines
isolation and purification, chick embryo, dose response relationship, drug,
enzyme linked immunosorbent assay, fibroblasts cytology, fibroblasts drug
effects, fibroblasts virology, hemagglutinin glycoproteins, influenza virus
drug effects, hemagglutinin glycoproteins, influenza virus metabolism, avian
metabolism, neuraminidase antagonists and inhibitors, neuraminidase metabolism,
nucleoproteins drug effects,
nucleoproteins metabolism, plant extracts pharmacology, time factors.
Serkedzhieva, I.U. (1979 ). Protivovirusna
aktivnostn na razlichni interferonovi induktori. [Antiviral activity of
different interferon inducers]. Acta Microbiologica Bulgarica 3:
44-9. ISSN: 0204-8809.
NAL
Call Number: QR1.A37
Descriptors: influenza A virus avian drug effects,
interferon inducers pharmacology, pyrimidines pharmacology.
Serkedzhieva, I.U., I. Gagov, and G. Georgiev (1975).
Prouchvane na interferon-indutsirashchata aktivnost na niakoi
novosintezirani s'edineniia ot grupata na khidroksipirimidina. II s'obshchenie
[Study of the interferon-inducing activity of various newly synthesized
compounds of the hydroxypyrimidine group in cell culture]. Acta
Microbiologica, Virologica Et Immunologica 2: 77-82. ISSN: 0324-0452.
NAL
Call Number: QR1.A3
Descriptors: interferon inducers, interferons
biosynthesis, pyrimidines pharmacology, chick embryo, fibroblasts, influenza A
virus avian drug effects, avian growth and development, interferons
pharmacology, tissue culture, virus replication drug effects.
Serkedzhieva, I.U., G. Georgiev, and M. Ivanova
(1975). Prouchvane na protivovirusnoto deistvie na novosintezirani
s'edineniia ot grupata na khidroksipirimidina [Study of the antiviral action of
newly synthesized compounds of the hydroxypirimidine group]. Acta
Microbiologica, Virologica Et Immunologica 2: 73-6. ISSN: 0324-0452.
NAL
Call Number: QR1.A3
Descriptors: antiviral agents pharmacology, influenza A
virus avian drug effects, pyrimidines pharmacology, cytopathogenic effect,
viral drug effects, avian growth and development, tissue culture, virus
replication drug effects.
Seto, J.T. and F.S. Chang (1969). Functional
significance of sialidase during influenza virus multiplication: an electron
microscope study. Journal of Virology 4(1): 58-66. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Descriptors: influenza A virus avian enzymology,
neuraminidase, orthomyxoviridae enzymology, virus replication, cell line, chick
embryo, conjunctiva, immune sera, microscopy, electron, tissue culture.
Seto, J.T. and R. Rott (1966). Functional
significance of sialidose during influenza virus multiplication. Virology
30(4): 731-7. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian enzymology, avian
growth and development, neuraminidase metabolism, adsorption, chick embryo,
complement fixation tests, immune sera, neutralization tests.
Sha, B. and M. Luo (1997). Structure of a
bifunctional membrane-RNA binding protein, influenza virus matrix protein M1.
Nature Structural Biology 4(3): 239-44.
ISSN: 1072-8368.
Abstract: Matrix protein (M1) of influenza virus is a
bifunctional protein that mediates the encapsidation of RNA-nucleoprotein cores
into the membrane envelope. It is therefore required that M1 binds both
membrane and RNA simultaneously. The X-ray crystal structure of the N-terminal
portion of type A influenza virus M1-amino acid residues 2-158-has been
determined at 2.08 A resolution at pH 4.0. The protein forms a dimer. A highly
positively charged region on the dimer surface is suitably positioned to bind
RNA while the hydrophobic surface opposite the RNA binding region may be
involved in interactions with the membrane. The membrane-binding hydrophobic
surface could be buried or exposed after a conformational change.
Descriptors: protein structure, secondary, RNA binding
proteins chemistry, viral matrix proteins chemistry, amino acid sequence,
crystallography, x-ray, dimerization, influenza A virus avian, human,
macromolecular systems, models, molecular, models, structural, molecular sequence
data, RNA binding proteins isolation and purification, sequence homology, amino
acid, software, viral matrix proteins isolation and purification.
Shalaby, A.A., R.D. Slemons, and D.E. Swayne (1994). Pathological
studies of A/chicken/Alabama/7395/75 (H4N8) influenza virus in
specific-pathogen-free laying hens. Avian Diseases 38(1):
22-32. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Specific-pathogen-free laying hens were
inoculated with avian influenza virus (AIV) A/chicken/Alabama/7395/75 (H4N8)
either intratracheally (IT) or intravenously (IV). IT inoculation produced a
localized infection of the upper and lower respiratory tracts with lesions of
tracheitis, bronchitis, airsacculitis, and pneumonia around the secondary bronchi.
IV inoculation produced a systemic infection with major lesions of nephritis,
interstitial pneumonia, salpingitis, and splenic and hepatic necrosis. In
IV-inoculated hens, AIV nucleo-protein was demonstrated within renal tubule
epithelium, in luminal surface and glandular oviduct epithelium, and in
mononuclear cells within pulmonary blood capillaries. However, no virus was
recovered from internal contents of eggs laid between days 1.5 and 5
postinfection. These data indicate that A/chicken/Alabama/7395/75 has tissue
tropism and pathogenicity for the respiratory and urogenital systems of
reproductively active laying hens. Site and severity of lesion development are
determined by the localized or systemic nature of AIV infection.
Descriptors: fowl plague pathology, influenza A virus
avian isolation and purification, chickens, kidney microbiology, kidney
pathology, lung microbiology, lung pathology, ovary microbiology, ovary
pathology, oviducts microbiology, oviducts pathology, oviposition, specific pathogen
free organisms.
Shinjoh, M., T. Yoshikawa, Y. Li, K. Shiraishi, H.
Ueki, and K. Nerome (2002). Prophylaxis and treatment of influenza
encephalitis in an experimental mouse model. Journal of Medical Virology
67(3): 406-17. ISSN: 0146-6615.
Descriptors: amantadine therapeutic use, antibodies, viral
therapeutic use, antiviral agents therapeutic use, encephalitis, viral drug
therapy, encephalitis, viral prevention and control, influenza A virus avian
pathogenicity, influenza vaccine therapeutic use, antibodies, viral blood,
brain pathology, brain virology, disease models, animal, dogs, encephalitis,
viral mortality, encephalitis, viral pathology, avian immunology, influenza
vaccine administration and dosage, lung pathology, lung virology, mice, treatment
outcome, vaccines, inactivated administration and dosage, vaccines, inactivated
therapeutic use.
Shinya, K., S. Hamm, M. Hatta, H. Ito, T. Ito, and Y.
Kawaoka (2004). PB2 amino acid at position 627 affects replicative
efficiency, but not cell tropism, of Hong Kong H5N1 influenza A viruses in
mice. Virology 320(2):
258-66. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: A single amino acid substitution, from
glutamic acid to lysine at position 627 of the PB2 protein, converts a
nonlethal H5N1 influenza A virus isolated from a human to a lethal virus in
mice. In contrast to the nonlethal virus, which replicates only in respiratory
organs, the lethal isolate replicates in a variety of organs, producing
systemic infection. Despite a clear difference in virulence and organ tropism
between the two viruses, it remains unknown whether the dissimilarity is a
result of differences in cell tropism or the reduced replicative ability of the
nonlethal virus in mouse cells in general. To determine how this single amino
acid change affects virulence and organ tropism in mice, we investigated the
growth kinetics of the two H5N1 viruses both in vitro and in vivo. The identity
of the PB2 amino acid at position 627 did not appreciably affect viral
replicative efficiency in chicken embryo fibroblasts and a quail cell line;
however, viruses with lysine at this position instead of glutamic acid grew
better in the different mouse cells tested. When the effect of this
substitution was investigated in mice, all of the test viruses showed the same
cell tropism, but infection by viruses containing lysine at position 627 spread
more rapidly than those viruses containing glutamic acid at this position.
Further analysis showed a difference in local immune responses: neutrophil
infiltration in lungs infected with viruses containing lysine at position 627
persisted longer than that associated with viruses lacking a glutamic acid
substitution. Our data indicate that the amino acid at position 627 of the PB2
protein determines the efficiency of viral replication in mouse (not avian)
cells, but not tropism among cells in different mouse organs. The presence of
lysine leads to more aggressive viral replication, overwhelming the host's
defense mechanisms and resulting in high mortality rates in mice.
Descriptors: amino acid substitution, avian influenza A
virus pathogenicity, avian influenza A virus physiology, viral proteins
genetics, virus replication, brain virology, cell line, chick embryo, influenza
physiopathology, influenza virology, avian influenza A virus genetics, mice,
viral proteins chemistry, viral proteins metabolism, virulence.
Shinya, K., A. Shimada, T. Ito, K. Otsuki, T. Morita,
H. Tanaka, A. Takada, H. Kida, and T. Umemura (2000). Avian influenza virus
intranasally inoculated infects the central nervous system of mice through the
general visceral afferent nerve. Archives of Virology 145(1):
187-95. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: To define the route of influenza virus
invasion into the central nervous system (CNS), an avian influenza A (H5N3)
virus was inoculated into mice intranasally or intravenously. Only the
intranasal infection group mice showed depression and retention of gas in the
digestive system. Pathological findings in the animals were bronchointerstitial
pneumonia and non-suppurative encephalitis restricted to the brain stem. The
nerve nucleus primarily affected was the nucleus of solitary tract. Prior to
the development of the CNS lesions, viral antigen was detected in vagal and trigeminal
ganglia. These results suggest that the primarily replicated virus in the
respiratory mucosa ascended to the CNS via sensory nerve routes, inducing
lesions in the brain stem, and then spread trans-synaptically in the CNS.
Descriptors: encephalitis, viral virology, influenza A
virus avian pathogenicity, orthomyxoviridae infections virology, visceral
afferents virology, antigens, viral analysis, brain pathology, brain virology,
brain stem pathology, brain stem virology, encephalitis, viral pathology,
ganglia virology, avian isolation and purification, lung virology, mice inbred
BALB c, orthomyxoviridae infections pathology, respiratory mucosa virology.
Shinya, K., F.D. Silvano, T. Morita, A. Shimada, M.
Nakajima, T. Ito, K. Otsuki, and T. Umemura (1998). Encephalitis in mice
inoculated intranasally with an influenza virus strain originated from a water
bird. Journal of Veterinary Medical Science the Japanese Society of
Veterinary Science 60(5): 627-9.
ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Abstract: Five-week-old ddY mice were inoculated
intranasally with a low virulent (4e) or highly virulent (24a5b) avian
influenza virus strain originated from a water bird. None of mice in the 4e
group showed clinical signs and brain lesions. Of the 24a5b group, two mice
died and one mouse was killed at a moribund state at day 7 post-inoculation
(PI). Four mice of the 24a5b group necropsied at day 5 or 7 PI had mild to
severe encephalitis in the brain stem and the cerebellar white matter.
Influenza virus antigen was detected in neurons, glial cells and vascular
endothelium in the lesions. The distribution of the lesions seems to indicate
the transneuronal invasion of the virus via cranial nerve fibers into the
brain.
Descriptors: birds virology, brain pathology,
encephalitis, viral pathology, influenza pathology, influenza A virus avian
pathogenicity, antigens, viral analysis, brain virology, brain stem pathology,
cerebellum pathology, encephalitis, viral virology, immunohistochemistry, avian
isolation and purification, mice, necrosis, virulence.
Shishkov, A.V., V.I. Goldanskii, L.A. Baratova, N.V.
Fedorova, A.L. Ksenofontov, O.P. Zhirnov, and A.V. Galkin (1999 ). The in
situ spatial arrangement of the influenza A virus matrix protein M1 assessed by
tritium bombardment. Proceedings of the National Academy of Sciences of
the United States of America 96(14): 7827-30. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Intact influenza A virions were bombarded
with thermally activated tritium atoms, and the intramolecular distribution of
the label in the matrix protein M1 was analyzed to determine the in situ
accessibility of its tryptic fragments. These data were combined with the
previously reported x-ray crystal structure of the M1 fragment 2-158 [Sha, B.
& Luo, M. (1997) Nat. Struct. Biol. 4, 239-244] and the predicted topology
of the C domain (159-252) to propose a model of M1 arrangement in the virus
particle.
Descriptors: influenza A virus avian physiology, protein
structure, secondary, viral matrix proteins chemistry, chick embryo,
crystallography, x-ray, avian ultrastructure, models, molecular, tritium, viral
matrix proteins isolation and purification.
Shneider, M.A., V.I. Golovkin, N.P. Chizhov, and E.B.
Shtil'bans (1987 ). Amfogliukamin v kompleksnoi khimioterapii nekotorykh
virusnykh zabolevanii. [Amphoglucamine in the combined chemotherapy of viral
diseases]. Voprosy Virusologii 32(6): 736-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: amphotericin B analogs and derivatives,
influenza drug therapy, multiple sclerosis drug therapy, amphotericin B
pharmacology, amphotericin B therapeutic use, amphotericin B toxicity, chick
embryo, drug evaluation, drug evaluation, preclinical, drug therapy,
combination, influenza A virus avian drug effects, mice, rimantadine
therapeutic use, tilorone therapeutic use, virus replication drug effects.
Shortridge, K.F., A.P. King, and R.G. Webster (1987).
Monoclonal antibodies for characterizing H3N2 influenza viruses that persist
in pigs in China. Journal of Infectious Diseases 155(3):
577-81. ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Descriptors: antigens, viral immunology, influenza A
virus, porcine immunology, influenza A virus immunology, swine microbiology,
viral core proteins, antibodies, monoclonal immunology, antibodies, viral
immunology, antigens, viral analysis, China, cross reactions, epitopes,
hemagglutinins viral immunology, Hong Kong, avian immunology, human immunology,
neuraminidase immunology, nucleoproteins immunology, Taiwan, viral proteins
immunology.
Shortridge, K.F., P.A. Underwood, and A.P. King
(1990). Antigenic stability of H3 influenza viruses in the domestic duck
population of southern China. Archives of Virology 114(1-2):
121-36. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: An antigenic analysis was carried out on 145
duck influenza virus isolates of the H3 haemagglutinin subtype obtained over
five years continuous surveillance from the region of southern China, a
hypothetical influenza epicentre. This was done using a panel of twelve
monoclonal antibodies raised to an early human strain of the H3 subtype. We
demonstrate the existence of an extensive range of antigenic profiles, broadly
similar but not identical to the human H3 strain, which persisted over the five
year period. This variability was as great during discrete twelve month periods
as over the whole five years. Hierarchic progression (observed with human
strains) was not evident and no correlation of antigenic drift, in either
positive or negative direction, was observed with the domestic duck isolates
over time. Changing dominant antigenic profiles were, however, observed in
faecal isolates with time within a single farm. The much broader range of
profiles detected in pond water samples from the same farm suggested the
existence of a heterogeneous antigenic reservoir. Local switching of dominant
profiles may occur due to changes of cohorts as birds are taken to market. In
vitro and in vivo passage experiments revealed a high degree of heterogeneity
in antigenic profiles in progeny of uncloned isolates, whereas the profiles of
cloned isolates were largely conserved. These results suggested that particular
antigenic profiles in primary isolates may result from mixtures of
subpopulations of the wild type virus in natural duck infections. Switching
between reactivity profiles of different progeny is likely to be largely a
result of regrouping of these subpopulations with lesser effects due to
mutation. Hypervariability in some of the cloned isolates was observed with a
few monoclonal antibodies recognising a region of HA reported to be
hypervariable in swine influenza virus. Reactivity with one particular antibody
was correlated with passage in chicken eggs. The ability of this enormously
varied pool of duck influenza H3 strains to cross the species barrier to man
and give rise to viruses with hierarchic capabilities was considered.
Descriptors: antigens, viral immunology, ducks
microbiology, hemagglutinins viral immunology, influenza A virus avian
immunology, human immunology, antibodies, monoclonal immunology, antibodies,
viral immunology, CHI square distribution, China, hemagglutination inhibition
tests, serial passage.
Silvano, F.D., Y. Kanata, M. Takeuchi, A. Shimada, K.
Otsuki, and T. Umemura (1997). Avian influenza A virus induced stunting
syndrome-like disease in chicks. Journal of Veterinary Medical Science
the Japanese Society of Veterinary Science 59(3): 205-7. ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Abstract: Two-day-old specific-pathogen free chicks
were inoculated with type A influenza virus (A/whistling swan/Shimane/499/83
(H5N3) through the air sac. Inoculated chicks showed mild to severe diarrhea
and lesions of pancreatitis and atrophy of the pancreas, thymus and bursa of
Fabricius. One chick died on each of days 4, 6 and 14 postinoculation (PI).
Reduced weight gain was conspicuous from day 22 PI. Positive immunoreaction to
the virus antigen was detected in the pancreas, kidneys, liver, lungs and air
sacs, and cecal lamina propria. Virus recovery persisted longer in the
pancreas. Some of these findings conformed to those of stunting syndrome.
Descriptors: chickens, growth disorders veterinary,
influenza A virus avian physiology, poultry diseases virology, air sacs
immunology, air sacs virology, antigens, viral analysis, antigens, viral
immunology, atrophy, bursa of fabricius pathology, growth disorders pathology,
growth disorders virology, avian immunology, kidney immunology, kidney
virology, liver immunology, liver virology, lung immunology, lung virology,
pancreas pathology, pancreatitis etiology, pancreatitis pathology, pancreatitis
veterinary, poultry diseases pathology, poultry diseases physiopathology,
regression analysis, syndrome, thymus gland pathology, weight gain physiology.
Silvano, F.D., M. Yoshikawa, A. Shimada, K. Otsuki,
and T. Umemura (1997). Enhanced neuropathogenicity of avian influenza A
virus by passages through air sac and brain of chicks. Journal of
Veterinary Medical Science the Japanese Society of Veterinary Science
59(3): 143-8. ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Abstract: Three-day-old, specific-pathogen-free (SPF)
chicks were inoculated with the strains of influenza A/whistling swan/Shimane/
499/83 (H5N3) via the air sac route. The strains had been passaged through air
sacs or air sacs and brains of SPF chicks. Two experiments were undertaken to
examine the pathogenicity of these strains and the development of brain lesions
based on time-interval changes. In experiment 1, original strain (4e) showed
low pathogenicity with mild respiratory signs and zero mortality. Air sac
passaged strains (18a and 24a) of 4e demonstrated mortalities of 50% and 67%,
respectively, and inoculated chicks showed hemorrhages and necrotic lesions in
major organs. Air sac-brain passaged strain (24a5b) of 4e produced 100%
mortality and severe nervous signs. Severe circulatory disturbance with
multiple foci of necrosis in major organs including the brain was found in
chicks inoculated with 24a5b. The 24a5b was analogous to highly pathogenic
avian influenza virus in regard to its pathogenicity to chicks. Hence, low
pathogenic influenza virus (4e) gradually aggravated its pathogenicity to
highly pathogenic virus (24a5b) by air sac and brain passages. In experiment 2,
chicks were inoculated with 24a5b, and the earliest histological lesion was the
enlargement of the vascular endothelial cells at 18 hr post-inoculation (PI)
followed by necrotizing encephalitis at 24 to 48 hr PI. Immunohistological
staining revealed avian influenza virus antigen initially in the vascular
endothelial cells and then in the astrocytes, neurons and ependyma.
Descriptors: air sacs virology, brain virology, chickens,
fowl plague pathology, influenza A virus pathogenicity, air sacs pathology,
antigens, viral analysis, brain immunology, brain pathology, endothelium,
vascular pathology, influenza A virus immunology, microscopy, electron methods,
microscopy, electron veterinary, necrosis, neurons ultrastructure, serial passage,
specific pathogen free organisms, time factors.
Sivanandan, V., K.V. Nagaraja, D.A. Halvorson, and
J.A. Newman (1991). A quantitative measurement of the effect of avian
influenza virus on the ability of turkeys to eliminate Pasteurella multocida
from the respiratory tract. Research in Veterinary Science 51(3):
254-7. ISSN: 0034-5288.
NAL
Call Number: 41.8 R312
Abstract: The effect of avian influenza virus (AIV)
infection on the ability of turkeys to eliminate Pasteurella multocida
from the respiratory tract was evaluated. Four-week-old turkeys were
experimentally infected with an apathogenic AIV subtype (H5N2) by the
oculonasal route and subsequently superinfected with P multocida (Urbach
strain) by the intranasal route three days after infection with AIV.
Quantitative clearance of P multocida from the trachea and lung was
determined using a pour plate technique on samples collected at intervals after
infection. Samples from turkeys which had been infected with AIV were found to
yield more P multocida than those from turkeys which had not been
infected with AIV. The numbers of P multocida increased in infected
birds to a greater extent than in birds which had not been infected with the
virus. The present study suggests that AIV infection may contribute to the
increased numbers and a decreased clearance of P multocida in turkeys.
Descriptors: fowl plague microbiology, influenza A virus
avian physiology, Pasteurella infections veterinary, Pasteurella
multocida physiology, poultry diseases microbiology, turkeys, fowl plague
complications, Pasteurella infections complications, Pasteurella
infections microbiology, respiratory system microbiology.
Skehel, J.J. (1973). Early polypeptide synthesis
in influenza virus-infected cells. Virology 56(1): 394-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian metabolism, peptide
synthesis, viral proteins biosynthesis, autoradiography, chick embryo,
cycloheximide pharmacology, dactinomycin pharmacology, densitometry,
electrophoresis, polyacrylamide gel, fibroblasts, avian growth and development,
methionine metabolism, sulfur radioisotopes, time factors, tissue culture,
transcription, genetic, virus replication.
Skehel, J.J. (1972). Polypeptide synthesis in
influenza virus-infected cells. Virology 49(1): 23-36. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cultured cells metabolism, influenza A virus
avian growth and development, peptide synthesis, viral proteins biosynthesis,
amino acids metabolism, carbon isotopes, cattle, cell line microbiology, chick
embryo, electrophoresis, disc, fibroblasts microbiology, fucose metabolism,
glycopeptides biosynthesis, hamsters, haplorhini, HeLa cells microbiology,
avian analysis, avian metabolism, kidney embryology, methionine metabolism,
molecular weight, neoplasms, experimental, peptides analysis, sulfur isotopes,
virus replication.
Skehel, J.J. and D.C. Burke (1969). Ribonucleic
acid synthesis in chick embryo cells infected with fowl-plague virus. Journal
of Virology 3(4): 429-38. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Descriptors: influenza A virus avian metabolism, RNA
nucleotidyltransferases metabolism, RNA viral biosynthesis, carbon isotopes,
cell nucleus, centrifugation, density gradient, chick embryo, dactinomycin
pharmacology, edetic acid pharmacology, electrophoresis, disc, hydrogen-ion
concentration, avian isolation and purification, magnesium pharmacology,
manganese pharmacology, nucleotides metabolism, ribosomes, tissue culture, tritium,
uracil nucleotides metabolism, uridine metabolism, valine metabolism.
Skehel, J.J. and D.C. Burke (1968). Ribonucleic
acid synthesis in fowl-plague virus-infected chick-embryo cells. Biochemical
Journal 110(3): 41-42. ISSN:
0264-6021.
NAL
Call Number: QP501,B64
Descriptors: chick embryo, influenza A virus avian,
orthomyxoviridae infections enzymology, RNA viral biosynthesis, centrifugation,
density gradient, RNA nucleotidyltransferases metabolism, ribosomes enzymology.
Skehel, J.J. and A.J. Hay (1978). Nucleotide
sequences at the 5' termini of influenza virus RNAs and their transcripts. Nucleic
Acids Research 5(4): 1207-19. ISSN:
0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: The results of analyses of the 5'-terminal
sequences of Fowl Plague virus RNAs are presented. The first 13 residues of
each of the eight RNA molecules which constitute the genome are in the
identical sequence 5'AGUAGAAAUUAGG- and this conservation of sequence is shown
to extend to other influenza viruses. The 5'-terminal sequences of virion RNA
transcripts produced in vitro are also reported and again the first 12
nucleotides of these are identical for all influenza type A transcripts
examined in the sequence 5'AGCAAAAGCAGG-. In addition the results of attempts
to determine the sequence relationship between vRNAs and the two classes of
complementary RNA synthesized in influenza infected cells are described which
support the conclusion that influenza messenger RNAs are incomplete
transcripts.
Descriptors: influenza A virus avian, RNA viral analysis,
base sequence, RNA, messenger metabolism, ribonucleotides analysis, templates,
genetic, transcription, genetic.
Skehel, J.J., A.J. Hay, and J.A. Armstrong (1978). On
the mechanism of inhibition of influenza virus replication by amantadine
hydrochloride. Journal of General Virology 38(1): 97-110. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The results of analyses of fowl plague
virus-specific RNA and protein synthesis in infected chick embryo fibroblasts
incubated in amantadine hydrochloride are reported. They indicate that provided
amantadine is present from the time of virus addition no expression of the
virus genome occurs and that the synthesis of even the first detectable
transcripts catalysed by the polymerase of the infecting virus particles is
prevented. In agreement with previous reports it is concluded that amantadine
prevents an unknown event which occurs immediately following virus infection.
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, virus replication drug effects, chick embryo, DNA directed
RNA polymerases metabolism, hemagglutinins viral analysis, avian growth and
development, avian metabolism, peptide synthesis, RNA viral biosynthesis,
tissue culture, viral proteins biosynthesis.
Slemons, R.D. and B.C. Easterday (1978). Virus
replication in the digestive tract of ducks exposed by aerosol to type-A
influenza. Avian Diseases 22(3): 367-77. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Enteric infection and cloacal shedding of
influenza virus was demonstrated in ducks exposed experimentally to an aerosol
of an avirulent type-A influenza virus. The fluorescent-antibldy technique was
used to identify sites of virus replication in the epithelial cells of the
digestive tract and the bursa.
Descriptors: ducks microbiology, influenza A virus avian
growth and development, intestines microbiology, aerosols, antigens, viral
analysis, bursa of fabricius microbiology, cloaca microbiology, fluorescent
antibody technique, avian immunology, avian isolation and purification, trachea
microbiology, virus replication.
Slemons, R.D., L.N. Locke, M.G. Sheerar, R.M. Duncan,
V.S. Hinshaw, and B.C. Easterday (1990). Kidney lesions associated with
mortality in chickens inoculated with waterfowl influenza viruses. Avian
Diseases 34(1): 120-8. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Seventy-six type A influenza viruses
recovered from waterfowl in Wisconsin, California, South Dakota, Florida,
Texas, Alabama, and Nebraska were tested for virulence in chickens. The
challenge to chickens was intravenous inoculation of first-, second-, or
third-egg-passage virus. Each of the virus strains was tested separately in
three or four chickens. Eighteen of the 76 viruses caused the death of one or
more chickens following inoculation. Postmortem lesions were similar in all
dead birds. In decreasing order of frequency, gross lesions included: swollen
kidneys evident as accentuated lobular patterns, urates in the pericardial sac,
and urates on the surface of the liver. Microscopic lesions present in kidneys
were consistent with visceral gout. Mortality was associated with inoculations
having higher concentrations of infectious virus. These results indicate that
the influenza A viruses circulating in duck populations may include strains
potentially pathogenic for chickens.
Descriptors: chickens, fowl plague pathology, influenza A
virus avian pathogenicity, kidney pathology, animals, wild, antibodies, viral
biosynthesis, birds, ducks, fowl plague microbiology, fowl plague mortality,
geese, avian immunology, avian isolation and purification, virulence.
Slemons, R.D. and D.E. Swayne (1992). Nephrotropic
properties demonstrated by A/chicken/Alabama/75 (H4N8) following intravenous
challenge of chickens. Avian Diseases 36(4): 926-31. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Tissue tropism properties of
A/chicken/Alabama/75 (H4N8) were examined after intravenous inoculation of
5-week-old specific-pathogen-free chickens. From 14 clinically normal chickens
euthanatized on days 1-20 postinoculation, the frequencies of virus recovery
were highest for cloacal swabs (86%), bursal swabs (64%), and kidney tissues
(64%) and lowest for tracheal swabs (14%), thymus tissues (14%), bone-marrow
swabs (7%), and brain tissues (0%). Evidence that the high frequency of virus
recovery from kidney tissues was associated with virus replication in the
kidney tissues was provided by high virus titers, ranging up to 10(9.5) mean
embryo infectious dose per gram of kidney tissue, and by identification of
intranuclear and intracytoplasmic type A influenza nucleoprotein in kidney
cells using immunohistochemistry. Virus-recovery and virus titer results from
three chickens that died on days 4 and 5 postinoculation paralleled the results
from the clinically normal chickens. These findings indicate that
A/chicken/Alabama/75 has nephrotropic properties similar to nephrotropic
properties previously reported for waterfowl-origin type A influenza viruses and
provide evidence that kidney lesions could be manifestations of systemic
influenza infections in commercial laying chickens.
Descriptors: chickens microbiology, fowl plague pathology,
influenza A virus avian isolation and purification, kidney microbiology,
poultry diseases microbiology, fowl plague microbiology, injections,
intravenous veterinary, kidney pathology, nucleoproteins analysis, poultry
diseases pathology, viral core proteins analysis.
Slemons, R.D. and D.E. Swayne (1990). Replication
of a waterfowl-origin influenza virus in the kidney and intestine of chickens.
Avian Diseases 34(2): 277-84.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Intravenous inoculation of chickens with a waterfowl-origin
type A influenza virus resulted in high titers of virus in kidney tissues and
viral nucleoprotein in renal tubular epithelial cells and in intestinal mucosal
epithelial cells. Virus titers in kidneys of four of eight clinically normal
chickens sampled on days 3 and 5 postinoculation (PI), one dead chicken on day
3 PI, and one dead chicken on day 7 PI exceeded 10(6) mean embryo infectious
dose per gram of tissue. Using immunofluorescent and immunoperoxidase staining,
viral nucleoprotein was identified in the cytoplasm and nucleus of tubular
epithelial cells in kidneys and in nucleus of mucosal epithelial cells lining
villi in the lower small intestine. Based on the low intravenous pathogenicity
index for this virus (0.3) along with the high virus titers in kidney tissues
and localization of viral antigen in kidney important site for replication of
avian influenza (AI) virus of low pathogenicity. Recovery of type A influenza
viruses from cloacal swabs could result from viral replication in kidneys as
well as in the lower intestine and/or the bursa of Fabricius.
Descriptors: chickens microbiology, fowl plague
microbiology, influenza A virus avian physiology, intestine, small
microbiology, kidney microbiology, fluorescent antibody technique, immunoenzyme
techniques, immunohistochemistry, virus replication.
Slepushkin, V.A., V.B. Grigor'ev, A.I. Starov, S.M.
Klimenko, and G.V. Kornilaeva (1986). Vydelenie i kharakteristika endotsitarnykh
vakuolei, soderzhashchikh virus grippa. [Isolation and characteristics of
endocytic vacuoles containing the influenza virus]. Voprosy Virusologii
31(2): 167-72. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Endocytic vacuoles (receptosomes) containing
influenza virus were isolated from the cytoplasm of Ehrlich ascitic carcinoma
cells and characterized. In the sucrose density gradient, the virus-containing
material was detected in two peaks with a buoyant density of 1.175-1.16 and
1.155-1.135 g/cm3 with which the activity of marker enzymes of cell plasma
membranes was associated. The virus was present in receptosomes in
morphologically and electrophoretically intact condition. Examinations for the
lipid composition of endocytic vacuoles showed the presence in their membranes
of large amounts of cholesterol and glycolipids, particularly asialo-GM1 which,
according to some authors may enhance the fusion of viral and cell membranes.
Descriptors: endocytosis, influenza A virus avian
pathogenicity, organoids microbiology, vacuoles microbiology, carcinoma,
Ehrlich tumor enzymology, carcinoma, Ehrlich tumor microbiology, carcinoma,
Ehrlich tumor ultrastructure, cell fractionation, cell membrane analysis, cell
membrane enzymology, cell membrane microbiology, chick embryo, chromatography,
thin layer, electrophoresis, polyacrylamide gel, endosomes analysis, endosomes
enzymology, endosomes microbiology,
glycolipids analysis, lipids analysis, microscopy, electron, vacuoles
analysis, vacuoles enzymology, virus cultivation.
Smirnov, I.U.A., A.S. Lipatov, I. Okuno, and A.K.
Gitel'man (1999). Obshchii antigennyi epitop v gemaggliutinine virusov
grippa A (H1, H2, H5, H6). [A common antigenic epitope in influenza A virus
(H1, H2, H5, H6) hemagglutinin]. Voprosy Virusologii 44(3): 111-5. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Avian influenza A viruses belonging to
hemagglutinin (HA) subtypes H5 and H6 were studied in the infectivity
neutralization test and radioimmunoprecipitation assay (RIPA) with monoclonal
antibody MAb C179. This MAb recognizes a conformational antigenic epitope in
the stem region of HA formed by two regions (amino acid positions 318-322 in
HA1 subunit and 47-58 in HA2), conserved in all H1 and H2 influenza viruses.
MAb C179 reacts with HA of H5 viruses in RIPA and neutralizes these strains as
efficiently as H2 viruses. C179 precipitates H6 subtype HA but does not
neutralize the infectivity of these viruses. Comparison of amino acid sequences
of H2, H5, and H6 strains showed identical epitope recognized by MAb C179 in H5
and H6 HAs, which differs from epitopes of H1 and H2 by two amino acids in the
HA2 subunit. Causes of disagreement between immunoprecipitation of H6 HA by MAb
C179 and neutralization of this serosubtype by this MAb are discussed.
Descriptors: antigens, viral immunology, epitopes
immunology, hemagglutinins viral immunology, influenza A virus immunology,
antibodies, monoclonal immunology, birds, cell line, chick embryo, dogs,
influenza A virus pathogenicity, neutralization tests, radioimmunoprecipitation
assay.
Smirnov, Y.A., A.K. Gitelman, E.A. Govorkova, A.S.
Lipatov, and N.V. Kaverin (2004). Influenza H5 virus escape mutants: immune
protection and antibody production in mice. Virus Research 99(2):
205-8. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Avian H5N1 influenza A viruses are considered
to be of high pandemic potential as they are able to cross the avian-human
species barrier and cause disease in humans. In the present study we assessed
the impact of amino acid substitutions in the hemagglutinin (HA) of antigenic
escape mutants of influenza A/Mallard/Pennsylvania/10218/84 (H5N2)
(Mld/PA/84-MA) virus on the level of neutralizing antibodies and the ability to
protect mice against challenge with the wild type H5 influenza virus.
beta-Propiolactone-inactivated vaccines prepared from eight different H5 escape
mutants could be separated into two groups based on levels of protection. One
group of escape mutants [m46(7), m46(7)-24B9, m46(7)-55, and m46(7)-55-24B9]
was characterized by providing high levels of protection (90.0-95.4% survival)
to mice against subsequent challenge with 5 LD(50) of wild type Mld/PA/84-MA
virus. The other group of escape mutants [m176/26, m55(2), m55(2)-24B9, and
m24B9-176/26] provided moderate level of protection (57.1-66.6% survival) in
mice. Analysis of the amino acid substitutions in the HA revealed that two
amino acid changes in antigenic site B of the HA molecule (D(126)-->N and
K(152)-->N) were associated for decreases in the levels of antibody and the
immune protection afforded by vaccination with these H5 virus escape mutants.
The phenotypic effects of mutations in HA gene of H5 virus may be of importance
to appraise the extent and direction of H5 influenza viruses antigenic evolution.
Descriptors: antibodies, viral blood, hemagglutinin
glycoproteins, influenza virus genetics, hemagglutinin glycoproteins, influenza
virus immunology, influenza prevention and control, avian influenza A virus
genetics, avian influenza A virus immunology, influenza vaccines immunology,
amino acid substitution, antigens, viral genetics, antigens, viral immunology,
genes, viral, influenza virology, avian influenza A virus growth and
development, mice, mutation, missense, neutralization tests, vaccines, inactivated
immunology, virus inactivation.
Smirnov, Y.A., A.S. Lipatov, A.K. Gitelman, Y. Okuno,
R. Van Beek, A.D. Osterhaus, and E.C. Claas (1999). An epitope shared by the
hemagglutinins of H1, H2, H5, and H6 subtypes of influenza A virus. Acta
Virologica 43(4): 237-44. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The membrane-inserted hemagglutinin (HA) is
the most variable protein of influenza viruses. Here we describe the
characterization of a shared epitope in the HA of influenza A virus H1, H2, and
H5 subtypes which were completely neutralized by a monoclonal antibody (MAb),
directed against this epitope. This MAb (C179) also efficiently precipitated
the HAs of these viruses. In addition, MAb C179 did not neutralize H6 subtype
strains despite complete amino acid homology of the epitope regions.
Furthermore, only the non-glycosylated form of the HA of one of the H6 subtype
strains could be precipitated by the MAb. The conformational epitope may be
masked by glycosylation, although it could not be excluded that differences in
the primary amino acid sequence may cause the decreased accessibility of the
epitope in H6 subtype strains.
Descriptors: epitopes immunology, hemagglutinin
glycoproteins, influenza virus immunology, influenza A virus avian immunology,
human immunology, amino acid sequence, antibodies, monoclonal immunology,
antibodies, viral immunology, electrophoresis, polyacrylamide gel, avian classification, human classification,
molecular sequence data, neutralization tests, radioimmunoprecipitation assay,
sequence analysis, DNA.
Smirnov, Y.A., A.S. Lipatov, I. Okuno, and A.K.
Gitelman (1999). Common antigenic epitope in hemagglutinins of influenza A
viruses (H1, H2, H6, H6). Voprosy Virusologii 44(3): 111-115. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Avian influenza A viruses belonging to
hemagglutinin (HA) subtypes H5 and H6 were studied in the infectivity
neutralization test and radioimmunoprecipitation assay (RIPA) with monoclonal
antibody MAb C179. This MAb recognizes a conformational antigenic epitope in
the stem region of HA formed by two regions (amino acid positions 318-322 in
HA1 subunit and 47-58 in HA2), conserved in all H1 and H2 influenza viruses.
MAb C179 reacts with HA of H5 viruses in RIPA and neutralizes these strains as
efficiently as H2 viruses. C179 precipitates H6 subtype HA but does not
neutralize the infectivity of these viruses. Comparison of amino acid sequences
of H2, H5, and H6 strains showed identical epitope recognized by MAb C179 in H5
and H6 HAs, which differs from epitopes of H1 and H2 by two amino acids in the
HA2 subunit. Causes of disagreement between immunoprecipitation of H6 HA by MAb
C179 and neutralization of this serosubtype by this MAb are discussed.
Descriptors: immune system, infection, virology virus
neutralization.
Smith, D.B. and S.C. Inglis (1985). Regulated
production of an influenza virus spliced mRNA mediated by virus-specific
products. EMBO Journal 4(9): 2313-9.
ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: The influenza virus NS2 mRNA is generated
through processing by cellular enzymes of a transcript (the NS1 mRNA) of virion
RNA segment 8. Production of this mRNA is altered in cells infected with a
mutant of influenza A (fowl plague) virus. The proportion of segment 8
transcripts which accumulated in a spliced form was found to be considerably
lower in mutant virus-infected cells than in cells infected with wild-type
virus, and the amplification in production of NS2 mRNA relative to that of the
NS1 mRNA, which normally occurs during infection with wild-type virus, was not
observed with the mutant. The NS1 mRNA specified by the mutant virus has
unaltered splice recognition sites and was apparently processed normally during
a mixed infection with a strain of virus which is wild-type for production of
NS2 mRNA. These results suggest that the production of NS2 mRNA is regulated by
virus-specific products; these products may act by increasing the efficiency of
splicing of NS1 mRNA.
Descriptors: influenza A virus avian genetics, RNA,
messenger genetics, RNA viral genetics, base sequence, chick embryo, DNA
metabolism, fibroblasts, mutation, nucleic acid hybridization, species
specificity, transcription, genetic, virion genetics.
Smith, J.C., R.H. Raper, L.D. Bell, N. Stebbing, and
D. McGeoch (1980). Inhibition of influenza virion transcriptases by
polynucleotides. Virology 103(1): 245-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: DNA directed RNA polymerases antagonists and
inhibitors, influenza A virus human enzymology, polynucleotides pharmacology,
avian enzymology, orthomyxoviridae enzymology, poly A pharmacology, poly I
pharmacology, poly U pharmacology, structure activity relationship, virion
enzymology.
Smith, V.W., W. Coakley, D. Maker, J.S. Mackenzie,
and P.A. Lalor (1980). The serological response of chickens to an avian
influenza A virus administered by various routes. Research in Veterinary
Science 29(2): 248-50. ISSN:
0034-5288.
NAL
Call Number: 41.8 R312
Abstract: An avian influenza A virus (Hav7 Neq2)
isolated from a feral duck in Western Australia was transmitted to groups of
broiler chickens by cloaca, mouth, eye drop or spray. No disease or deaths
occurred. Serum samples were examined by haemagglutination inhibition test and
enzyme linked immunosorbent assays and the results gave reasonable correlation.
Chickens infected by cloaca or spray gave the best overall seroconversions.
Descriptors: chickens immunology, influenza A virus avian
immunology, antibodies, viral analysis, beak, cloaca, enzyme linked
immunosorbent assay, eye, hemagglutination inhibition tests, injections, viral
vaccines administration and dosage.
Smolenskii, V.I., S.G. Afrikantov, and I.V. Zhukov
(1980). Gripp kur, vyzvannyi variantom virusa GP-4. [Influenza in hens
caused by a variant of the GP-4 virus]. Veterinariia (4): 64-6. ISSN: 0042-4846.
NAL
Call Number: 41.8 V6426
Descriptors: chickens, fowl plague microbiology, influenza
A virus avian isolation and purification, variation genetics, antigens, viral
analysis, avian immunology, serotyping.
Snyder, M.H., M.L. Clements, D. Herrington, W.T.
London, E.L. Tierney, and B.R. Murphy (1986). Comparison by studies in
squirrel monkeys, chimpanzees, and adult humans of avian-human influenza A
virus reassortants derived from different avian influenza virus donors. Journal
of Clinical Microbiology 24(3): 467-9.
ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: We evaluated the abilities of three different
avian influenza A viruses to attenuate the wild-type human influenza
A/Korea/1/82 (H3N2) virus in squirrel monkeys, chimpanzees, and adult
seronegative human volunteers. Two of these, avian influenza A/Mallard/NY/78
and A/Mallard/Alberta/76 viruses, appeared to be satisfactory donors of
attenuating genes for the production of live influenza A reassortant virus
vaccines for human use because the reassortants exhibited an acceptable balance
between attenuation and immunogenicity.
Descriptors: influenza A virus avian immunology, human
immunology, influenza vaccine immunology, antibodies, viral biosynthesis, avian
genetics, avian physiology, human genetics, human physiology, Pan
troglodytes, recombination, genetic, saimiri, vaccines, attenuated, virus
replication.
Snyder, M.H., E.H. Stephenson, H. Young, C.G. York,
E.L. Tierney, W.T. London, R.M. Chanock, and B.R. Murphy (1986). Infectivity
and antigenicity of live avian-human influenza A reassortant virus: comparison
of intranasal and aerosol routes in squirrel monkeys. Journal of
Infectious Diseases 154(4): 709-11.
ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Descriptors: antibodies, viral biosynthesis, influenza A
virus avian immunology, human immunology, influenza vaccine immunology,
administration, intranasal, aerosols, immunization, avian pathogenicity, human
pathogenicity, saimiri, vaccines, attenuated, virulence.
Sokolov, B.P. and S.G. Markushin (1984). Oligopeptidnye
karty matriksnogo belka temperaturochuvstvitel'nogo mutanta (TS 303) virusa
chumy ptits. [Oligopeptide maps of the matrix protein of a
temperature-sensitive mutant (TS 303) of the fowl plague virus]. Voprosy
Virusologii 29(1): 66-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Oligopeptide maps of M proteins of
"wild" fowl plague virus (FPV) and a temperature-sensitive mutant of
FPV were compared with respect of gene. In maps of M proteins labeled with
14C-chlorella hydrolysate and 35S-methionine the mutant virus was found to lack
one of oligopeptides present in maps of M proteins of the "wild"
virus. The electrophoretic mobility of M proteins of ts 303 and FPV in 25%
polyacrylamide gel was similar.
Descriptors: influenza A virus avian analysis, mutation,
oligopeptides analysis, temperature, viral proteins analysis, electrophoresis,
polyacrylamide gel, viral matrix proteins.
Sokolov, B.P., I.A. Rudneva, and V.M. Zhdanov (1983).
Comparative study and grouping of nonstructural (NS1) proteins of influenza
A viruses by the method of oligopeptide mapping. Archives of Virology
78(3-4): 221-31. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Oligopeptide mapping of 35S-methionine
labeled non-structural (NS1) proteins of 23 influenza. A virus strains showed
the presence of both common and variable oligopeptides. Analysis of the
oligopeptide maps revealed at least four groups of NS1 proteins. The first
group includes NS1 proteins of several human H1N1 influenza viruses (that were
designated as H0N1 according to the old classification). The second group is
composed of NS1 proteins of H1N1 and H2N2 viruses. The third group includes NS1
proteins of H3N2 human influenza viruses. The fourth group is composed of NS1
proteins of five avian influenza viruses and an equine (H3N8) influenza virus.
Two animal influenza viruses A/equi/Prague/56 (H7N7) and A/duck/England/56
(H11N6) contain NS1 proteins that belong to the second group.
Descriptors: influenza A virus human classification,
influenza A virus classification, oligopeptides analysis, viral proteins
classification, avian analysis, avian classification, human analysis, influenza
A virus analysis, trypsin, viral nonstructural proteins, viral proteins
analysis.
Sokolov, B.P., I.A. Rudneva, and V.M. Zhdanov (1981).
Gruppirovanie nestrukturnykh belkov NS1 virusov grippa A. [Grouping of the
NS1 nonstructural proteins of influenza A viruses]. Voprosy Virusologii
(6): 650-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Peptide mapping was used for comparative
analysis of nonstructural proteins (NS1) of 21 strains of human and animal
influenza A viruses. At least 4 groups of NS1 proteins could be distinguished
by the analysis of the peptide maps; we designated these groups as 0, 1, 2, and
3. Group O includes NS1 proteins of human influenza virus serotype HON1, group
1 - NS1 proteins of viruses of serotypes H1N1 and H2N2, group 2 - NS1 proteins
of viruses of serotype H3N2. NS1 proteins of avian influenza viruses A/duck
Czechoslovakia/63, A/turkey Massachusetts/65, A/petrel Australia/1/71, A/duck
Ukraine/63, and A/turkey Ontario/68 have been included into group 3.
Descriptors: influenza A virus classification, viral
proteins classification, electrophoresis methods, electrophoresis,
polyacrylamide gel, influenza A virus analysis, peptides analysis, peptides classification,
viral proteins analysis.
Sokolov, M.I. (1972). Nekotorye aktual'nye voprosy
genetiki virusov pozvonochnykh. [Genetics of vertebrate viruses]. Vestnik
Akademii Meditsinskikh Nauk SSSR 27(6): 84-7. ISSN: 0002-3027.
Descriptors: orthomyxoviridae radiation effects, genetics,
microbial, influenza A virus avian radiation effects, mutation, nucleic acid
hybridization, RNA, viral, radiation genetics, recombination, genetic,
ultraviolet rays, virulence, virus replication.
Sokolov, M.I. and I.A. Miasnikova (1972). Mutagennoe
deistvie UF-luchei na virus istinnoi chumy ptits. Selektsiia i kharakteristika
nekotorykh svoistv plius- i minus UF-mutantov. [The mutagenic effect of
ultraviolet rays on the virus of true fowl plague. Selection and characteristics
of several properties of plus and minus ultraviolet mutants]. Voprosy
Virusologii 17(4): 453-8. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian radiation
effects, mutation radiation effects,
ultraviolet rays, chick embryo, fibroblasts, genetics, microbial, avian
isolation and purification, plaque assay, radiation effects, tissue culture,
virus cultivation.
Sokolova, N.L. (1976). Dinamika nakopleniya
gemagglyutininov v ekstraembrional'noi zhidkosti kurinykh embrionov,
zarazhennykh virusom grippa ptits GP1-GP2. [Dynamics of the development of
haemagglutinins in extraembryonic fluids of chick embryos infected with avian
influenzavirus GP1-GP8]. Sbornik Nauchnykh Trudov, Moskovskaya
Veterinarnaya Akademiya 87: 82-86.
Descriptors: avian influenza virus, hemagglutination,
chick embryos, strains, pathogenicity.
Spooner, L.L. and R.D. Barry (1977). Participation
of DNA-dependent RNA polymerase II in replication of influenza viruses. Nature
268(5621): 650-2. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: amanitins pharmacology, DNA directed RNA
polymerases metabolism, influenza A virus avian growth and development, RNA
polymerase ii metabolism, virus replication drug effects, cell line, drug
resistance, avian metabolism, RNA polymerase ii antagonists and inhibitors, RNA
viral biosynthesis, time factors, viral proteins biosynthesis.
Sprecher Goldberger, S. (1966). The existence of
two different metabolic patterns for the synthesis of RNA viruses. Archiv
Fur Die Gesamte Virusforschung 18(2): 198-209. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: enterovirus growth and development, RNA
viruses growth and development, RNA viral biosynthesis, adenine metabolism,
antimetabolites pharmacology, chick embryo, culture media, dactinomycin
pharmacology, fibroblasts, formates metabolism, histones pharmacology,
influenza A virus avian growth and development, methotrexate pharmacology,
nucleosides metabolism, orotic acid metabolism, phenylalanine pharmacology,
puromycin pharmacology, radiation effects, thymidine metabolism, ultraviolet
rays, uridine metabolism.
Sriram, G., W.J. Bean Jr, V.S. Hinshaw, and R.G.
Webster (1978). Heterogeneity in the RNAs of Hav7Neq2 avian influenza
viruses. Abstracts of the Annual Meeting of the American Society for
Microbiology 78: 242.
NAL
Call Number: 448.39 SO12A
Descriptors: avian influenza virus, heterogeneity, RNA.
Stallknecht, D.E., M.T. Kearney, S.M. Shane, and P.J.
Zwank (1990). Effects of pH, temperature, and salinity on persistence of
avian influenza viruses in water. Avian Diseases 34(2): 412-8. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The combined effects of water temperature,
salinity, and pH on persistence of avian influenza virus (AIV) were evaluated
in a model distilled-water system using three isolates from ducks sampled in
Cameron Parish, Louisiana. Variables were tested within the ranges normally
associated with surface water. Differences were detected between temperature
(17 C and 28 C), pH (6.2, 7.2, 8.2), and salinity (0 ppt and 20 ppt), with a
strong interactive effect observed between pH and salinity. Estimated
persistence of infectivity for 1 x 10(6) mean tissue-culture infective dose of
A/mottled duck/LA/38M/87 (H6N2) was longest at 17 C/0 ppt/pH 8.2 (100 days) and
shortest at 28 C/20 ppt/pH 8.2 (9 days). Differences in the response to these
variables were apparent between viruses. The ability of AIV to persist in
surface water was also evaluated using samples collected from varied waterfowl
habitats in coastal Louisiana. Observations were consistent with the model
system, with duration of infectivity decreasing with increased salinity and pH.
This suggests that experimental results may have application to field
conditions.
Descriptors: influenza A virus avian growth and
development, water microbiology, chick embryo, ducks, fresh water, hydrogen-ion
concentration, linear models, Louisiana, regression analysis, sodium chloride,
specific pathogen free organisms, temperature.
Stankova, I.G., M.F. Simeonov, V. Maximova, A.S.
Galabov, and E.V. Golovinsky (1999). Synthesis and anti-virus activity of
some nucleosides analogues. Zeitschrift Fur Naturforschung. C, Journal
of Biosciences 54(1-2): 75-83. ISSN:
0341-0382.
NAL
Call Number: QH301.Z4
Abstract: New 3'-, 5'-, 5-bromo-2'-deoxyuridine (3a-g)
and 3'-, 5'-thymidine (4a-i) analogues with amino acid and peptide residues
were synthesized and evaluated for antiviral activity. The influence of long
peptide chains, essential amino acids and the effect of this structural
modification on the antiviral activity has been also reported. Three
5-bromo-2'-deoxyuridine derivatives containing glycyl-, glycyl-glycyl- and
glycyl-glycyl-glycyl- residues (3a, 3b, 3c) showed a strong activity against
the herpes virus PsRV and a moderate one vs. HSV-1. The corresponding thymidine
analogues were considerably less effective, and only compounds 4d and 4h showed
a borderline effect against PsRV.
Descriptors: anti-HIV agents chemical synthesis, antiviral
agents chemical synthesis, bromodeoxyuridine analogs and derivatives,
bromodeoxyuridine chemical synthesis, thymidine analogs and derivatives,
thymidine chemical synthesis, amino acids, anti-HIV agents chemistry, anti-HIV
agents pharmacology, antiviral agents chemistry, antiviral agents pharmacology,
bromodeoxyuridine chemistry, bromodeoxyuridine pharmacology, cultured cells,
chick embryo, chickens, drug design, fibroblasts cytology, fibroblasts
virology, HIV drug effects, herpesvirus 1, human drug effects, herpesvirus 1,
suid drug effects, influenza A virus avian drug effects, microbial sensitivity
tests, peptides, structure activity relationship, thymidine chemistry,
thymidine pharmacology.
Starov, A.I. and A.G. Bukrinskaia (1981). Transkriptsiia
genoma virusa grippa. Lokalizatsiia i zavisimost' ot praimernoi funktsii iadra.
[Transcription of influenza virus genome. Location and dependence on the
nuclear primer function]. Molekuliarnaia Biologiia 15(6):
1415-22. ISSN: 0026-8984.
NAL
Call Number: QH506.A1M62
Abstract: The synthesis of the complete and incomplete
transcripts (the templates in genome replication and mRNA, respectively) of
influenza A WSN virus in chicken fibroblasts was analyzed by gel
electrophoresis analysis of the duplexes formed between virion RNA and
complementary RNA. Three steps in the transcription could be defined: 1)
primary transcription when similar amounts of mRNA of all the genes are
accumulated; 2) early secondary transcription when mRNA of NS gene is
synthesized in larger amounts than that of other genes and 3) late secondary
transcription when the amplification of transcription from all the genes is
performed. The synthesis of complete transcripts starts during or after primary
transcription. When actinomycin D was added to infected cells, the synthesis of
incomplete transcripts was inhibited to a larger degree then that of complete
transcripts. Most of incomplete transcripts was observed within the cell
nucleic while the complete transcripts were found in the nuclei and cytoplasm,
suggesting that the synthesis of incomplete transcripts is located in the
nuclei. alpha-Amanitin blocked the synthesis of incomplete transcripts without
interfering with that of complete transcripts. These data suggest that the
synthesis of complete transcripts does not require the synthesis of cell mRNA
as primers in transcription.
Descriptors: cell nucleus metabolism, genes, structural
drug effects, genes viral drug effects, influenza A virus avian genetics,
transcription, genetic drug effects, amanitins pharmacology, chickens,
dactinomycin pharmacology, fibroblasts, RNA, messenger genetics.
Steinhoff, M.C., N.A. Halsey, M.H. Wilson, B.A.
Burns, R.K. Samorodin, L.F. Fries, B.R. Murphy, and M.L. Clements (1990). Comparison
of live attenuated cold-adapted and avian-human influenza A/Bethesda/85 (H3N2)
reassortant virus vaccines in infants and children. Journal of
Infectious Diseases 162(2): 394-401.
ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: Randomized, placebo-controlled studies with
10(3)-10(7) 50% tissue-culture infectious dose (TCID50) of avian-human (ah) and
cold-adapted (ca) influenza A/Bethesda/85 (H3N2) reassortant viruses were
completed in 106 seronegative young children 6-48 months of age. Although the
reassortants differed in six of eight RNA segments, they exhibited similar
properties in level of attenuation, infectivity, immunogenicity, and efficacy.
The 50% human infectious dose was 10(4.6) TCID50 for ah and 10(4.4) for ca
vaccines. Both reassortants were satisfactorily attenuated with restricted
replication and were no more reactogenic than placebo. The mean peak titer of
virus shed was 10(1.5) (ah) to 10(2.0) (ca) TCID50/ml, and each of 37 isolates
tested retained their characteristic vaccine phenotypes. Infection with ah or
ca virus conferred immunity to experimental challenge with homologous virus.
These findings indicate that both ah and ca influenza A/Bethesda/85 (H3N2)
reassortants should be suitable vaccine candidates for use in healthy infants
and young children.
Descriptors: influenza prevention and control, influenza A
virus avian immunology, human immunology, influenza vaccine immunology,
antibodies, viral biosynthesis, child, preschool, cold, dose response
relationship, immunologic, double blind method, enzyme linked immunosorbent
assay, immunoglobulin G biosynthesis, infant, avian isolation and purification,
human isolation and purification, randomized controlled trials, vaccines,
attenuated immunology, vaccines, synthetic immunology.
Stephenson, J.R. and N.J. Dimmock (1974). Inhibition
of the processing of ribosomal RNA in avian cells infected with an influenza
virus. Biochimica Et Biophysica Acta 361(2): 198-208. ISSN: 0006-3002.
NAL
Call Number: 381 B522
Descriptors: cell nucleus metabolism, cytoplasm
metabolism, fibroblasts metabolism, influenza A virus avian, RNA, ribosomal
biosynthesis, carbon radioisotopes,
chick embryo, electrophoresis, polyacrylamide gel, fibroblasts cytology,
hemagglutinins viral, methylation, molecular weight, RNA, ribosomal isolation
and purification, RNA, ribosomal metabolism, RNA viral biosynthesis, tritium,
uridine metabolism, virus replication.
Stephenson, J.R., A.J. Hay, and J.J. Skehel (1977). Characterization
of virus-specific messenger RNAs from avian fibroblasts infected with fowl
plague virus. Journal of General Virology 36(2): 237-48. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: In cell-free protein synthesizing systems
from wheat embryos, messenger RNAs extracted from chick embryo fibroblasts
infected with fowl plague virus direct the synthesis of nine virus-specific
polypeptides, two of which may be related to the virus-specific
glycopolypeptides. All of the mRNAs are complementary in sequence to virion
RNA, and RNAs which do not contain poly A appear to be translated as
efficiently as their polyadenylated counterparts. Under certain conditions of
incubation, virion RNA also directs the synthesis of discrete polypeptides but
these products are not detected in infected cells.
Descriptors: influenza A virus avian analysis, RNA,
messenger analysis, RNA viral analysis, cell free system, chick embryo,
fibroblasts, avian metabolism, peptide synthesis, RNA, messenger metabolism,
RNA viral metabolism, tissue culture, translation, genetic, viral proteins
biosynthesis.
Sterkers, G., J. Michon, Y. Henin, E. Gomard, C.
Hannoun, and J.P. Levy (1985). Fine specificity analysis of human
influenza-specific cloned cell lines. Cellular Immunology 94(2):
394-405. ISSN: 0008-8749.
NAL
Call Number: QR180.C4
Abstract: Influenza-specific human-T-cell clones,
proliferating in the presence of virus-infected cells with restriction by class
II molecules and displaying class II-restricted CTL activity or specific helper
activity in antibody synthesis, have been analyzed for antigenic specificities.
All of them were obtained by in vitro stimulation against influenza A/Texas
virus. In all cases the virus specificity appeared identical in cytolytic and
proliferative responses. Three of the clones were broadly cross-reactive,
recognizing all or almost all type A influenza strains. The three remaining
clones were subtype specific when tested with human strains and recognized the
surface glycoproteins of influenza virus. One of these lines reacted with an
epitope of the neuraminidase N2 while the other two recognized the
hemagglutinin H3. By using a large panel of mammalian and avian influenza
strains, it can be demonstrated that hemagglutinin-specific human T cells can
recognize a cross-reacting determinant shared by H3 and H4 subtypes of
hemagglutinin which has never been detected with antibodies.
Descriptors: influenza A virus immunology, T lymphocytes
immunology, antigens, viral immunology, cell line, clone cells, cytotoxicity,
immunologic, ducks immunology, epitopes immunology, horses immunology.
Sterz, I. and E. Weiss (1974). Electron
microscopical and virological studies of chicken thrombocytes in vitro infected
with fowl plague virus (FPV). Medical Microbiology and Immunology
159(2): 151-60. ISSN: 0300-8584.
Descriptors: blood platelets microbiology, influenza A
virus avian immunology, adsorption, chickens, microscopy, electron,
phagocytosis, time factors.
Sterz, I. and E. Weiss (1973). Elektronenmikroskopische
Untersuchungen zur Phagozytose und Vermehrung des Virus der Klassischen
Geflugelpest (KP) in Thrombozyten infizierter Huhner. [Electron microscopy
studies on phagocytosis and replication of fowl plague virus in thrombocytes of
infected chickens]. Zentralblatt Fur Veterinarmedizin. Reihe B Journal
of Veterinary Medicine. Series B 20(8): 613-21. ISSN: 0514-7166.
NAL
Call Number: 41.8 Z52
Descriptors: fowl plague microbiology, influenza A virus
avian growth and development, phagocytosis, virus replication, blood platelets
microbiology, chickens, fowl plague blood, microscopy, electron.
Steuler, H., W. Rohde, and C. Scholtissek (1984). Sequence
of the neuraminidase gene of an avian influenza A virus (A/parrot/Ulster/73,
H7N1). [Abstract]. Zentralblatt Fur Bakteriologie Mikrobiologie Und
Hygiene, A 258(4): 534.
NAL
Call Number: 448.3 C33 (1)
Descriptors: avian influenza virus, DNA, molecular
conformation, neuraminidase sequence.
Steuler, H., W. Rohde, and C. Scholtissek (1984). Sequence
of the neuraminidase gene of an avian influenza A virus (A/parrot/ulster/73,
H7N1). Virology 135(1): 118-24.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The complete sequence of the neuraminidase
(NA) gene of the influenza A strain A/parrot/ Ulster /73 ( H7N1 ) has been
determined after reverse transcribing and cloning it into the pBR322 plasmid,
followed by subcloning into M13 vectors and sequencing with dideoxynucleotide
chain terminators. The gene consists of 1458 nucleotides and codes for a
protein of 469 amino acids. The neuraminidase has seven potential glycosylation
sites. According to the molecular weight as determined by electrophoretic
migration in polyacrylamide gel all of these sites might carry a carbohydrate
side chain. When the parrot Ulster NA was compared with two other N1
neuraminidases, those of the human PR8 and WSN strains, deletions in the stalk
region of 15 amino acids for PR8 NA and of 16 amino acids for WSN NA were
apparent. No further rearrangements were found within N1 neuraminidases.
Although the parrot Ulster strain was isolated 40 years after the two human
strains, the base sequence homology of their NA genes is still 83 or 82%,
respectively.
Descriptors: genes, structural, genes viral, influenza A
virus avian enzymology, neuraminidase genetics, allantoin, amino acid sequence,
base sequence, chick embryo, DNA restriction enzymes, avian genetics.
Steuler, H., B. Schroder, H. Burger, and C.
Scholtissek (1985). Sequence of the nucleoprotein gene of influenza
A/parrot/Ulster/73. Virus Research 3(1): 35-40. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The nucleotide sequence of the nucleoprotein
(NP) gene of the avian influenza A virus strain A/parrot/Ulster/73 (H7N1) has
been determined. The gene (RNA segment 5) consists of 1565 bases. The only
large open reading frame of the complementary RNA codes for a protein of 498
amino acids. A comparison of its sequence with that of three other influenza
virus NPs shows that the NP of the parrot Ulster strain, although closely
related to the NP of the other avian strain (A/FPV/Rostock/34), is definitely
more closely related genetically to the NPs of the two human influenza strains,
A/PR/8/34 and A/NT/60/68 than that of FPV. This raises the question how far the
NP gene can cross the species barrier by reassortment and become adapted by mutation
to the new host.
Descriptors: influenza A virus avian genetics,
nucleoproteins genetics, RNA viral genetics, viral proteins genetics, amino
acid sequence, base sequence, cloning, molecular, genes, structural, genes
viral, human genetics.
Stevens, J., A.L. Corper, C.F. Basler, J.K.
Taubenberger, P. Palese, and I.A. Wilson (2004). Structure of the uncleaved
human H1 hemagglutinin from the extinct 1918 influenza virus. Science
303(5665): 1866-70. ISSN: 1095-9203.
NAL
Call Number: 470 Sci2
Abstract: The 1918 "Spanish" influenza
pandemic represents the largest recorded outbreak of any infectious disease.
The crystal structure of the uncleaved precursor of the major surface antigen
of the extinct 1918 virus was determined at 3.0 angstrom resolution after
reassembly of the hemagglutinin gene from viral RNA fragments preserved in 1918
formalin-fixed lung tissues. A narrow avian-like receptor-binding site, two
previously unobserved histidine patches, and a less exposed surface loop at the
cleavage site that activates viral membrane fusion reveal structural features
primarily found in avian viruses, which may have contributed to the
extraordinarily high infectivity and mortality rates observed during 1918.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, influenza A virus, human immunology, amino acid sequence, binding
sites, carbohydrate conformation, cloning, molecular, crystallography, x-ray,
glycosylation, hemagglutinin glycoproteins, influenza virus metabolism,
histidine chemistry, histidine metabolism, history, 20th century, hydrogen
bonding, influenza epidemiology, influenza history, influenza virology, avian
immunology, human classification, human pathogenicity, porcine immunology,
molecular sequence data, protein conformation, protein structure, quaternary,
protein structure, secondary, tertiary, receptors, virus metabolism, sialic
acids metabolism.
Stieneke Grober, A., M. Vey, H. Angliker, E. Shaw, G.
Thomas, C. Roberts, H.D. Klenk, and W. Garten (1992). Influenza virus
hemagglutinin with multibasic cleavage site is activated by furin, a
subtilisin-like endoprotease. EMBO Journal 11(7): 2407-14. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: Many viruses have membrane glycoproteins that
are activated at cleavage sites containing multiple arginine and lysine
residues by cellular proteases so far not identified. The proteases responsible
for cleavage of the hemagglutinin of fowl plague virus, a prototype of these
glycoproteins, has now been isolated from Madin-Darby bovine kidney cells. The
enzyme has a mol. wt of 85,000, a pH optimum ranging from 6.5 to 7.5, is
calcium dependent and recognizes the consensus sequence R-X-K/R-R at the
cleavage site of the hemagglutinin. Using a specific antiserum it has been
identified as furin, a subtilisin-like eukaryotic protease. The fowl plague
virus hemagglutinin was also cleaved after coexpression with human furin from
cDNA by vaccinia virus vectors. Peptidyl chloroalkylketones containing the
R-X-K/R-R motif specifically bind to the catalytic site of furin and are
therefore potent inhibitors of hemagglutinin cleavage and fusion activity.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian enzymology, membrane proteins metabolism, subtilisins metabolism,
viral envelope proteins metabolism, affinity labels, amino acid chloromethyl
ketones pharmacology, amino acid sequence, blotting, western, cattle, cultured
cells, chick embryo, chromatography, liquid, DNA, dogs, furin, hemagglutinin
glycoproteins, influenza virus, hydrogen-ion concentration, avian metabolism,
molecular sequence data, vaccinia virus genetics.
Stitz, L., R.T. Huang, H. Hengartner, R. Rott, and
R.M. Zinkernagel (1985). Cytotoxic T cell lysis of target cells fused with
liposomes containing influenza virus haemagglutinin and neuraminidase. Journal
of General Virology 66(Pt. 6): 1333-9.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The lytic activity of secondary cytotoxic
lymphocytes against influenza A virus was tested on cells which had been fused
with liposomes containing the haemagglutinin and the neuraminidase of an avian
influenza A virus (fowl plague virus, FPV). Fusion was obtained solely by the
activity of the haemagglutinin and neuraminidase incorporated into the
liposomes, without the need for any additional fusion factor. Highly
reproducible lysis of these FPV-liposome target cells by influenza A-specific
cytotoxic cells was found. In contrast, target cells containing the
glycoproteins HN and F of Newcastle disease virus (NDV) were not lysed. In
almost all experiments effector cell populations capable of lysing target cells
also lysed the natural killer cell (NK)-sensitive cell line YAC-1. However,
high NK activity alone was not sufficient to lyse target cells fused with
liposomes containing the viral surface glycoproteins. To our knowledge this is
the first report where after artificial introduction of viral surface
components into cell membranes (either by fusion or by transfection) lysis of
target cells was monitored also for non-specific lysis mediated by NK-like
cells. Both the H-2 restriction and the virus specificity of lysis of
FPV-liposome target cells indicate that influenza virus haemagglutinin and
possibly neuraminidase do function as target antigens for influenza-specific T
cells.
Descriptors: antigens, viral immunology, hemagglutinins
viral immunology, neuraminidase immunology, orthomyxoviridae immunology, T
lymphocytes, cytotoxic immunology, glycoproteins immunology, influenza A virus
avian immunology, killer cells, natural immunology, liposomes, mice inbred BALB
c, mice, inbred c3h, mice, inbred c57bl, Newcastle disease virus immunology,
viral envelope proteins immunology.
Stitz, L., M. Reinacher, and H. Becht (1977). Studies
on the inhibitory effect of lectins on myxo-virus release. Journal of
General Virology 34(3): 523-30.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Lectins of different specificities do not
interfere with the maturation of myxo-viruses; their inhibitory effect on virus
replication is mainly due to prevention of the detachment of infectious virus
particles from the host cell. In chick embryo fibroblasts infected with an
influenza virus and treated with concanavalin A, budding occurs into
intracytoplasmic vacuoles, but this phenomenon is not observed with a
parainfluenza virus and with different cells.
Descriptors: influenza A virus avian growth and
development, lectins pharmacology, Newcastle disease virus growth and
development, virus replication drug effects, chick embryo, concanavalin A
pharmacology, avian isolation and purification, methylmannosides pharmacology,
Newcastle disease virus isolation and purification, sonication, tissue culture,
vacuoles microbiology.
Strobel, I., R. Grassmann, E. Hofmann, G. Hobom, U. Schulze,
E. Niedobitek, E. Wagner, B. Fleckenstein, and G. Schuler (1998). Efficient
transduction of mature human dendritic cells by using an avian influenza virus
as a vector. Journal of Investigative Dermatology 110(4): 605. ISSN: 0022-202X.
NAL
Call Number: 448.8 J8292
Descriptors: cell biology, immune system, molecular
genetics, gene transfer, gene transfer method, meeting abstract, meeting
poster.
Strobel, I., M. Krumbholz, A. Menke, E. Hoffmann,
P.R. Dunbar, A. Bender, G. Hobom, A. Steinkasserer, G. Schuler, and R.
Grassmann (2000). Efficient expression of the tumor-associated antigen
MAGE-3 in human dendritic cells, using an avian influenza virus vector. Human
Gene Therapy 11(16): 2207-18. ISSN:
1043-0342.
Abstract: Dendritic cells (DCs) are the most potent
inducers of immune reactions. Genetically modified DCs, which express
tumor-associated antigens (TAA), can efficiently induce antitumor immunity and
thus have a high potential as tools in cancer therapy. The gene delivery is
most efficiently achieved by viral vectors. Here, we explored the capacity of
influenza virus vectors to transduce TAA genes. These viruses abortively infect
DCs without interfering with their antigen-presenting capacity. In contrast to
other viruses used for DC transduction, influenza viruses can be efficiently
controlled by antiviral pharmaceuticals, lack the ability to integrate into
host chromosomes, and fail to establish persistent infections. Genes encoding a
melanoma-derived TAA (MAGE-3), or the green fluorescence protein (GFP), were
introduced into a high-expression avian influenza virus vector.
Monocyte-derived mature DCs infected by these recombinants efficiently produced
GFP or MAGE-3. More than 90% of the infected DCs can express a transduced gene.
Importantly, these transduced DCs retained their characteristic phenotype and
their potent allogeneic T cell stimulatory capacity, and were able to stimulate
MAGE-3-specific CD8(+) cytotoxic T cells. Thus influenza virus vectors provide
a highly efficient gene delivery system in order to transduce human DCs with
TAA, which consequently stimulate TAA-specific T cells.
Descriptors: antigens, neoplasm genetics, dendritic cells
metabolism, gene transfer techniques, influenza A virus avian genetics,
neoplasm proteins genetics, neoplasm proteins metabolism, antigens, neoplasm
metabolism, CD8 positive T lymphocytes metabolism, cell line, cell separation,
dogs, flow cytometry, genetic vectors, immunoblotting, immunophenotyping,
luminescent proteins genetics, luminescent proteins metabolism, microscopy,
phase contrast, phenotype, plasmids metabolism, reverse transcriptase
polymerase chain reaction, T lymphocytes, cytotoxic metabolism, transduction,
genetic, tumor cultured cells.
Strube, M., G. Bodo, and C. Jungwirth (1985). Sensitivity
of ortho- and paramyxovirus replication to human interferon alpha. Molecular
Biology Reports 10(4): 237-43. ISSN:
0301-4851.
NAL
Call Number: QH506.M684
Abstract: Replication of the influenza virus strains
Influenza Ao/WSN (H0N1), fowl plague (Hav1N1) and B-Lee/40 (ATCC) and the
paramyxovirus, New Castle disease virus (Victoria) are highly sensitive to
human interferon type alpha in Madin Darby bovine kidney cells. Pretreatment of
cells with human interferon type alpha resulted in protection of the cells
against viral cytopathic effect. The inhibition of the orthomyxovirus strains
used in this study and New Castle disease virus replication is mediated by an
inhibition of viral protein synthesis. Residual WSN virus particles released
from interferon treated cells showed the same structural protein pattern as
virus particles isolated from control cells. Glycosylation of the viral
structural components appeared to be unaffected by interferon.
Descriptors: DNA replication drug effects, interferon type
I pharmacology, Newcastle disease virus drug effects, orthomyxoviridae drug
effects, virus replication drug effects, cattle, dogs, influenza A virus avian
drug effects, human drug effects, influenza B virus drug effects, kinetics,
mice, Newcastle disease virus genetics, orthomyxoviridae genetics, species
specificity, structure activity relationship.
Subbarao, E.K., Y. Kawaoka, and B.R. Murphy (1993). Rescue
of an influenza A virus wild-type PB2 gene and a mutant derivative bearing a
site-specific temperature-sensitive and attenuating mutation. Journal of
Virology 67(12): 7223-7228. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Live attenuated influenza A virus vaccines
are currently produced by the transfer of attenuating genes from a donor virus
to new epidemic variants of influenza A virus, with the selection of
reassortant viruses that possess the protective antigens (i.e., the two surface
glycoproteins) of the epidemic virus and the attenuating genes from the donor
virus. The previously studied attenuated donor viruses were produced by
conventional methods such as passage of virus at low temperature or chemical
mutagenesis. The present paper describes a new strategy for the generation of a
donor virus bearing an attenuating, non-surface-glycoprotein gene. This
strategy involves the introduction of attenuating mutations into the cDNA copy
of the PB2 polymerase gene by site-directed mutagenesis, transfection of in
vitro RNA transcripts of PB2 cDNA, and recovery of the transfected PB2 gene into
an infectious virus. An avian-human influenza A virus PB2 single-gene
reassortant virus (with an avian influenza A virus PB2 gene) that replicates
efficiently in avian tissue but poorly in mammalian cells was used as a helper
virus to rescue a transfected synthetic RNA derived from a human influenza A
virus PB2 gene. The desired human influenza A virus mutant PB2 transfectant was
favored in this situation because the avian influenza A virus PB2 gene
restricts viral replication in mammalian cells in culture, the system used for
rescue, thereby providing strong selection for the virus bearing the human
influenza A virus PB2 gene. We validated the feasibility of this approach by
rescuing the PB2 gene of the wild-type influenza A/Ann Arbor/6/60 virus and a
mutant derivative that had a single amino acid substitution introduced at
position 265 by site-directed mutagenesis. Previously, this amino acid
substitution had been shown to specify both a temperature-sensitive (ts) and an
attenuation (aft) phenotype. The rescued mutant 265 PB2 transfectant virus
exhibited the ts and att phenotypes, which confirms that these phenotypes were
specified by this single amino acid substitution. The transfectant virus was
immunogenic and protected hamsters from subsequent challenge with wild-type
virus. The cDNA copy of this influenza A/Ann Arbor/6/60 virus mutant 265 PB2
gene will be used as a substrate for the introduction of additional attenuating
mutations by site-directed mutagenesis.
Descriptors: genetics, immune system, microbiology,
pharmacology, avian influenza A virus, challenge protection, hamster
immunogenicity, host range, restriction, exploitation, human influenza A virus,
vaccine donor, virus generation method.
Sudnik, I.U.M., V.I. Votiakov, A.S. Ba, A.S.I.
Khmel'nitskii, and V.A. Tsvirko (1986). Izuchenie gemoliza, indutsirovannogo
virusom grippa. [Hemolysis induced by the influenza virus]. Voprosy
Virusologii 31(3): 354-7. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: hemolysis, influenza A virus avian
pathogenicity, chick embryo, hydrogen-ion concentration, kinetics, light,
scattering, radiation, time factors, virus cultivation.
Sugimura, T., Y. Murakami, and T. Ogawa (2000). The
susceptibility of culture cells to avian influenza viruses. Journal of Veterinary
Medical Science the Japanese Society of Veterinary Science 62(6):
659-60. ISSN: 0916-7250.
NAL
Call Number: SF604.J342
Abstract: The susceptibilities of culture cells to
twelve avian influenza virus strains were determined with ten established cell
lines including MDCK and ESK cells and three primary culture cells. The
established cell lines derived from embryonic swine kidney (ESK) and chicken
kidney (CK) primary culture cells were more sensitive to the avian influenza
viruses than the other eleven cells. The ESK cell had a particularly higher
infective titer than the MDCK cell with and without trypsin supplement in
culture medium, and dispersion of the infective titers was narrower than that
of the MDCK cell. The ESK cell is a suitable candidate for routine work on
avian influenza viruses in laboratories.
Descriptors: fowl plague immunology, influenza A virus
avian immunology, cell line immunology, chick embryo, chickens, cytopathogenic
effect, viral immunology, fowl plague virology, hemagglutination, avian
pathogenicity, poultry, swine, trypsin chemistry.
Sugimura, T., T. Ogawa, Y. Tanaka, and T. Kumagai
(1981). Antigenic type of fowl plague virus isolated in Japan in 1925. National
Institute of Animal Health Quarterly 21(2): 104-5. ISSN: 0027-951X.
NAL
Call Number: 41.9 T5750
Descriptors: antigens, viral analysis, influenza A virus
avian immunology, cross reactions, hemagglutination inhibition tests, Japan.
Sugrue, R.J., R.B. Belshe, and A.J. Hay (1990). Palmitoylation
of the influenza A virus M2 protein. Virology 179(1): 51-6. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The M2 proteins of a variety of influenza A
viruses of different subtypes were shown to possess associated palmitate.
Susceptibility to removal by reduction or treatment with hydroxylamine is
consistent with attachment via a thioester linkage to cysteine. The absence of
the acyl group from the M2 proteins of several equine viruses of the H3N8
subtype correlates with the replacement of cysteine 50 with phenylalanine and
points to this as the site of palmitate attachment.
Descriptors: influenza A virus metabolism, palmitic acids
metabolism, viral matrix proteins metabolism, amino acid sequence, chick
embryo, avian metabolism, human metabolism, molecular sequence data, molecular
weight, palmitic acid, sequence homology, nucleic acid, viral matrix proteins
isolation and purification.
Sugrue, R.J. and A.J. Hay (1991). Structural
characteristics of the M2 protein of influenza A viruses: evidence that it
forms a tetrameric channel. Virology 180(2): 617-24. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The evidence presented shows that the M2
protein of influenza A viruses exists in infected cells as a homotetramer
composed of two disulfide-linked dimers held together by noncovalent
interactions. The amphiphilic nature of the transmembrane alpha-helical domain
is consistent with the protein forming a transmembrane channel with which
amantadine, the specific anti-influenza A drug, interacts. Together these
features provide a structural basis for the hypothesis that M2 has a proton
translocation function capable of regulating the pH of vesicles of the
trans-Golgi network, a role important in promoting the correct maturation of
the hemagglutinin glycoprotein.
Descriptors: influenza A virus avian physiology, viral
matrix proteins isolation and purification, cultured cells, centrifugation,
density gradient, chick embryo, chickens, ducks, electrophoresis, gel, two
dimensional, electrophoresis, polyacrylamide gel, macromolecular systems,
models, structural, molecular weight, protein conformation, viral matrix
proteins metabolism.
Sulimov, A.A. and V.N. Siurin (1967). Metodika
metki virusa klassicheskoi chumy ptits radioaktivnym fosforom. [The method of
marking classic fowl plague virus with radioactive phosphorus]. Veterinariia
44(3): 33-5. ISSN: 0042-4846.
NAL
Call Number: 41.8 V6426
Descriptors: influenza A virus avian isolation and
purification, phosphorus isotopes, bacteriological techniques.
Suzuki, Y. (2000). [Receptor sialylsugar chains as
determinants of host range of influenza viruses]. Nippon Rinsho Japanese
Journal of Clinical Medicine 58(11): 2206-10. ISSN: 0047-1852.
Abstract: All types of the hemagglutinin(HA) of human,
pig, horse and aq. bird influenza A viruses, recognize sialyl lacto-series type
I and II sugar chains(Sialic acid(SA) alpha 2-3(6)Gal beta 1-3(4) GlcNAc beta
1-) in glycoproteins and glycolipids in the target cells as common receptor
molecules. Avian and equine influenza viruses preferentially binds the terminal
sialic acid alpha 2-3Gal(SA2-3Gal) linkage, while human influenza viruses
preferentially bind the SA2-6Gal linkage. SA distribution in animal species
influence influenza virus host range. Swine trachea has both receptors for
avian influenza viruses (SA2-3Gal specific) and for human influenza
viruses(SA2-6Gal specific). In the case of horses, a virus with an HA
recognizing Neu5Ac2-6Gal, but not Neu5Ac2-3Gal, failed to replicate in horses,
while one with an HA recognizing the Neu5Gc2-3Gal moiety replicated in horses.
The abundance of the Neu5Gc2-3Gal moiety in epithelial cells of horse trachea
supports that recognition of Neu5Gc2-3Gal moiety is critical for viral
replication in horses. The Neu5Gc2-3Gal is also associated with viral
replication in duck intestine, primarily in the crypt epitherial cells. Such
recognition, together with biochemical evidence of Neu5Gc in crypt cells,
correlated exactly with the ability of the virus to replicate in duck colon.
These results indicate the evidence of biologic effect of different sialic acid
species in different animals.
Descriptors: orthomyxoviridae physiology, receptors, virus
chemistry, sialic acids analysis, glycolipids analysis, glycoproteins analysis.
Swayne, D.E. (1997). Pathobiology of H5N2 Mexican
avian influenza virus infections of chickens. Veterinary Pathology
34(6): 557-67. ISSN: 0300-9858.
NAL
Call Number: 41.8 P27
Abstract: To determine the association between specific
structural changes in the hemagglutinin gene and pathogenicity of avian
influenza viruses (AIVs), groups of 4-week-old White Plymouth Rock chickens
were inoculated intravenously or intranasally with AIVs of varying
pathogenicities isolated from chickens in central Mexico during 1994-1995.
Mildly pathogenic (MP) viruses had a common hemagglutinin-connecting peptide
sequence of Pro-Gln-Arg-Glu-Thr-Arg decreases Gly and had restricted capability
for replication and production of lesions in tissues. The principle targets for
virus replication or lesion production were the lungs, lymphoid organs, and
visceral organs containing epithelial cells, such as kidney and pancreas. Death
was associated with respiratory and/or renal failure. By contrast, highly
pathogenic (HP) AIVs had one substitution and the addition of two basic amino
acids in the hemagglutinin connecting peptide, for a sequence of
Pro-Gln-Arg-Lys-Arg-Lys-Thr-Arg decreases Gly. The HP AIVs were pantropic in
virus replication and lesion production ability. However, the most severe
histologic lesions were produced in the brain, heart, adrenal glands, and
pancreas, and failure of multiple critical organs was responsible for disease
pathogenesis and death. No differences in lesion distribution patterns or in
sites of AIV replication were evident to explain the variation in mortality
rates for different HP AIVs, but HP AIVs that produced the highest mortality
rates had more severe necrosis in heart and pancreas. The ability of individual
HP AIVs to produce low or high mortality rates could not be explained by
changes in sequence of the hemagglutinin-connecting peptide alone, but probably
required the addition of other undetermined genomic changes.
Descriptors: chickens, fowl plague pathology, influenza A
virus avian genetics, avian pathogenicity, avian physiology, adrenal glands
chemistry, adrenal glands pathology, adrenal glands virology, brain pathology,
brain virology, brain chemistry, fowl plague epidemiology, fowl plague
mortality, hemagglutinins viral chemistry, hemagglutinins viral genetics,
immunohistochemistry, kidney chemistry, kidney pathology, kidney virology,
Mexico epidemiology, myocardium chemistry, myocardium pathology, pancreas
chemistry, pancreas pathology, pancreas virology, specific pathogen free
organisms, spleen chemistry, spleen pathology, spleen virology, viral proteins
analysis, viral proteins metabolism, virus replication.
Swayne, D.E. and J.R. Beck (2004). Heat
inactivation of avian influenza and Newcastle disease viruses in egg products.
Avian Pathology 33(5): 512-8.
ISSN: 0307-9457.
NAL
Call Number: SF995.A1A9
Abstract: Avian influenza (AI) and Newcastle disease
(ND) viruses are heat labile viruses, but exact parameters for heat
inactivation at egg pasteurization temperatures have not been established. In
this study we artificially infected four egg products with two AI (one low [LP]
and one high pathogenicity [HP]) and three ND (two low and one highly virulent)
viruses, and determined inactivation curves at 55, 57, 59, 61 and 63 degrees C.
Based on D(t) values, the time to inactivation of the viruses was dependent on
virus strain and egg product, and was directly related to virus titre, but
inversely related to temperature. For all temperatures, the five viruses had
the most rapid and complete inactivation in 10% salt yolk, while the most
resistant to inactivation was HPAI virus in dried egg white. This study
demonstrated that the LPAI and all ND viruses were inactivated in all egg
products when treated using industry standard pasteurization protocols. By
contrast, the HPAI virus was inactivated in liquid egg products but not in
dried egg whites when using the low-temperature industry pasteurization
protocol.
Descriptors: chickens virology, eggs virology, heat,
influenza A virus, avian pathogenicity, Newcastle disease virus pathogenicity,
virus inactivation, time factors.
Swayne, D.E., M.J. Radin, T.M. Hoepf, and R.D.
Slemons (1994). Acute renal failure as the cause of death in chickens
following intravenous inoculation with avian influenza virus
A/chicken/Alabama/7395/75 (H4N8). Avian Diseases 38(1):
151-157. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: One-day-old and 5-week-old commercial
leghorn, specific-pathogen-free leghorn, and broiler chickens were inoculated
intravenously with either avian influenza virus isolate
A/chicken/Alabama/7395/75 (H4N8) (Ck/AL) or sterile diluent. Ck/AL infection
resulted in a 44% mortality rate, reduced weight gains, and necrosis of
proximal renal tubules and/or tubulointerstitial nephritis. The renal tubule
necrosis was more severe and widespread in chickens that died than in chickens
that were euthanatized. Hyperuricemia, hypercalcemia, and hyperphosphatemia
were present in 5-week-old chickens at day 5 postinfection. Influenza virus
isolate Ck/AL was nephropathogenic, and death was associated with acute severe
renal damage and failure. Some data suggested that the pathogenicity of Ck/AL
may be more severe in leghorns than broilers.
Descriptors: chickens, avian influenza virus, kidney
diseases, biological differences, age, experimental infection, in vivo
experimentation, pathogenicity, kidneys, histopathology, symptoms, animal
morphology, biological properties, birds, disease transmission, domestic
animals, domesticated birds, experimentation, Galliformes, infection,
influenza virus, livestock, microbial properties, organic diseases,
pathogenesis, pathology, poultry, urinary tract, urinary tract diseases,
urogenital system, useful animals, viruses,
age differences.
Swayne, D.E. and R.D. Slemons (1994). Comparative
pathology of a chicken-origin and two duck-origin influenza virus isolates in
chickens: the effect of route of inoculation. Veterinary Pathology
31(2): 237-45. ISSN: 0300-9858.
NAL
Call Number: 41.8 P27
Abstract: Forty-nine 5-week-old chickens were
inoculated by the intravenous (i.v.), intratracheal (IT), or intranasal (IN)
routes with either a chicken-origin or one of two duck-origin type A influenza
virus isolates. Twelve control chickens were inoculated with sterile
chorioallantoic fluid. For all viruses, i.v. inoculation produced predominate
lesions of renal tubule necrosis (nephrosis) and nephritis, and influenza virus
nucleoprotein was localized in nuclei and cytoplasm of necrotic renal tubule
epithelium. Chickens inoculated by the IT route, and to a lesser extent the IN
route, had mild to severe tracheitis, bronchitis, and ventromedial pneumonia
associated with secondary bronchi but lacked renal tubule necrosis and
nephritis. These data indicate low-virulence avian-origin influenza viruses
were nephrotropic during simulated systemic infection (i.v. inoculation) and
pneumotropic during simulated local infection (IT and IN inoculation). Gross
and histologic kidney lesions produced by i.v. inoculation of the
chicken-origin influenza virus were similar to changes reported in outbreaks of
low-virulence influenza virus in laying chickens.
Descriptors: chickens microbiology, ducks microbiology,
fowl plague pathology, influenza A virus avian pathogenicity, poultry diseases
pathology, acute disease, administration, intranasal, immunohistochemistry,
injections, intravenous, intubation, intratracheal, virulence.
Swayne, D.E. and D.L. Suarez (2003). Additional
glycosylation at the receptor binding site of the hemagglutinin (HA) for H5 and
H7 viruses may be an adaptation to poultry hosts, but does it influence
pathogenicity? Avian Diseases 47(Special Issue): 942-950. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Descriptors: binding sites, genes, hemagglutinins,
pathogenicity, phylogenetics, poultry, viral proteins, avian influenza virus,
Italy, United Kingdom, Galliformes.
Tablante, N., L. Carr, and G. Malone. (2004). Guidelines
for In-House Composting of Poultry Mortalities Due to Catastrophic Diseases.
In: 2004 Virginia Poultry Health & Management Seminar, Roanoke, VA, p.
23.
NAL
Call Number:
TD899.P65.T3 2004
Abstract: Comprehensive guidelines were
developed and used to train poultry company presonnel on in-house composting
procedures. Results to date suggest in-house composting of avian influenza
infected flocks is a biosecure, cost effective and efficient means of dosposal
of broiler carcasses in clear-span houses.
Descriptors: poultry, avian influenza,
composting, in-house composting, infected flocks.
Tagov, I. (1970). Kum antivirusnoto deistvie na
amonieviia ion vurkhu reproduksiiata na niakoi virusi ot miksogrupata v
kletuchni kulturi. [Anti-viral effect of the ammonium ion on the reproduction
of certain viruses of the myxo-group in cell cultures]. Izvestiia Na
Mikrobiologicheskiia Institut 21: 201-12.
ISSN: 0068-3957.
NAL
Call Number: 448.39 B87
Descriptors: ammonium chloride pharmacology, influenza A
virus avian drug effects, orthomyxoviridae drug effects, virus replication drug
effects, ammonium sulfate pharmacology, cattle immunology, kidney, tissue
culture, virus cultivation.
Takahashi, T., Y. Suzuki, D. Nishinaka, N. Kawase, Y.
Kobayashi, K.I. Hidari, D. Miyamoto, C.T. Guo, K.F. Shortridge, and T. Suzuki
(2001). Duck and human pandemic influenza A viruses retain sialidase
activity under low pH conditions. Journal of Biochemistry 130(2):
279-83. ISSN: 0021-924X.
NAL
Call Number: 385 J822
Abstract: The majority of influenza A viruses isolated
from wild birds, but not humans, can replicate in the duck intestinal tract.
Here we demonstrate that all duck isolates tested universally retain sialidase
activities under low pH conditions independent of their neuraminidase (NA)
subtypes. In contrast, the sialidase activities of most isolates from humans
and pigs practically disappear below pH 4.5, with the exception of four human
pandemic viruses isolated in 1957 and 1968. Sequence comparisons among duck,
human, and swine N2 NA subtypes indicate that amino acids at positions 153,
253, 307, 329, 344, 347, 356, 368, 390, and 431 may be associated with the low
pH stability of duck and human pandemic N2 NAs. This finding suggests that the
low pH stability of duck influenza A virus NA may be a critical factor for
replication in the intestinal tract through the digestive tract of ducks, and
that the properties of NAs are important for understanding the epidemiology of
the influenza virus.
Descriptors: influenza virology, influenza A virus avian
enzymology, human enzymology, neuraminidase metabolism, ducks, enzyme
stability, hydrogen-ion concentration, influenza transmission, avian
physiology, human physiology, porcine enzymology, phylogeny, sequence analysis,
swine.
Takeuchi, K. and R.A. Lamb (1994). Influenza virus
M2 protein ion channel activity stabilizes the native form of fowl plague virus
hemagglutinin during intracellular transport. Journal of Virology
68(2): 911-9. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The influenza A/fowl plague virus/Rostock/34
hemagglutinin (HA), which is cleaved intracellularly and has a high pH
threshold (pH 5.9) for undergoing its conformational change to the low-pH form,
was expressed from cDNA in CV-1 and HeLa T4 cells in the absence of other
influenza virus proteins. It was found, by biochemical assays, that the
majority of the HA molecules were in a form indistinguishable from the low-pH
form of HA. The acidotropic agent, ammonium chloride, stabilized the
accumulation of HA in its native form. Coexpression of HA and the homotypic
influenza virus M2 protein, which has ion channel activity, stabilized the
accumulation of HA in its pH neutral (native) form, and the M2 protein ion
channel blocker, amantadine, prevented the rescue of HA in its native form.
These data provide direct evidence that the influenza virus M2 protein ion
channel activity can affect the status of the conformational form of cleaved HA
during intracellular transport.
Descriptors: hemagglutinins viral metabolism, influenza A
virus metabolism, ion channels, viral matrix proteins metabolism, amantadine
pharmacology, ammonium chloride pharmacology, biological transport, cultured
cells, cercopithecus aethiops, endopeptidases pharmacology, glucosaminidase
pharmacology, HeLa cells, hemagglutinin glycoproteins, influenza virus, hemagglutinins
viral drug effects, hemagglutinins viral genetics, hydrogen-ion concentration,
influenza A virus avian metabolism, oxidation reduction, protein conformation, recombinant proteins
metabolism, viral matrix proteins genetics.
Takeuchi, K., M.A. Shaughnessy, and R.A. Lamb (1994).
Influenza virus M2 protein ion channel activity is not required to maintain
the equine-1 hemagglutinin in its native form in infected cells. Virology
202(2): 1007-11. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The equine-1 influenza virus A/Cornell/74
(H7N7) hemagglutinin (HA) is cleaved to HA1 and HA2 in the trans Golgi network
(TGN) of infected cells. The avian influenza virus A/chicken/Germany/34 (fowl
plague virus Rostock) H7 HA is also cleaved to HA1 and HA2 intracellularly in
the TGN. To maintain the fowl plague virus Rostock HA in its native form during
transport through the TGN, a functioning M2 ion channel activity is required,
otherwise the HA undergoes its transition to the low-pH form (Sugrue et al.,
1990, EMBO J. 9, 3469-3476). Studies were initiated to investigate if the
equine H7 HA has intracellular requirements different from those of the fowl
plague virus Rostock HA. We report here that the pH of transition to the low-pH
form of the equine-1 HA is approximately pH 5.3 and that the M2 protein ion
channel blocker, amantadine, does not have a discernable effect on the native
conformation of equine-1 HA during transport through the TGN. Moreover, the
equine-1 HA expressed from cDNA does not require coexpression of a functional
M2 protein to maintain HA in its native conformation.
Descriptors: hemagglutinins viral metabolism, influenza A
virus metabolism, ion channels physiology, viral matrix proteins physiology,
amantadine pharmacology, biological transport, Golgi apparatus metabolism,
hydrogen-ion concentration, protein processing, post translational, virus
replication drug effects.
Taylor, H.P., S.J. Armstrong, and N.J. Dimmock (
1987). Quantitative relationships between an influenza virus and neutralizing
antibody. Virology 159(2): 288-98.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: In this quantitative study of the interaction
of influenza virus with neutralizing antibody we have determined the maximum
number of antibody molecules which can bind to the haemagglutinin (HA) of
native influenza A/FPV/Rostock/34 (H7N1) particles in aqueous suspension and
the minimum number which is required to cause neutralization. Using
radiolabelled immunoglobulins approximately one IgG molecule, whether of
monoclonal or polyclonal origin, binds per HA spike under conditions of
antibody saturation. In the same manner, we have determined that when
infectivity is neutralized by 63% (1/e) about 70 molecules of monoclonal IgGs
HC2 and HC10 were bound per virus particle and this is supported by independent
evidence from electron microscopy. However, the kinetics of neutralization were
single-hit or at most, under critical conditions of low temperature (4 degrees)
and minimal neutralizing concentrations of antibody, two-hit. This apparent
conflict is reconciled by a hypothesis which proposes that neutralization
occurs only when antibody binds to certain "neutralization relevant"
HA spikes which are in the minority. It is suggested that these only differ
from the majority of "neutralization irrelevant" HA spikes by their
transmembrane interaction with the core of the virion.
Descriptors: antibodies, viral immunology, hemagglutinins
viral immunology, influenza A virus avian immunology, antibodies, monoclonal immunology,
hemagglutination inhibition tests, hemagglutinin glycoproteins, influenza
virus, immunoglobulin G immunology, neutralization tests, radioimmunoassay.
Taylor, H.P. and N.J. Dimmock (1994). Competitive
binding of neutralizing monoclonal and polyclonal IgG to the HA of influenza A
virions in solution: only one IgG molecule is bound per HA trimer regardless of
the specificity of the competitor. Virology 205(1): 360-3. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Two-step solution competition assays were
performed in solution with influenza type A virions and hemagglutinin
(HA)-specific neutralizing monoclonal antibodies (mabs). These demonstrated
that the binding of one molecule of IgG mab per HA trimer prevented the binding
of mabs directed against other antigenic sites on the HA (site A, site B, or
site D), even though these are topographically separate and antigenically
independent. Furthermore the same procedures showed that one molecule of mab
per trimer prevented the binding of polyclonal HA-specific IgG obtained from
the serum of rabbits immunized with whole virus. This restricted binding is
clearly a property of the intact virion, since others using purified HA have
shown that up to four IgG molecules of different specificities can bind per
trimer. Since the surface area of the globular head of the trimer is equivalent
to approximately 10 nonoverlapping antibody footprints, it is not understood
how one prebound IgG molecule prevents the binding of other IgG molecules.
Descriptors: hemagglutinins viral immunology,
immunoglobulin G immunology, influenza A virus avian immunology, viral envelope
proteins immunology, antibodies, monoclonal immunology, antibody specificity,
binding sites, antibody, binding, competitive, chick embryo, hemagglutinin
glycoproteins, influenza virus, neutralization tests, solutions, virion
immunology.
Tentsov, I., A.K. Gitel'man, and A.G. Burkrinskaia
(1978). Vnutrikletochnye struktury virusa grippa. [Intracellular structures
of influenza virus]. Molekuliarnaia Biologiia 12(2): 308-15. ISSN: 0026-8984.
NAL
Call Number: QH506.A1M62
Abstract: The intracellular influenza virus-containing
structures involved in RNA synthesis in the cytoplasm and in the nucleoplasm of
infected chicken fibroblasts were studied. Two approaches were used: (1) short
pulse labeling of infected cell with [3H]uridine; (2) determination in vitro of
polymerase activity of intracellular virus-specific structures. Both methods
revealed functionally active virus-specific structures in the nucleoplasm and
showed that a functionally active virus-specific structure was localized in the
nucleoplasm of infected cells. This structure contained proteins of the viral
ribonucleoprotein, but sedimented somewhat faster (at 60--90S in velocity
sucrose and glycerol gradients). Meanwhile, polymerase-containing structures in
the cytoplasm of infected cells sedimented in the position of viral
ribonucleoproteins (25--60S).
Descriptors: influenza A virus avian ultrastructure, viral
proteins analysis, cell nucleus enzymology, cell nucleus microbiology, cultured
cells, cytoplasm microbiology, DNA directed RNA polymerases metabolism,
electrophoresis, polyacrylamide gel, avian analysis, avian enzymology, uridine
metabolism.
Thiry, L. (1968). The action of sparsomycin and
gougerotin on virus growth. Journal of General Virology 2(1):
143-53. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: amino acids metabolism, anti bacterial agents
pharmacology, RNA, messenger antagonists and inhibitors, viruses drug effects,
arginine metabolism, asparagine metabolism, carbon isotopes, encephalitis
viruses drug effects, glycine metabolism, herpesviridae drug effects, influenza
A virus avian drug effects, leucine metabolism, lysine metabolism, molecular biology,
Newcastle disease virus drug effects, phenylalanine metabolism, proline
metabolism, vaccinia virus drug effects, virus replication drug effects.
Thomas, F.C., T. Ouwerkerk, and P. McKercher (1982). Inactivation
by gamma irradiation of animal viruses in simulated laboratory effluent. Applied
and Environmental Microbiology 43(5): 1051-6. ISSN: 0099-2240.
NAL
Call Number: 448.3 Ap5
Abstract: Several animal viruses were treated with
gamma radiation from a 60Co source under conditions which might be found in
effluent from an animal disease laboratory. Swine vesicular disease virus,
vesicular stomatitis virus, and blue-tongue virus were irradiated in tissues
from experimentally infected animals. Pseudorabies virus, fowl plague virus,
swine vesicular disease virus, and vesicular stomatitis virus were irradiated
in liquid animal feces. All were tested in animals and in vitro. The D10
values, that is, the doses required to reduce infectivity by 1 log10, were not
apparently different from those expected from predictions based on other data
and theoretical considerations. The existence of the viruses in pieces of
tissue or in liquid feces made no difference in the efficacy of the gamma
radiation for inactivating them. Under the "worst case" conditions
(most protective for virus) simulated in this study, no infectious agents would
survive 4.0 Mrads.
Descriptors: feces microbiology, sewage, viruses radiation
effects, bluetongue virus radiation effects, enteroviruses, porcine radiation
effects, gamma rays, herpesvirus 1, suid radiation effects, influenza A virus
avian radiation effects, vesicular stomatitis Indiana virus radiation effects.
Thomas, G.P., M. Forsyth, C.R. Penn, and J.W.
McCauley (1994). Inhibition of the growth of influenza viruses in vitro by
4-guanidino-2,4-dideoxy-N-acetylneuraminic acid. Antiviral Research
24(4): 351-356. ISSN: 0166-3542.
NAL
Call Number: QR355.A5
Abstract: The sialidase inhibitor
4-guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid was tested for
growth inhibitory effects against a panel of avian influenza A viruses
encompassing all nine neuraminidase subtypes. Growth in tissue culture of
viruses from each subtype was inhibited by this compound at concentrations
within a range previously found effective against human N1 and N2 viruses. This
compound may prove a selective agent for the treatment (and prevention) of
influenza virus infections.
Descriptors: enzymology, microbiology, pharmacology,
antiviral drug avian influenza viruses human influenza viruses neuraminidase
inhibition pharmacodynamics 4-guanidino-2,4-dideoxy-N-acetylneuraminic acid.
Thrum, H., K. Eckardt, G. Bradler, R. Fugner, E.
Tonew, and M. Tonew (1975). Streptovirudins, new antibiotics with
antibacterial and antiviral activity. I. Culture taxonomy, fermentation and
production of streptovirudin complex. Journal of Antibiotics 28(7):
514-21. ISSN: 0021-8820.
NAL
Call Number: 396.8 J824
Abstract: A new antibiotic complex has been isolated
from cultures of Streptomyces strain No. JA 10124. On the basis of
taxonomic studies, the producing microorganism is described as Streptomyces
griseoflavus (Krainsky, 1914) Waksman et Henrici, 1948, subsp.
thuringiensis subsp. nov., type strain JA 10124. The antibiotic complex,
designated as streptovirudin, was isolated from extracts of both mycelium and
culture filtrate. It is a white amorphous material which consists of ten
closely related components including streptovirudins A, B, C, D and E. The streptovirudin
complex exhibits antibiotic activity against Gram-positive bacteria, Mycobacteria,
and various DNA- and RNA-viruses.
Descriptors: anti bacterial agents isolation and
purification, antiviral agents isolation and purification, administration, oral,
anti bacterial agents administration and dosage, anti bacterial agents
pharmacology, antiviral agents pharmacology, Chlamydia drug effects,
fermentation, herpesvirus 1, suid drug effects, influenza A virus avian drug
effects, injections, intraperitoneal, injections, intravenous, injections,
subcutaneous, mice, Mycobacterium drug effects, Newcastle disease virus
drug effects, sheep, sindbis virus drug effects, Streptomyces analysis, Streptomyces
classification, vaccinia virus drug effects.
Tian, S.F., A.J. Buckler White, W.T. London, L.J.
Reck, R.M. Chanock, and B.R. Murphy (1985). Nucleoprotein and membrane
protein genes are associated with restriction of replication of influenza
A/Mallard/NY/78 virus and its reassortants in squirrel monkey respiratory tract.
Journal of Virology 53(3): 771-5.
ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: An avian influenza A virus,
A/Mallard/NY/6750/78(H2N2), was restricted in in replication in the respiratory
tract of squirrel monkeys. Avian-human influenza A reassortant viruses
possessing the six RNA segments coding for nonsurface proteins (i.e., internal
genes) of this avian virus were as restricted in replication in squirrel
monkeys as their avian influenza parent. These findings indicated that
restriction of replication of the avian influenza virus is a function of one or
more of its internal genes. For an investigation of which of the avian
influenza genes was responsible for restricted replication in the respiratory
tract of primates, reassortant viruses were produced that contained human
influenza virus surface antigens from the A/Udorn/72(H3N2) virus and one or
more of the internal genes derived from the avian influenza virus parent.
Avian-human reassortant influenza A viruses containing only the nucleoprotein
or matrix protein RNA segment from the avian influenza virus parent were as
restricted in their growth as an avian-human influenza reassortant virus
containing each of the six avian influenza internal genes. In addition, an
avian-human influenza reassortant virus possessing only the avian RNA 1 and
nonstructural genes (which by themselves do not specify restricted replication)
manifested a significant reduction of virus replication in squirrel monkey
tracheas. Thus, the avian nucleoprotein and matrix genes appear to play a major
role in the host range restriction exhibited by the A/Mallard/78 virus and its
reassortants, but the combination of RNA 1 and nonstructural genes also
contributes to restriction of replication.
Descriptors: genes viral, influenza A virus genetics,
nucleoproteins genetics, viral proteins genetics, virus replication, birds
microbiology, heat, influenza A virus physiology, RNA viral analysis, saimiri
microbiology, trachea microbiology, viral matrix proteins.
Tian, S.F., A.J. Buckler White, W.T. London, L.J.
Reck, R.M. Chanock, and B.R. Murphy (1986). [Nucleoprotein and membrane
protein genes responsible for restriction of replication of influenza
A/Mallard/NY/78 virus and its reassortants in the respiratory tract of squirrel
monkeys]. Zhongguo Yi Xue Ke Xue Yuan Xue Bao Acta Academiae Medicinae
Sinicae 8(1): 1-6. ISSN: 1000-503X.
Descriptors: genes viral, influenza A virus avian
genetics, recombination, genetic, virus replication, avian physiology, membrane
proteins genetics, nucleoproteins genetics, respiratory system microbiology,
saimiri.
Timakov, V.D., V.A. Zuev, E.P. Mirchink, and V.V.
Peters (1972). Alterations of L-cell cultures infected by influenza viruses.
Brief report. Archiv Fur Die Gesamte Virusforschung 37(2):
279-81. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian growth and
development, l cells cell line microbiology, orthomyxoviridae growth and
development, adsorption, cytopathogenic effect, viral, mitosis, simplexvirus growth and development,
vesicular stomatitis Indiana virus growth and development, virus replication.
Tollis, M. and T.L. Di (2002). Recent developments
in avian influenza research: Epidemiology and immunoprophylaxis. Veterinary
Journal 164(3): 202-215. ISSN:
1090-0233.
NAL
Call Number: SF601.V484
Abstract: Influenza A viruses have been isolated from
humans, from several other mammalian species and a wide variety of avian
species, among which, wild aquatic birds represent the natural hosts of influenza
viruses. The majority of the possible combinations of the 15 haemagglutinin
(HA) and nine neuraminidase (NA) subtypes recognized have been identified in
isolates from domestic and wild birds. Infection of birds can cause a wide
range of clinical signs, which may vary according to the host, the virus
strain, the host's immune status, the presence of any secondary exacerbating
microorganisms and environmental factors. Most infections are inapparent,
especially in waterfowl and other wild birds. In contrast, infections caused by
viruses of H5 and H7 subtypes can be responsible for devastating epidemics in
poultry. Despite the warnings to the poultry industry about these viruses, in
1997 an avian H5N1 influenza virus was directly transmitted from birds to
humans in Hong Kong and resulted in 18 confirmed infections, thus strengthening
the pandemic threat posed by avian influenza (AI). Indeed, reassortant viruses,
harbouring a combination of avian and human viral genomes, have been
responsible for major pandemics of human influenza. These considerations
warrant the need to continue and broaden efforts in the surveillance of AI.
Control programmes have varied from no intervention, as in the case of the
occurrence of low pathogenic (LP) AI (LPAI) viruses, to extreme, expensive
total quarantine-slaughter programmes carried out to eradicate highly
pathogenic (HP) AI (HPAI) viruses. The adoption of a vaccination policy,
targeted either to control or to prevent infection in poultry, is generally
banned or discouraged. Nevertheless, the need to boost eradication efforts in
order to limit further spread of infection and avoid heavy economic losses, and
advances in modern vaccine technologies, have prompted a re-evaluation of the
potential use of vaccination in poultry as an additional tool in comprehensive
disease control strategies. This review presents a synthesis of the most recent
research on AI that has contributed to a better understanding of the ecology of
the virus and to the development of safe and efficacious vaccines for poultry.
Descriptors: animal husbandry, epidemiology, immune
system, infection, veterinary medicine, virology, avian influenza, respiratory
system disease, viral disease, avian influenza research: epidemiology,
immunoprophylaxis, recent developments avian influenza vaccine development
immunoprophylaxis poultry vaccine development: efficacy, safety.
Tomassini, J.E. (1996). Expression, purification,
and characterization of orthomyxovirus: influenza transcriptase. Methods
in Enzymology 275: 90-9. ISSN:
0076-6879.
NAL
Call Number: QP601.M49
Descriptors: influenza A virus avian enzymology, RNA
directed DNA polymerase biosynthesis, RNA directed DNA polymerase isolation and
purification, ribonucleoproteins isolation and purification, transcription,
genetic, base sequence, centrifugation,
density gradient methods, chick embryo, electrophoresis, polyacrylamide gel
methods, indicators and reagents, avian genetics, molecular sequence data, RNA
directed DNA polymerase chemistry, recombinant proteins biosynthesis,
recombinant proteins chemistry, recombinant proteins isolation and
purification, ribonucleoproteins metabolism, templates, genetic.
Tompkins, S.M., C.Y. Lo, T.M. Tumpey, and S.L.
Epstein (2004). Protection against lethal influenza virus challenge by RNA
interference in vivo. Proceedings of the National Academy of Sciences of
the United States of America 101(23): 8682-6. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Influenza virus infection is responsible for
hundreds of thousands of deaths annually. Current vaccination strategies and
antiviral drugs provide limited protection; therefore, new strategies are
needed. RNA interference is an effective means of suppressing virus replication
in vitro. Here we demonstrate that treatment with small interfering RNAs
(siRNAs) specific for highly conserved regions of the nucleoprotein or acidic
polymerase inhibits influenza A virus replication in vivo. Delivery of these
siRNAs significantly reduced lung virus titers in infected mice and protected
animals from lethal challenge. This protection was specific and not mediated by
an antiviral IFN response. Moreover, influenza-specific siRNA treatment was
broadly effective and protected animals against lethal challenge with highly
pathogenic avian influenza A viruses of the H5 and H7 subtypes. These results
indicate that RNA interference is promising for control of influenza virus
infection, as well as other viral infections.
Descriptors: influenza prevention and control, RNA
interference, base sequence, influenza A virus, avian genetics, avian
physiology, mice, inbred balb c, RNA, small interfering administration and
dosage, small interfering genetics, viral genetics, virus replication.
Tonew, E., K. Augsten, B. Gumpert, and H. Ulbricht
(1973). The antiviral activity of
1-(p-(methylnitrosamino)-benzylidenamino)-adamantane on the fowl plague virus
in tissue cultures. II. Spectrophotometrical studies. Acta
Microbiologica Polonica. Series A Microbiologia Generalis 5(3): 221-3. ISSN: 0567-7815.
NAL
Call Number: QR1.A32
Descriptors: amantadine pharmacology, influenza A virus
avian drug effects, spectrophotometry, benzyl compounds pharmacology, chick
embryo, cytopathogenic effect, viral drug effects, fibroblasts, nitrosamines pharmacology, time
factors, tissue culture, virus replication drug effects.
Tonew, E., K. Eckardt, W. Fleck, and P. Zopel (1970).
Die antivirale Wirkung des Streptomyceten-Antibioticums IMET A 8136-A
(Borrelidin) auf das Virus der klassischen Geflugelpest in vitro. [The
antiviral effect of the Streptomyces antibiotic IMET A 8136-A (borrelidin) on
the classical fowl plague virus in vitro]. Zeitschrift Fur Allgemeine
Mikrobiologie 10(5): 353-61. ISSN:
0044-2208.
NAL
Call Number: QR1.Z4
Descriptors: anti bacterial agents pharmacology, antiviral
agents pharmacology, influenza A virus avian drug effects, anti bacterial
agents biosynthesis, antiviral agents biosynthesis, chick embryo,
cytopathogenic effect, viral, fibroblasts, hemadsorption, hemagglutination
tests, avian growth and development, streptomyces metabolism, tissue culture,
virus cultivation, virus replication.
Tonew, E., M.K. Indulen, and D.R. Dzeguze (1982). Antiviral
action of dipyridamole and its derivatives against influenza virus A. Acta
Virologica 26(3): 125-9. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Dipyridamole proved to be active against
influenza viruses A/England 42/72, A/Bangkok 1/79 and A/fowl plague (FPV). The
antiviral activities assayed by various methods varied from 90-99 per cent. No
inhibition was found against influenza virus B/Leningrad 235/74 in vitro. Three
dipyridamole derivatives were significantly active in tissue cultures against
influenza virus A/England 42/72 and A/FPV. In white mice infected with
influenza virus A/England 42/72 dipyridamole administered orally showed a
protection rate of 62.5 per cent.
Descriptors: antiviral agents pharmacology, dipyridamole
pharmacology, influenza A virus drug effects, dipyridamole analogs and
derivatives, dipyridamole therapeutic use, influenza drug therapy, influenza A
virus avian drug effects, mice, rimantadine therapeutic use.
Tonew, E., M. Tonew, M.K. Indulen, and D.R. Dzeguze
(1982). Effects of streptovirudin on influenza viruses type A and B:
inhibition of the lipid-linked oligosaccharide synthesis of fowl plague virus.
Acta Virologica 26(6): 444-52.
ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Antibiotics of the streptovirudin complex
(SV) inhibited the growth of influenza A and B viruses such as influenza A/fowl
plague virus (FPV), strain Weybridge (Hav1 Neq1), influenza A/England 42/72
(H3N2), influenza A/Port Chalmers 1/73 (H3N2), influenza B/Leningrad 235/74,
influenza B/Tokyo 7/66, and influenza B/Jamagata in chick embryo cell (CEC)
cultures, in permanent canine kidney cells (MDCK), and in suspended fragments
of chick embryo chorioallantoic membranes (CAM). As revealed by
spectrophotometric turbidity measurements, SV completely inhibited the FPV-induced
cytopathic effect (CPE). A 99.99% reduction of infectious virus yield was
obtained in one-step growth cycle experiments and in the plaque reduction test.
The haemagglutination inhibition titres of influenza viruses in suspended CAM
fragment cultures in the presence of SV drugs were also substantially reduced.
The incorporation assays indicated that SV exhibited no effect on virus-induced
RNA synthesis, but influenced virus maturation by inhibition of lipid-linked
oligosaccharide synthesis. A partial protection from infection was found in
influenza virus A/England infected mice.
Descriptors: anti bacterial agents pharmacology, influenza
A virus avian drug effects, human drug effects, oligosaccharides biosynthesis,
orthomyxoviridae drug effects, cell line, cytopathogenic effect, viral drug
effects, dogs, dose response relationship, drug, glucose metabolism, avian
metabolism, mice, RNA viral biosynthesis, virus replication drug effects.
Tonew, M. and E. Klimke (1974). Antiviral
1,3,4-thiadiazoles. I. Action on multiplication of Mengo Virus in FL cells.
Chemotherapy 20(6): 350-60. ISSN:
0009-3157.
NAL
Call Number: RM260.C5
Descriptors: antiviral agents pharmacology, mengovirus
drug effects, thiadiazoles pharmacology, virus replication drug effects, cultured
cells, culture media, cytopathogenic effect, viral, depression, chemical,
influenza A virus avian drug effects, microbial sensitivity tests, plaque
assay, thiazoles, time factors, vaccinia virus drug effects.
Tonew, M., W. Laass, E. Tonew, R. Franke, H. Goldner,
and W. Zschiesche (1978). Antiviral activity of dipyridamole derivatives.
Acta Virologica 22(4): 287-95.
ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Among 46 novel pyrimido [5.4-d] pyrimidine
derivatives, 26 compounds were found to exhibit antiviral activity as revealed
in a test programme against Mengo, Coxsackie B1, fowl plague, vaccinia and
pseudorabies viruses, as concerns inhibition of plaque formation and of
infectious virus yield. Attempts to disclose structure-activity relationships
by discriminant analysis pointed to a possible importance of hydrophobic
substitution for the antiviral effectiveness against Mengo virus of the
derivatives investigated.
Descriptors: antiviral agents, dipyridamole analogs and
derivatives, cell line, chemistry, dipyridamole pharmacology, enterovirus B,
human drug effects, herpesvirus 1, suid drug effects, influenza A virus avian
drug effects, mengovirus drug effects, Newcastle disease virus drug effects,
vaccinia virus drug effects, virus replication drug effects.
Treanor, J., Y. Kawaoka, R. Miller, R.G. Webster, and
B. Murphy (1989). Nucleotide sequence of the avian influenza
A/Mallard/NY/6750/78 virus polymerase genes. Virus Research 14(3):
257-69. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The avian influenza A/Mallard/NY/6750/78
virus is currently being evaluated as a donor of attenuating genes in the
construction of live avian-human influenza A reassortant virus vaccines for use
in humans. We determined the nucleotide sequences of the three polymerase gene
segments of this virus. This completes the nucleotide sequence of the six
transferrable genes of the avian donor virus. Comparison of the nucleotide and
deduced amino acid sequences of the non-glycoprotein genes of the avian
A/Mallard/78 virus with representative avian and human influenza A viruses
suggests that the PB1 gene of H2N2 subtype human influenza A viruses may have
been derived from a non-human, possibly avian influenza A virus by genetic
reassortment. In addition, several regions of conserved amino acids with
potential functional significance were identified in the deduced amino acid
sequences of the polymerase proteins.
Descriptors: influenza A virus avian genetics, amino acid
sequence, base sequence, DNA, viral genetics, genes viral, avian enzymology,
molecular sequence data, RNA directed DNA polymerase genetics, sequence
homology, nucleic acid.
Treanor, J.J., M.H. Snyder, W.T. London, and B.R.
Murphy (1989). The B allele of the NS gene of avian influenza viruses, but
not the A allele, attenuates a human influenza A virus for squirrel monkeys.
Virology 171(1): 1-9. ISSN:
0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The nonstructural (NS) genes of avian
influenza A viruses have been divided into two groups on the basis of
nucleotide sequence homology, which we have referred to here as alleles A and
B. We sequenced the NS genes of eight additional avian influenza A viruses in
order to define the differences between these two alleles more thoroughly. Four
of the viruses had NS gene sequences which resembled that of A/FPV/Rostock/34
and belonged to allele A while the other four viruses had NS gene sequences
more similar to that of A/Duck/Alberta/76 and belonged to allele B. There was
approximately 90% sequence homology within alleles and 72% homology between
alleles. As previously reported the NS genes of human influenza A viruses
belong to allele A. We constructed single gene avian-human reassortant
influenza A viruses containing an allele A or B NS gene segment from an avian
influenza A virus and all other genes from a human influenza A virus and tested
these reassortants for their ability to grow in the respiratory tract of a
nonhuman primate. Reassortants containing an avian NS gene segment of allele B
were significantly restricted in growth in the respiratory tract of squirrel
monkeys while reassortants with an allele A NS gene segment were not. The
divergent evolution of the B NS allele in birds may have resulted in gene
products which do not function optimally in cooperation with genes from a human
virus in viral replication in primate respiratory epithelium.
Descriptors: capsid genetics, influenza A virus avian
genetics, human growth and development, viral core proteins genetics, alleles,
amino acid sequence, base sequence, genes viral, human genetics, molecular
sequence data, nasopharynx microbiology, saimiri microbiology, sequence
homology, nucleic acid, trachea microbiology, viral nonstructural proteins,
virus replication.
Treanor, J.J., E.L. Tierney, W.T. London, and B.R.
Murphy (1991). Characterization of the attenuating M and NP gene segments of
the avian influenza A/Mallard/78 virus during in vitro production of
avian-human reassortant vaccine viruses and after replication in humans and
primates. Vaccine 9(7): 495-501.
ISSN: 0264-410X.
NAL
Call Number: QR189.V32
Abstract: A unique requirement for live attenuated
reassortant influenza vaccines is the need to generate new reassortant vaccine
viruses with the appearance of each new antigenic variant. Thus, the attenuation
phenotype conferred by the attenuated donor influenza virus must remain
genetically stable during the generation of each new reassortant vaccine virus.
In this study we used nucleotide sequence analysis to evaluate the genetic
stability of the attenuating M and NP genes of the avian influenza
A/Mallard/NY/6750/78 attenuated donor virus during the in vitro generation and
subsequent in vivo replication of avian-human (AH) influenza A reassortant
vaccine viruses in monkeys and humans. Nucleotide sequence changes in the M and
NP genes occurred at a rate of approximately 0.61 substitutions/1000
nt/reassortant during in vitro generation of four AH reassortant viruses. Only
two nucleotide sequence changes occurred in the M and NP gene segments of four isolates
of H1N1 or H3N2 AH vaccine viruses following 6-8 days of replication in
seronegative children, and neither change affected amino acids previously
identified as playing a potential role in attenuation. In addition, there were
no changes in the nucleotide sequence of the M and NP genes of single gene AH
reassortant viruses following five serial passages in squirrel monkeys.
Finally, there was no change in the level or duration of replication of the
single gene reassortant viruses in the upper or lower respiratory tract of
monkeys following serial passage.(ABSTRACT TRUNCATED AT 250 WORDS)
Descriptors: influenza A virus avian genetics, influenza
vaccine genetics, nucleoproteins, viral core proteins genetics, viral matrix
proteins genetics, base sequence, cloning, molecular, avian pathogenicity,
avian physiology, human genetics, human pathogenicity, human physiology,
molecular sequence data, mutation
genetics, polymerase chain reaction, recombination, genetic physiology,
saimiri, vaccines, attenuated genetics, vaccines, synthetic genetics, virus
replication genetics.
Tucker, S.P., C.R. Penn, and J.W. McCauley (1991). Characterisation
of the influenza virus associated protein kinase and its resemblance to casein
kinase II. Virus Research 18(2-3): 243-61. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The protein kinase activity associated with
purified influenza virus has been examined. By use of a radiolabelled
photoreactive ATP analogue (3'-O-(4-benzoyl) benzoyl adenosine triphosphate) a
47 kD polypeptide has been identified that binds ATP. A comparison of the
sensitivity of the kinase activity and the 47 kDa polypeptide labelling to
inhibitors indicate that the 47 kDa polypeptide is likely to represent the
major protein kinase activity of the virus. The virus associated protein kinase
phosphorylates the synthetic peptide RREEETEEE, a peptide substrate for casein
kinase II. Antiserum directed against casein kinase II revealed a positive
signal in immunoblots of purified virus. We propose that the major protein
kinase activity associated with purified virus preparations is host cell casein
kinase II.
Descriptors: influenza A virus avian enzymology, influenza
A virus enzymology, protein kinases metabolism, adenosine analogs and
derivatives, adenosine pharmacology, adenosine triphosphate analogs and
derivatives, adenosine triphosphate metabolism, adenosine triphosphate
pharmacology, allantois metabolism, amino acid sequence, calcium metabolism,
cyclic amp metabolism, electrophoresis, polyacrylamide gel, ethylmaleimide
pharmacology, guanosine triphosphate metabolism, heparin pharmacology,
immunoblotting, avian immunology, avian metabolism, influenza A virus
immunology, influenza A virus metabolism, kinetics, molecular sequence data,
photochemistry methods, protein kinases chemistry, protein kinases immunology.
Tumova, B. and D. Fedova (1968). Propagation of
type A Myxovirus influenzae in diploid cell strain WI-38. I. Adaptation
experiments with strains of human and animal origin. Acta Virologica
12(4): 324-30. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: diploidy, orthomyxoviridae growth and
development, tissue culture, virus cultivation, chick embryo, hemagglutination
tests, influenza A virus avian growth and development, orthomyxoviridae
immunology, orthomyxoviridae pathogenicity, virulence.
Tumova, B. and H.G. Pereira (1965). Genetic
interaction between influenza A viruses of human and animal origin. Virology
27(3): 253-61. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: orthomyxoviridae, ultraviolet rays, antigens,
birds, complement fixation tests, genetics, hemagglutination inhibition tests,
horses, influenza, influenza A virus avian, radiation effects, swine.
Tumova, B., E. Svandova, and G. Stumpa (1968). Findings
of antibodies to animal influenza viruses in human sera and their significance
for the study of interviral antigenic relationship. Journal of Hygiene,
Epidemiology, Microbiology, and Immunology 12(3): 284-95. ISSN: 0022-1732.
NAL
Call Number: 448.8 J826
Descriptors: antibodies analysis, antigens analysis,
orthomyxoviridae immunology, adult, age factors, aged, antigen antibody
reactions, depression, chemical, ducks, hemagglutination inhibition tests,
influenza A virus avian immunology, middle aged, neutralization tests, periodic
acid pharmacology, potassium pharmacology, turkeys.
Tumpey, T.M., M. Renshaw, J.D. Clements, and J.M.
Katz (2001). Mucosal delivery of inactivated influenza vaccine induces
B-cell-dependent heterosubtypic cross-protection against lethal influenza A
H5N1 virus infection. Journal of Virology 75(11): 5141-50. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Influenza vaccines that induce greater
cross-reactive or heterosubtypic immunity (Het-I) may overcome limitations in
vaccine efficacy imposed by the antigenic variability of influenza A viruses.
We have compared mucosal versus traditional parenteral administration of
inactivated influenza vaccine for the ability to induce Het-I in BALB/c mice
and evaluated a modified Escherichia coli heat-labile enterotoxin
adjuvant, LT(R192G), for augmentation of Het-I. Mice that received three
intranasal (i.n.) immunizations of H3N2 vaccine in the presence of LT(R192G)
were completely protected against lethal challenge with a highly pathogenic
human H5N1 virus and had nasal and lung viral titers that were at least
2,500-fold lower than those of control mice receiving LT(R192G) alone. In
contrast, mice that received three vaccinations of H3N2 vaccine subcutaneously
in the presence or absence of LT(R192G) or incomplete Freund's adjuvant were
not protected against lethal challenge and had no significant reductions in
tissue virus titers observed on day 5 post-H5N1 virus challenge. Mice that were
i.n. administered H3N2 vaccine alone, without LT(R192G), displayed partial
protection against heterosubtypic challenge. The immune mediators of Het-I were
investigated. The functional role of B and CD8+ T cells in Het-I were evaluated
by using gene-targeted B-cell (IgH-6(-/-))- or beta2-microglobulin
(beta2m(-/-))-deficient mice, respectively. beta2m(-/-) but not IgH-6(-/-)
vaccinated mice were protected by Het-I and survived a lethal infection with
H5N1, suggesting that B cells, but not CD8+ T cells, were vital for protection
of mice against heterosubtypic challenge. Nevertheless, CD8+ T cells
contributed to viral clearance in the lungs and brain tissues of
heterotypically immune mice. Mucosal but not parenteral vaccination induced
subtype cross-reactive lung immunoglobulin G (IgG), IgA, and serum IgG
anti-hemagglutinin antibodies, suggesting the presence of a common
cross-reactive epitope in the hemagglutinins of H3 and H5. These results
suggest a strategy of mucosal vaccination that stimulates cross-protection
against multiple influenza virus subtypes, including viruses with pandemic
potential.
Descriptors: B lymphocytes immunology, fowl plague
prevention and control, influenza A virus avian immunology, influenza vaccine
immunology, adjuvants, immunologic administration and dosage, administration,
cutaneous, administration, intranasal, antibodies, viral analysis, antibodies,
viral blood, bacterial toxins administration and dosage, CD8 positive T
lymphocytes immunology, cross reactions, enterotoxins administration and
dosage, Escherichia coli immunology, fowl plague immunology, fowl plague
virology, Freund's adjuvant administration and dosage, hemagglutinins viral
immunology, immunoglobulin A analysis, immunoglobulin A blood, immunoglobulin G
analysis, immunoglobulin G blood, influenza A virus avian isolation and
purification, lung immunology, lung virology, mice inbred BALB c, mice, inbred
c57bl, mice, knockout, species specificity, vaccines, inactivated immunology.
Ullah, S., M. Ashfaque, S.U. Rahman, M. Akhtar, and
A. Rehman (2004). Newcastle disease virus in the intestinal contents of
broilers and layers. Pakistan Veterinary Journal 24(1): 28-30. ISSN: 0253-8318.
NAL
Call Number: SF604.P32
Abstract: Two hundred intestines pieces (100 each of
broilers and layers) of about 8 cm length were collected from the poultry sale
shops in Faisalabad city, Pakistan. These pieces were opened, scratched and
vigorously shaken into sterilized normal saline, the suspension was centrifuged
and supernatants were subjected to spot haemagglutination with 2% chicken
RBC's. Out of 200 samples, 95% samples of layers and 75% of the broilers showed
positive spot haemagglutination. Micro haemagglutination inhibition with
Newcastle disease (ND) antiserum revealed 85 and 66 samples positive in layers
and broilers, respectively. A total of 10% samples of the layers and 9% of the
broilers were not inhibited by ND antiserum suggesting other HA viruses. A
total of 20 samples were used to isolate the virus in embryonated eggs
(allantoic route). These isolates were confirmed as NDV by haemagglutination
inhibition test. Five isolates were tested for intracerebral pathogenicity
index (ICPI) in day old chicks. The ICPI values obtained were 0.28, 0.31, 0.37,
0.38 and 0.46. The isolates were found to be lentogenic.
Descriptors: broiler chickens, layer chickens, intestines,
Newcastle disease virus, identification, hemagglutination tests, agglutination
tests, Galliformes, immunological techniques.
Urakawa, S. (1977). Studies on the antigenic
variants of avian influenza A virus (A/tern/South Africa/61, Hav 5 Nav 2)
obtained in the presence of homologous antiserum. Japanese Journal of
Veterinary Research 25(1-2): 33.
ISSN: 0047-1917.
NAL
Call Number: 41.8 V6446
Descriptors: avian influenza virus, antiserum, antigenc
varients, studies.
Uzunova, A. and R. Petrova (1976). Prouchvane
reproduktsiiata na rezistenten spriamo amantadina variant na virusa na gripa i
rekombinant, poluchen mezhdu nego i virusa na klasicheskata chuma po ptitsite,
v kletuchni kulturi [Studies of the reproduction of amantadine-resistant
variant of the influenza virus and its recombination with the classical fowl
pest virus in cell cultures]. Acta Microbiologica, Virologica Et
Immunologica 4: 98-104. ISSN: 0324-0452.
NAL
Call Number: QR1.A3
Descriptors: influenza A virus avian growth and
development, orthomyxoviridae growth and development, recombination, genetic,
virus replication, amantadine pharmacology, cell line, cytopathogenic effect,
viral, drug resistance, microbial, orthomyxoviridae drug effects, variation
genetics.
Vallbracht, A., B. Flehmig, and H.J. Gerth (1979). Influenza
virus: appearance of high mouse-neurovirulent recombinants. InterVirology
11(1): 16-22. ISSN: 0300-5526.
NAL
Call Number: QR355.I5
Abstract: Recombinants from two influenza A strains
that lacked mouse neurovirulence were tested, along with their parent strains,
for mouse neurovirulence and for the ability to propagate in dissociated mouse
embryo brain cells. The parents used were (i) strain A/Rostock/34 (FPV)
(Hav1N1), with a high chicken neurovirulence, and (ii) the mouse-lung-adapted
human strain Engl/1/61 (H2N2), lacking neurovirulence. In some of the
recombinants high mouse neurovirulence could be detected after intracerebral
inoculation of low virus doses. There was neither a correlation between surface
antigen and neurovirulence nor between neurovirulence and mouse lung virulence
in our system, although neurovirulence was only found in strains with Hav1
hemagglutinin. There was an association between replication in mouse embryo
brain cells in culture and high mouse neurovirulence.
Descriptors: influenza A virus avian pathogenicity, human
pathogenicity, recombination, genetic, brain microbiology, avian genetics, avian
growth and development, human genetics, human growth and development, mice,
virulence, virus replication.
Vallbracht, A., C. Scholtissek, B. Flehmig, and H.J.
Gerth (1980). Recombination of influenza A strains with fowl plague virus
can change pneumotropism for mice to a generalized infection with involvement
of the central nervous system. Virology 107(2): 452-60. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus avian genetics, human
genetics, recombination, genetic, administration, intranasal, brain
microbiology, cultured cells, genes viral, human pathogenicity, injections,
intraperitoneal, mice, orthomyxoviridae infections etiology, orthomyxoviridae
infections pathology, pneumonia microbiology, trypsin pharmacology, viremia,
virulence, virus replication drug effects.
Van Campen, H. (1990). Tissue tropism of a
virulent avian influenza A virus in chickens. Dissertation Abstracts
International, B 50(12): 5502. ISSN:
0419-4217.
NAL
Call Number: Z5055.U49D53
Descriptors: vian influenza virus, virulence, Gallus
gallus, chickens, pathogenesis.
Van Campen, H., B.C. Easterday, and V.S. Hinshaw
(1989). Destruction of lymphocytes by a virulent avian influenza A virus.
Journal of General Virology 70(Pt. 2): 467-72. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Infection of chickens by a virulent avian
influenza A virus, A/turkey/Ont/7732/66 (H5N9), was associated with a severe
lymphopenia. High titres of infectious virus were found in lymphoid tissues
early in infection and were accompanied by severe damage to the lymphocyte
populations as demonstrated by histopathological examination. Non-lymphoid cell
populations in these tissues were unaffected, as were other organs examined.
The viral nucleoprotein was localized by immunoperoxidase staining to
lymphocytes in affected tissues early in infection.
Descriptors: influenza A virus avian pathogenicity,
lymphopenia veterinary, chickens, fowl plague microbiology, fowl plague
pathology, avian isolation and purification, lymphocytes microbiology,
lymphocytes pathology, lymphoid tissue microbiology, lymphoid tissue pathology,
lymphopenia microbiology, lymphopenia pathology, necrosis, time factors,
virulence.
Van Campen, H., B.C. Easterday, and V.S. Hinshaw
(1989). Virulent avian influenza A viruses: their effect on avian
lymphocytes and macrophages in vivo and in vitro. Journal of General
Virology 70(Pt. 11): 2887-95. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: To investigate the pathogenesis of virulent
avian influenza A viruses, the effect of A/turkey/Ont/7732/66 (H5N9) (Ty/Ont),
A/tern/South Africa/1961 (H5N3) (Tern/S.A.) and A/chicken/Pennsylvania/1370/83
(H5N2) (Ck/Penn) on avian lymphoid cell populations was examined in vivo.
Previous studies have shown that infection of chickens with Ty/Ont resulted in
the extensive destruction of lymphoid tissues. In this study, other virulent
avian H5 influenza viruses, Tern/S.A. or Ck/Penn, had little or no effect on
lymphoid tissues of infected chickens. Therefore the effect of Ty/Ont on
lymphoid tissue is a specific activity of this virus only and not of other
virulent avian H5 influenza strains. To examine the role of viral replication
in the destruction of lymphocytes, in vitro cultures of avian macrophages and
lymphocytes were inoculated with Ty/Ont. Macrophages supported the synthesis of
viral proteins whereas lymphocytes produced small, but detectable amounts of
viral protein; however, infectious virus was not produced by either cell type.
Furthermore inoculation of chicken spleen cells with Ty/Ont in vivo and in
vitro had a profound effect on the proliferative response of lymphocytes to
concanavalin A. These results suggest that Ty/Ont infects macrophages as well
as lymphocytes in the chicken, and the effects of the virus on both cell types
may well contribute to lymphoid necrosis.
Descriptors: influenza veterinary, influenza A virus avian
immunology, lymphocytes immunology, macrophages immunology, poultry diseases
immunology, chickens microbiology, immunoenzyme techniques, influenza
immunology, avian pathogenicity, lymphocyte activation, lymphocytes
microbiology, macrophages microbiology, poultry diseases microbiology, RNA
viral biosynthesis, viral proteins biosynthesis, virus replication.
van der Goot, J.A., M.C.M. de Jong, G. Koch, and M.
van Boven (2003). Comparison of the transmission characteristics of low and
high pathogenicity avian influenza A virus (H5N2). Epidemiology and
Infection 131(2): 1003-1013. ISSN:
0950-2688.
NAL
Call Number: RA651.A1E74
Descriptors: influenza virus A and B, characteristics,
comparisons, disease transmission, pathogenicity.
van Eijk, M., M.R. White, J.J. Batenburg, A.B.
Vaandrager, L.M. van Golde, H.P. Haagsman, and K.L. Hartshorn (2004). Interactions
of influenza A virus with sialic acids present on porcine surfactant protein D.
American Journal of Respiratory Cell and Molecular Biology 30(6):
871-9. ISSN: 1044-1549.
Abstract: Pigs can be infected with both human and
avian influenza A virus (IAV) strains and are therefore considered to be
important intermediates in the emergence of new IAV strains due to mixing of
viral genes derived from human, avian, or porcine influenza viruses. These
reassortant strains may have potential to cause pandemic influenza outbreaks in
humans. The innate immune response against IAV plays a significant role in
containment of IAV in the airways. We studied the interactions of IAV with
porcine surfactant protein D (pSP-D), an important component of this first line
defense system. Hemagglutination inhibition analysis shows that the distinct
interactions of pSP-D with IAV mediated by the N-linked carbohydrate moiety in
the carbohydrate recognition domain of pSP-D depend on the terminal sialic
acids (SAs) present on this carbohydrate. Analysis by both lectin staining and
by cleavage with linkage-specific sialidases shows that the carbohydrate of
pSP-D is exclusively sialylated with alpha(2,6)-linked SAs, in contrast to
surfactant protein A, which contains both alpha(2,3)- and alpha(2,6)-linked SAs
on its N-linked carbohydrate. Enzymatic modification of the SA-linkages present
on pSP-D demonstrates that the type of SA-linkage is important for its
hemagglutination-inhibitory activity, and correlates with receptor-binding
specificity of the IAV strains. The SAs present on pSP-D appear especially
important for interactions with poorly glycosylated IAV strains. It remains to
be elucidated to what extent the unique sialylation profile of pSP-D is
involved in host range control of IAV in pigs, and whether it facilitates
adaptation of avian or human IAV strains that can contribute to the production
of reassortant strains in pigs.
Descriptors: influenza A virus metabolism, pulmonary
surfactant associated protein D chemistry, sialic acids metabolism, swine,
carbohydrate conformation, carbohydrate sequence, chickens, hemagglutination
inhibition tests, molecular sequence data, molecular structure, neuraminidase
metabolism, pulmonary surfactant associated protein A chemistry, pulmonary
surfactant associated protein A metabolism, pulmonary surfactant associated
protein D metabolism, pulmonary surfactants chemistry, receptors, cell surface,
sialic acids chemistry.
van Meer, G., J. Davoust, and K. Simons (1985). Parameters
affecting low-pH-mediated fusion of liposomes with the plasma membrane of cells
infected with influenza virus. Biochemistry 24(14): 3593-602. ISSN: 0006-2960.
NAL
Call Number: 381 B523
Abstract: Unilamellar liposomes can be fused at low pH
with the plasma membrane of cells that express the hemagglutinin glycoprotein
of influenza virus on their surface [van Meer, G., & Simons, K. (1983) J.
Cell Biol. 97, 1365-1374]. Here, we have resolved this fusion process into two
kinetically distinct steps. The first and more rapid step converts the bound liposome
to a form that can no longer be released by neuraminidase. The second step is
the actual membrane fusion as measured by the loss of resonance energy transfer
between two liposomal fluorescent phospholipids,
N-(7-nitro-2,1,3-benzoxadiazol-4-yl)dioleoylphosphatidylethanolami ne
(N-NBD-PE) and N-(lissamine rhodamine B
sulfonyl)dioleoylphosphatidylethanolamine (N-Rh-PE). In contrast to the first
step, the rate of the second one was highly dependent on the liposomal lipid
composition and the cell type used. The replacement of 50% of the
phosphatidylcholine (PC) in egg PC-cholesterol liposomes by unsaturated
phosphatidylethanolamine (PE) species increased the rate of fusion at least
2-fold. Of the PE-containing liposomes that were associated with Madin-Darby canine
kidney (MDCK) cells after 30 s of fusion, 80% had actually fused with the
plasma membrane. Fringe pattern fluorescence photobleaching experiments showed
that after fusion a fraction of the cell-associated N-Rh-PE diffused laterally
in the plasma membrane. Without fusion, the N-Rh-PE was completely immobile.
Under optimal conditions, the mobile fractions were 65% on MDCK cells and 78%
on baby hamster kidney cells. The mobility was acquired simultaneously with the
dilution of the fluorescent phospholipids as measured from the loss of
resonance energy transfer. The mobile fraction of N-Rh-PE on the cell surface
can therefore be used as a second independent measure of actual membrane
fusion. Finally, we observed that upon fusion up to 80% of the nonexchangeable
liposome markers cholesterol [14C]oleate and glycerol tri[14C]oleate became
accessible to cellular hydrolases. The results showed that this hydrolysis
assay can also be used to monitor the second step of the fusion process.
Descriptors: cell membrane physiology, influenza A virus
avian physiology, liposomes, cell line, cell transformation, viral, cholesterol
esters metabolism, dogs, energy transfer, hamsters, hydrogen-ion concentration,
kidney, kinetics, neuraminidase, spectrometry, fluorescence.
van Meer, G. and K. Simons (1982). Viruses budding
from either the apical or the basolateral plasma membrane domain of MDCK cells
have unique phospholipid compositions. EMBO Journal 1(7):
847-52. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: Influenza virus and vesicular stomatitis
virus (VSV) obtain their lipid envelope by budding through the plasma membrane
of infected cells. When monolayers of Madin-Darby canine kidney (MDCK) cells, a
polarized epithelial cell line, are infected with fowl plague virus (FPV), an
avian influenza virus, or with VSV, new FPV buds through the apical plasma
membrane whereas VSV progeny is formed by budding through the basolateral
plasma membrane. FPV and VSV were isolated from MDCK host cells prelabeled with
[32P]orthophosphate and their phospholipid compositions were compared.
Infection was carried out at 31 degrees C to delay cytopathic effects of the
virus infection, which lead to depolarization of the cell surface. 32P-labeled
FPV was isolated from the culture medium, whereas 32P-labeled VSV was released
from below the cell monolayer by scraping the cells from the culture dish 8 h
after infection. At this time little VSV was found in the culture medium,
indicating that the cells were still polarized. The phospholipid composition of
the two viruses was distinctly different. FPV was enriched in
phosphatidylethanolamine and phosphatidylserine and VSV in phosphatidylcholine,
sphingomyelin, and phosphatidylinositol. When MDCK cells were trypsinized after
infection and replated, non-infected control cells attached to reform a
confluent monolayer within 4 h, whereas infected cells remained in suspension.
FPV and VSV could be isolated from the cells in suspension and under these
conditions the phospholipid composition of the two viruses was very similar. We
conclude that the two viruses obtain their lipids from the plasma membrane in
the same way and that the different phospholipid compositions of the viruses
from polarized cells reflect differences in the phospholipid composition of the
two plasma membrane domains.
Descriptors: influenza A virus avian physiology,
phospholipids analysis, vesicular stomatitis Indiana virus physiology, cell
line, cell membrane microbiology, dogs, avian analysis, kidney, trypsin,
vesicular stomatitis Indiana virus analysis.
Varghese, J.N., P.M. Colman, A. van Donkelaar, T.J.
Blick, A. Sahasrabudhe, and J.L. McKimm Breschkin (1997). Structural
evidence for a second sialic acid binding site in avian influenza virus
neuraminidases. Proceedings of the National Academy of Sciences of the
United States of America 94(22): 11808-12.
ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: The x-ray structure of a complex of sialic
acid (Neu5Ac) with neuraminidase N9 subtype from A/tern/Australia/G70C/75 influenza
virus at 4 degrees C has revealed the location of a second Neu5Ac binding site
on the surface of the enzyme. At 18 degrees C, only the enzyme active site
contains bound Neu5Ac. Neu5Ac binds in the second site in the chair
conformation in a similar way to which it binds to hemagglutinin. The residues
that interact with Neu5Ac at this second site are mostly conserved in avian
strains, but not in human and swine strains, indicating that it has some
as-yet-unknown biological function in birds.
Descriptors: influenza A virus avian enzymology, n
acetylneuraminic acid metabolism, neuraminidase chemistry, viral proteins
chemistry, binding sites, computer simulation, crystallography, x-ray, models,
molecular, molecular sequence data, neuraminidase metabolism, protein
conformation, sequence homology, amino acid, surface properties, viral proteins
metabolism.
Vashkova, V.V. and V.M. Zhdanov (1966). Vliianie
virusa na khromosomnye perestroiki i mitoticheskuiu aktivnost' v kletkakh
kul'tury tkani cheloveka. [Effects of virus on chromosome rearrangements and
mitotic activity in human tissue culture cells]. Voprosy Virusologii
11(1): 91-3. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian, tissue culture, cell
division, chromosome aberrations etiology, chromosome disorders, cytopathogenic
effect, viral, embryo, virus cultivation.
Veits, J., D. Lueschow, K. Kindermann, O. Werner,
J.P. Teifke, T.C. Mettenleiter, and W. Fuchs (2003). Deletion of the
non-essential UL0 gene of infectious laryngotracheitis (ILT) virus leads to
attenuation in chickens, and UL0 mutants expressing influenza virus
haemagglutinin (H7) protect against ILT and fowl plague. Journal of
General Virology 84(12): 3343-3352.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: infection, fowl plague, infectious
laryngotracheitis virus infection, immunofluorescence, immunologic techniques,
western blot, genetic techniques.
Vewy, M., M. Orlich, S. Adler, H.D. Klenk, R. Rott,
and W. Garten (1992). Hemagglutinin activation of pathogenic avian influenza
viruses of serotype H7 requires the protease recognition motif R-X-K/R-R. Virology
188(1): 408-413. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The hemagglutinin of influenza virus
A/FPV/Rostock/34 (H7) was altered at its multibasic cleavage site by
site-directed mutagenesis and assayed for proteolytic activation after
expression in CV-1 cells. The results indicated that the cellular protease
responsible for activation recognizes the tetrapeptide motif R-X-K/R-R that
must be presented in the correct sequence position. Studies on plaque variants
of influenza virus A/fowl/Victoria/75 (H7N7) showed that alteration of the
consensus sequence resulted in a loss of pathogenicity for chickens.
Descriptors: fowls, avian influenza virus, viral
hemagglutinins, proteinases, proteolysis, amino acid sequences, mutants,
clones, pathogenicity, cleavae site.
Vikhrev, N.E., A.A. Zhvirblene, E.S. Severin, S.S.
Iamnikova, and D.K. L'vov (1986). Nekotorye osobennosti prigotovleniia
immunofermentnykh kon"iugatov na osnove monoklonal'nykh antitel.
[Characteristics of the preparation of monoclonal antibody-based immunoenzyme
conjugates]. Voprosy Virusologii 31(4): 507-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antibodies, monoclonal isolation and
purification, immunoenzyme techniques, antibodies, monoclonal analysis,
antibody specificity, chick embryo, hybridomas immunology, influenza A virus avian immunology,
isoelectric focusing, mice, rabbits.
Vlasov, V.V., V.V. Gorn, N.I.U. Nomokonova, T.N.
Fokina, and L.V. Iurchenko (1991). Podavlenie transliatsii in vitro mRNK
belka M1 virusa grippa s pomoshch'iu antismyslovykh oligonukleotidov.
[Suppression of translation in vitro of the mRNA of the M1 protein of influenza
virus using antisense oligonucleotides]. Molekuliarnaia Biologiia
25(5): 1332-7. ISSN: 0026-8984.
NAL
Call Number: QH506.A1M62
Abstract: Effect of antisense oligonucleotides on the
in vitro translation of the influenza virus M1 protein mRNA was investigated.
The most efficient arrest of mRNA translation was achieved by simultaneous
action of two or three oligonucleotides (14-16-mers) complementary to the
juxtaposed sequences in the 5'-terminus of the molecule around and upstream of
the initiation codon.
Descriptors: RNA, messenger genetics, RNA viral genetics,
translation, genetic drug effects, viral matrix proteins genetics, autoradiography,
base sequence, electrophoresis, polyacrylamide gel, influenza A virus avian
metabolism, molecular sequence data, oligonucleotides, antisense pharmacology,
rabbits.
Vogel, U., M. Kunerl, and C. Scholtissek (1994). Influenza
A virus late mRNAs are specifically retained in the nucleus in the presence of
a methyltransferase or a protein kinase inhibitor. Virology 198(1):
227-33. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The synthesis of influenza A virus RNA and
proteins represents a highly regulated process whereby variable amounts of
early and late viral RNAs and proteins may be produced. This regulation is
upset by the presence of the methyltransferase inhibitor 3-deazaadenosine
(3DA-Ado) or the protein kinase inhibitor H7, resulting in complete or partial
inhibition of synthesis of late proteins but normal production of early
proteins. Although the total yield of viral mRNAs is somewhat reduced by
treatment with 3DA-Ado, the mRNAs that are produced can still be translated in
vitro. Both 3DA-Ado and H7 interfere specifically with the transport of the
late viral mRNAs from the nucleus to the cytoplasm, but do not affect transport
of early mRNA. From these results we conclude that during influenza virus
replication, posttranscriptional regulation takes place on the level of mRNA
transport. Since hemagglutinin mRNA migrates to the cytoplasm in the presence
of 3DA-Ado plus cycloheximide, we assume that a viral protein is involved in
the regulation mechanism.
Descriptors: cell nucleus metabolism, influenza A virus
avian genetics, methyltransferases antagonists and inhibitors, protein kinases
antagonists and inhibitors, RNA, messenger metabolism, RNA viral metabolism, 1
5 isoquinolinesulfonyl 2 methylpiperazine, biological transport drug effects,
cell nucleus drug effects, chick embryo, avian enzymology, isoquinolines
pharmacology, piperazines pharmacology, RNA, messenger drug effects, RNA viral drug effects, translation, genetic
drug effects, tubercidin pharmacology.
Vogel, U. and C. Scholtissek (1995). Inhibition of
the intracellular transport of influenza viral RNA by actinomycin D. Archives
of Virology 140(10): 1715-23. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: In primary chicken embryo cells infected with
fowl plague virus addition of actinomycin D at defined times during the
infection cycle has different consequences on viral replication. If actinomycin
D is added immediately after infection with a concentration, which inhibits
viral RNA synthesis only partially, it interferes with the nucleo-cytoplasmic
transport of all viral RNA species (mRNA and vRNA) so far tested. If
actinomycin D is present during infection (adsorption, penetration and
uncoating) no viral RNA is synthesized, and the nucleocapsid of the infecting
virus does not reach the nucleus, as shown by fluorescent antibodies. Therefore
the primary effect of actinomycin D on influenza virus replication is on the
transport of the incoming vRNPs from the cytoplasm to the cell nucleus, which
is the cell compartment where transcription takes place.
Descriptors: dactinomycin pharmacology, hemagglutinins
viral genetics, influenza A virus avian genetics, RNA viral metabolism,
biological transport drug effects, capsid metabolism, cell compartmentation,
cell nucleus metabolism, cultured cells, chick embryo, cytoplasm metabolism,
nucleoproteins metabolism, RNA, heterogeneous nuclear metabolism, RNA,
messenger metabolism, tubercidin pharmacology, viral proteins biosynthesis,
virus replication drug effects.
von Hoyningen Huene, V. and C. Scholtissek (1983). Low
genetic mixing between avian influenza viruses of different geographic regions.
Archives of Virology 76(1): 63-7.
ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The degree of genetic relatedness of vRNA
segments 1, 2, and 3 of avian influenza A viruses was investigated by molecular
hybridization. The results indicate that avian influenza A viruses isolated
within a given geographic region are genetically more closely related than
strains from different regions, irrespective of the year of isolation and the
species from which the virus was isolated. Studies on RNA segment 4 of viruses
within the subtype H7 isolated in different regions gave similar results. Thus
the genetic composition of avian influenza A viruses appears to be maintained
to a rather high degree within a given geographic region and the intrusion of
genes from "foreign regions" appears to be taking place with low
frequency. The results are discussed with respect to the worldwide distribution
of influenza virus genes by migrating birds.
Descriptors: genes viral, influenza A virus avian
genetics, RNA viral genetics, recombination, genetic, Europe, Great Britain,
avian classification, North America, nucleic acid hybridization.
von Nicolai, H., R. Drzeniek, and F. Zilliken (1971).
Kinetische und chemische Untersuchungen uber den Abbau von
Di-N-acetylneuraminosyl-lacto-N-tetraose durch Neuraminidasen von Myxoviren und
Vibrio cholerae. [Kinetic and chemical experiments on the decay of
di-N-acetylneuraminosyl-lacto-N-tetraose by neuraminidases of myxoviruses and Vibrio
cholerae]. Zeitschrift Fur Naturforschung. Teil B Chemie, Biochemie,
Biophysik, Biologie 26(10): 1049-51.
ISSN: 0044-3174.
NAL
Call Number: QH301.Z4
Descriptors: influenza A virus avian enzymology,
neuraminic acids metabolism, neuraminidase metabolism, Newcastle disease virus
enzymology, oligosaccharides metabolism, vibrio enzymology, chromatography,
paper, galactose metabolism, glucosamine metabolism, milk, human,
oligosaccharides isolation and purification, Vibrio cholerae enzymology.
Vorontsova, T.V., A.B. Germanov, and M.I. Sikolov
(1971). Induktsiia S-mutatsii u virusa istinnoi chumy ptits s pomoshch'iu
etilenimina. [Induction of S-mutations in fowl plague virus using ethylene
imine]. Voprosy Virusologii 16(4): 416-21. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian drug effects,
mutagens pharmacology, ethylenes pharmacology, ethylenes toxicity, genetics,
microbial, imines pharmacology, imines toxicity, mathematics.
Votiakov, V.I., E.I. Boreko, and L.K. Zaporozhets
(1984). Izuchenie tkanevoi reaktsii i infektsionnosti virusa grippa pri
razmnozhenii v kul'ture tkani v prisutstvii remantadina. [Tissue reaction and
influenza virus infectiousness during multiplication in tissue culture in the
presence of remantadine]. Voprosy Virusologii 29(4): 468-73. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The effect of remantadine in tissue culture
of primary chick embryo fibroblasts (CEF) infected with classical fowl plague
virus (FRV) was found to be dual. On the one hand, in low concentrations
remantadine effectively inhibited in CEF reproduction of the virus sensitive to
it. On the other, in high (subtoxic) concentrations in CEF infected with either
sensitive or remantadine-resistant FPV variants it induced virus reproduction.
The latter became noninfectious for normal CEF but retained its capacity for
multiplication in cells treated with high concentrations of remantadine.
Descriptors: adamantane analogs and derivatives, influenza
A virus avian pathogenicity, rimantadine pharmacology, virus replication drug
effects, chick embryo, cytopathogenic effect, viral drug effects, dose response
relationship, drug, avian drug effects, plaque assay, virus cultivation.
Wagner, R., D. Heuer, T. Wolff, A. Herwig, and H.D.
Klenk (2002). N-Glycans attached to the stem domain of haemagglutinin
efficiently regulate influenza A virus replication. Journal of General
Virology 83(Pt. 3): 601-9. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The haemagglutinin (HA) protein of fowl
plague virus A/FPV/Rostock/34 (H7N1) contains three N-linked oligosaccharide side
chains in its stem domain. These stem glycans, which are attached to the Asn
residues at positions 12, 28 and 478, are highly conserved throughout all HA
protein sequences analysed to date. In a previous study, in which mutant HA
proteins lacking individual stem glycosylation sites had been expressed from an
SV-40 vector, it was shown that these glycans maintain the HA protein in the
metastable form required for fusion activity. In the present study, the
functional role of the stem N-glycans for virus replication was investigated
using recombinant influenza viruses generated by an RNA polymerase I-based
system. Studies in Madin-Darby canine kidney cells and embryonated chickens'
eggs revealed that the N-glycan at Asn(12) is crucial for virus replication. In
both culture systems, growth of virus lacking this glycan (mutant cg1) was
completely blocked at 37 degrees C and inhibited at 33 degrees C. Loss of the
glycan from Asn(478) (mutant cg3) caused less striking, but still measurable,
effects. Interestingly, it was not possible to generate mutant viruses
containing the HA protein lacking the N-glycan at Asn(28). It is concluded from
this that the N-glycan at Asn(28) is indispensable for the formation of
replication-competent influenza viruses. When compared to viruses containing
wild-type HA protein, mutants cg1 and cg3 showed a significantly decreased pH
stability. Taken together, these data show that the HA stem glycans are potent
regulators of influenza virus replication.
Descriptors: hemagglutinin glycoproteins, influenza virus
chemistry, hemagglutinin glycoproteins, influenza virus metabolism, influenza A
virus avian chemistry, avian physiology, polysaccharides metabolism, virus
replication, asparagine metabolism, cell line, chick embryo, dogs, flow cytometry,
genetic engineering, glycosylation, hemagglutinin glycoproteins, influenza
virus genetics, hydrogen-ion concentration, avian genetics, models, molecular,
mutation, oligosaccharides metabolism, protein conformation, RNA genetics, temperature.
Wagner, R., S. Liedtke, E. Kretzschmar, H. Geyer, R.
Geyer, and H.D. Klenk (1996). Elongation of the N-glycans of fowl plague
virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by
coexpression of human beta 1,2-N-acetylglucosaminyltransferase I. Glycobiology
6(2): 165-75. ISSN: 0959-6658.
NAL
Call Number: QP552.G59G593
Abstract: Spodoptera frugiperda (Sf9)-cells
differ markedly in their protein glycosylation capacities from vertebrate cells
in that they are not able to generate complex type oligosaccharide side chains.
In order to improve the oligosaccharide processing properties of these cells we
have used baculovirus vectors for expression of human (beta
1,2-N-acetylglucosaminyltransferase I (hGNT-I), the enzyme catalysing the
crucial step in the pathway leading to complex type N-glycans in vertebrate
cells. One vector (Bac/GNT) was designed to express unmodified GNT-I protein,
the second vector (Bac/tagGNT) to express GNT-I protein with a tag epitope
fused to its N-terminus. In Sf9-cells infected with Bac/tagGNT-virus a protein
of about 50 kDa representing hGNT-I was detected with an antiserum directed
against the tag epitope. HGNT-I activity was increased at least threefold in
lysates of infected cells when N-acetylglucosamine (GlcNAc)-free ovalbumine was
used as substrate. To monitor hGNT-I activity in intact Sf9-cells, the
glycosylation of coexpressed fowl plague virus hemagglutinin (HA) was
investigated employing a galactosylation assay and chromatographic analysis of
isolated HA N-glycans. Coexpression of hGNT-I resulted in an at least fourfold
increase of HA carrying terminal GlcNAc-residues. The only structure detectable
in this fraction was GlcNAcMan3GlcNAc2. These results show that hGNT-I is
functionally active in Sf9-cells and that the N-glycans of proteins expressed
in the baculovirus/insect cell system are elongated by coexpression of
glycosyltransferases of vertebrate origin. Complete complex type
oligosaccharide side chains were not observed when hGNT-I was overexpressed,
thus supporting the concept that Sf9-cells do not contain glycosyltransferases
acting after hGNT-I.
Descriptors: hemagglutinins viral biosynthesis, influenza
A virus avian genetics, N-acetylglucosaminyltransferases genetics,
polysaccharides biosynthesis, base sequence, carbohydrate conformation,
carbohydrate sequence, cell line, cloning, molecular, DNA primers,
hemagglutinins viral genetics, avian metabolism, molecular sequence data,
N-acetylglucosaminyltransferases metabolism, recombinant proteins, Spodoptera.
Wagner, R., T. Wolff, A. Herwig, S. Pleschka, and
H.D. Klenk (2000). Interdependence of hemagglutinin glycosylation and
neuraminidase as regulators of influenza virus growth: a study by reverse
genetics. Journal of Virology 74(14): 6316-23. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The hemagglutinin (HA) of fowl plague virus
A/FPV/Rostock/34 (H7N1) carries two N-linked oligosaccharides attached to
Asn123 and Asn149 in close vicinity to the receptor-binding pocket. In previous
studies in which HA mutants lacking either one (mutants G1 and G2) or both
(mutant G1,2) glycosylation sites had been expressed from a simian virus 40
vector, we showed that these glycans regulate receptor binding affinity (M.
Ohuchi, R. Ohuchi, A. Feldmann, and H. D. Klenk, J. Virol. 71:8377-8384, 1997).
We have now investigated the effect of these mutations on virus growth using
recombinant viruses generated by an RNA polymerase I-based reverse genetics
system. Two reassortants of influenza virus strain A/WSN/33 were used as helper
viruses to obtain two series of HA mutant viruses differing only in the
neuraminidase (NA). Studies using N1 NA viruses revealed that loss of the
oligosaccharide from Asn149 (mutant G2) or loss of both oligosaccharides
(mutant G1,2) has a pronounced effect on virus growth in MDCK cells. Growth of
virus lacking both oligosaccharides from infected cells was retarded, and virus
yields in the medium were decreased about 20-fold. Likewise, there was a
reduction in plaque size that was distinct with G1,2 and less pronounced with
G2. These effects could be attributed to a highly impaired release of mutant
progeny viruses from host cells. In contrast, with recombinant viruses
containing N2 NA, these restrictions were much less apparent. N1 recombinants showed
lower neuraminidase activity than N2 recombinants, indicating that N2 NA is
able to partly overrule the high-affinity binding of mutant HA to the receptor.
These results demonstrate that N-glycans flanking the receptor-binding site of
the HA molecule are potent regulators of influenza virus growth, with the
glycan at Asn149 being dominant and that at Asn123 being less effective. In
addition, we show here that HA and NA activities need to be highly balanced in
order to allow productive influenza virus infection.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian growth and development, neuraminidase
genetics, cattle, cell line, chickens, erythrocytes virology, glycosylation,
hemagglutinin glycoproteins, influenza virus metabolism, avian genetics, avian
metabolism, mutagenesis, site directed, neuraminidase metabolism, plaque assay,
receptors, virus genetics, receptors, virus metabolism, recombination, genetic.
Walker, J.A. and Y. Kawaoka (1993). Importance of
conserved amino acids at the cleavage site of the haemagglutinin of a virulent
avian influenza A virus. Journal of General Virology 74(Pt. 2):
311-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The virulence of avian influenza A viruses
depends on the cleavability of the haemagglutinin (HA) by an intracellular
protease at multiple basic amino acids. Although previous studies have
demonstrated the importance of these amino acids for processing by the cellular
protease, with emphasis on conserved residues near the cleavage site, the
minimal requirements for cleavage remain unknown. By expressing site-specific
mutants of the HA of a virulent avian influenza virus, A/turkey/Ireland/1378/85
(H5N8), in the simian virus 40 system and testing for their cleavability by an
endogenous protease in CV-1 cells, and their fusion activity in a polykaryon
formation assay, we were able to show that glycine at the amino terminus of HA2
is not essential for cleavage and that maximal cleavage requires at least five
basic residues at the cleavage site, when carbohydrate is nearby. Moreover, we
confirmed, that a conserved proline upstream of the cleavage site is not
essential for HA cleavage or fusion activity, and that lysine replacement of
the carboxyl-terminal arginine of HA1 abolishes cleavability. These findings
should help identify the proteases responsible for intracellular cleavage of
the HA of virulent avian influenza viruses.
Descriptors: conserved sequence genetics, hemagglutinins
viral chemistry, influenza A virus avian chemistry, amino acid sequence,
conserved sequence physiology, hemagglutinins viral genetics, hemagglutinins
viral metabolism, avian metabolism, avian pathogenicity, molecular sequence
data, mutation, virulence genetics.
Walker, J.A., S.S. Molloy, G. Thomas, T. Sakaguchi,
T. Yoshida, T.M. Chambers, and Y. Kawaoka (1994). Sequence specificity of
furin, a proprotein-processing endoprotease, for the hemagglutinin of a
virulent avian influenza virus. Journal of Virology 68(2): 1213-8. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The virulence of avian influenza viruses
correlates with the sensitivity of their hemagglutinin (HA) to cellular
proteases. Furin, a proprotein-processing subtilisin-related endoprotease, is a
leading candidate for the enzyme that cleaves the HA of virulent avian viruses.
We therefore compared the specificity of furin with those of proteases in a
variety of cultured cells and in a rat Golgi fraction, using the HA cleavage
mutants of a virulent avian influenza virus, A/Turkey/Ireland/1378/85 (H5N8).
The results indicated similar sequence specificities among the endoproteases
when purified furin was used. In experiments with the vaccinia virus expression
system, overexpressed furin cleaved mutant HAs that were not recognized by the
endogenous proteases, resulting in an apparent broader specificity of furin.
These findings authenticate the proposed role of furin as an HA-activating
protease in vivo and caution against the use of expression vectors to study
protease sequence specificity.
Descriptors: hemagglutinins viral metabolism, influenza A
virus avian metabolism, protein precursors metabolism, protein processing, post
translational, subtilisins metabolism, amino acid sequence, cultured cells, Furin,
Golgi apparatus enzymology, hemagglutinin glycoproteins, influenza virus, liver
enzymology, molecular sequence data, rats, recombinant proteins biosynthesis,
substrate specificity, subtilisins genetics.
Walker, J.A., T. Sakaguchi, Y. Matsuda, T. Yoshida,
and Y. Kawaoka (1992). Location and character of the cellular enzyme that
cleaves the hemagglutinin of a virulent avian influenza virus. Virology
190(1): 278-87. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: H.-D. Klenk, W. Garten, and R. Rott (1984,
EMBO J. 3, 2911-2915) have reported that hemagglutinin (HA) cleavage of
virulent avian influenza viruses occurs in later steps of its intracellular
transport and that the cleavage enzyme is calcium dependent and has a neutral
pH optimum. The precise intracellular location of the HA cleavage, however, has
never been established. Furthermore, because Klenk et al. used the whole cell
lysate to examine the cleavage activity and the amino acid sequencing of the
cleaved product was not done, the identity of the cleavage enzyme remains to be
established. We therefore attempted to systematically characterize the HA
cleavage of the virulent avian virus A/tern/South Africa/61 (H5N3). Using an
inhibitor of glycoprotein transport (Brefeldin A) and temporal markers of
glycoprotein processing, we found that the endoprotease responsible for the HA
cleavage acts after the acquisition of endo-N-acetylglucosaminidase H
resistance but before the addition of galactose to the molecule, and thus is
located in the medial and/or trans Golgi. This observation was directly
confirmed by in vitro experiments using rat liver subcellular membrane
fractions containing Golgi complex. A fraction rich in galactosyltransferase (a
trans Golgi marker) demonstrated the highest HA cleavage activity. The
endoprotease in this fraction cleaved only the HA of the virulent avian
influenza virus but not that of an avirulent virus. Through amino-terminal
sequencing of the HA2 produced by digestion with the endoprotease in the rat
Golgi fraction, we established that HA cleavage by the protease occurs at the
authentic site. Further studies using the rat Golgi fraction showed that the HA
cleavage enzyme is calcium dependent and has a low pH (6.0) optimum. Thus, the pH
optimum of the enzyme in the Golgi fraction differs from that in whole cell
lysate reported previously.
Descriptors: endopeptidases metabolism, hemagglutinins
viral metabolism, influenza A virus avian metabolism, biological transport,
cattle, cell line, cell membrane enzymology, electrophoresis, polyacrylamide
gel, glycosylation, Golgi apparatus enzymology, hydrogen-ion concentration,
avian physiology, liver enzymology, monensin pharmacology, protein precursors
metabolism, rats, inbred strains, virus replication.
Wang, C., K. Takeuchi, L.H. Pinto, and R.A. Lamb
(1993). Ion channel activity of influenza A virus M2 protein:
characterization of the amantadine block. Journal of Virology 67(9):
5585-94. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The influenza A virus M2 integral membrane
protein has ion channel activity which can be blocked by the antiviral drug
amantadine. The M2 protein transmembrane domain is highly conserved in amino
acid sequence for all the human, swine, equine, and avian strains of influenza
A virus, and thus, known amino acid differences could lead to altered
properties of the M2 ion channel. We have expressed in oocytes of Xenopus
laevis the M2 protein of human influenza virus A/Udorn/72 and the avian
virus A/chicken/Germany/34 (fowl plague virus, Rostock) and derivatives of the
Rostock ion channel altered in the presumed pore region. The pH of activation
of the M2 ion channels and amantadine block of the M2 ion channels were
investigated. The channels were found to be activated by pH in a similar manner
but differed in their apparent Kis for amantadine block.
Descriptors: amantadine pharmacology, influenza A virus
avian physiology, human physiology, ion channels drug effects, viral matrix
proteins metabolism, amino acid sequence, fluorescent antibody technique,
hydrogen-ion concentration, kinetics, mathematics, membrane potentials drug
effects, models, biological, molecular sequence data, mutagenesis, site
directed, oocytes drug effects, oocytes physiology, RNA, messenger metabolism,
viral matrix proteins biosynthesis, viral matrix proteins drug effects, Xenopus
laevis.
Wang ChingWen
and Wang ChingHo (2003). Experimental
selection of virus derivatives with variations in virulence from a single
low-pathogenicity H6N1 avian influenza virus field isolate. Avian
Diseases 47(4): 1416-1422. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Descriptors: egg production, genes, hemagglutinins,
hemorrhage, mortality, phylogeny, renal lesions, virulence, avian influenza
virus, Taiwan.
Wang HeMin, He Cheng, Zhang JianPing, and Li HaoPeng
(2004). Studies on avian influenza inactivated vaccine of AIV-H5N1. Journal
of China Agricultural University 9(1): 41-44. ISSN: 1007-4333.
NAL
Call Number: S19.C58
Descriptors: antibodies, antigens, disease control,
disease prevention, dosage, immune response, inactivated vaccines, vaccination,
vaccine development, avian influenza virus, fowl, embryos.
Wang, M. and R.G. Webster (1990). Lack of
persistence of influenza virus genetic information in ducks. Archives of
Virology 111(3-4): 263-7. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Clearance of infectious virus and RNA
occurred concurrently after oral infection of ducks with influenza virus. There
was no evidence from polymerase chain reaction (PCR) analysis of the
hemagglutinin (HA) gene for persistence of viral genetic information. No
detectable RNA was found in the spleen indicating processing of antigen near
the site of replication.
Descriptors: ducks microbiology, fowl plague microbiology,
influenza A virus avian genetics, RNA viral genetics, chronic disease, DNA
probes, fowl plague genetics, avian isolation and purification, molecular
sequence data, polymerase chain reaction, RNA viral isolation and purification,
virus replication.
Wang, X., A.E. Castro, M.D. Castro, H. Lu, D.
Weinstock, N. Soyster, W. Scheuchenzuber, and M. Perdue (2000). Production
and evaluation criteria of specific monoclonal antibodies to the hemagglutinin
of the H7N2 subtype of avian influenza virus. Journal of Veterinary
Diagnostic Investigation, Official Publication of the American Association of
Veterinary Laboratory Diagnosticians, Inc 12(6): 503-9. ISSN: 1040-6387.
NAL
Call Number: SF774.J68
Abstract: To enhance the rapidity in diagnosing the
spread of avian influenza virus (AIV) in chicken layer flocks, studies were
initiated to develop more sensitive and specific immunological and molecular
methods for the detection of AIV. In this study, the purification of the
hemagglutinin protein (H) from field isolates of H7N2, the production of
monoclonal antibodies (MAbs), and their evaluation as diagnostic reagents are
reported. Hybridomas were generated by fusion of SP2/0-Ag14 myelomas and spleen
cells from immunized mice. Hybridomas secreting antibodies specific for the H
protein were assayed by an ELISA and cloned using limiting dilution. The MAbs
produced were characterized by hemagglutination inhibition (HI),
immunohistochemistry (IHC), indirect fluorescent antibody assay (IFA), Western
blots, and IFA flow cytometry using various AIV subtypes (i.e., H4N2, H5N3,
H7N2). Of the various MAbs assayed, 6 had consistent and reproducible results
in each of the assays used. The results obtained in this investigation enhanced
the usage of the MAbs to viral H protein in the surveillance of AIV in
chickens.
Descriptors: antibodies, monoclonal diagnostic use, fowl
plague diagnosis, hemagglutinin glycoproteins, influenza virus immunology,
influenza A virus avian isolation and purification, poultry diseases diagnosis,
antibodies, monoclonal biosynthesis, blotting, western, chickens, fluorescent
antibody technique, indirect, hemagglutination inhibition tests, hybridomas,
immunohistochemistry, avian immunology, mice, poultry diseases virology.
Ward, C.W. (1981). Structure of the influenza
virus hemagglutinin. Current Topics in Microbiology and Immunology
94-95: 1-74. ISSN: 0070-217X.
NAL
Call Number: QR1.C8
Descriptors: hemagglutinins viral analysis, hemagglutinins
viral immunology, influenza A virus avian immunology, human immunology, amino
acid sequence, base sequence, epitopes, genes viral, avian genetics, human
genetics, macromolecular systems, protein conformation, variation genetics.
Ward, C.W., R.G. Webster, A.S. Inglis, and T.A.
Dopheide (1981). Composition and sequence studies show that
A/duck/Ukraine/1/63 haemagglutinin (Hav7) belongs to the Hong Kong (H3)
subtype. Journal of General Virology 53(Pt. 1): 163-8. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The haemagglutinin chains HA1 and HA2 from
the avian influenza virus A/duck/Ukraine/1/63 (Hav7, Neq2) have been subjected
to amino acid analysis and N-terminal sequencing. Automated sequenator analysis
of HA1 (40 cycles), after enzymic removal of the N-terminal pyroglutamic acid
blocking group, and HA2 (43 cycles) showed that the Hav7 haemagglutinin closely
resembled the human Hong Kong (H3) haemagglutinins including the presence of
the characteristic extended 10 residue sequence at the N-terminus of HA1. These
findings, together with the amino acid compositions for both chains,
demonstrate that the Hav7 haemagglutinin is structurally similar to the Hong
Kong (H3) haemagglutinins.
Descriptors: hemagglutinins viral classification,
influenza A virus avian immunology, human immunology, amino acid sequence,
amino acids analysis, hemagglutinins viral analysis.
Ward, M.D., F.J. Fuller, J. Mehrotra, and E.V. De
Buysscher (1999). The nucleoprotein of Newcastle disease virus: the avian
immune response to rNP of NDV is not different from the response to rNP of
avian influenza virus. Proceedings of the Western Poultry Diseases
Conference 48: 141.
NAL
Call Number: SF995.W4
Descriptors: Newcastle disease virus, nucleoproteins,
chickens, immune response.
Weber, T., G. Paesold, C. Galli, R. Mischler, G.
Semenza, and J. Brunner (1994). Evidence for H(+)-induced insertion of
influenza hemagglutinin HA2 N-terminal segment into viral membrane. Journal
of Biological Chemistry 269(28): 18353-8.
ISSN: 0021-9258.
NAL
Call Number: 381 J824
Abstract: Fusion of influenza virus with target
membranes is induced by acid and involves complex changes in the viral fusion
protein hemagglutinin. At 0 degree C, in a first kinetically resolvable step,
the hemagglutinin polypeptide 2 (HA2) N-terminal segment (fusion peptide) is
exposed and inserts into the target membrane (Tsurudome, M., Gluck, R., Graf,
R., Falchetto, R., Schaller, U., and Brunner, J. (1992) J. Biol. Chem. 267,
20225-20232). We now report studies of the changes taking place at pH 5.0 and
37 degrees C, conditions that result in fusion or, in the absence of a target
membrane, in inactivation of the virus' fusion capacity. To this end, we synthesized
the new photosensitive phospholipid, 1-palmitoyl-2-[decanedioyl
mono-[2-(125I)iodo-4-(3-trifluoromethyl-3H-diazirin-3-yl)-benzyl]e ster]-
sn-glycero-3-phosphocholine (specific radioactivity, > 2000 Ci/mmol), and
worked out a protocol to incorporate this lipid into the viral membrane.
Subsequent photoactivation of the reagent resulted in selective labeling of the
C-terminal portion of the HA2 polypeptide chain, in agreement with the membrane
topology of hemagglutinin. When, however, prior to reagent activation, the
viruses were exposed at pH 5.0, 37 degrees C, both the HA2 C-terminal and the
N-terminal regions were labeled, suggesting that the HA2 N-terminal segment
(fusion peptide) inserted into the viral membrane. Possible implications for
fusion and virus inactivation are discussed.
Descriptors: hemagglutinins viral metabolism, hydrogen-ion
concentration, influenza A virus avian physiology, membrane fusion, azirines
chemical synthesis, chick embryo, hemagglutinin glycoproteins, influenza virus,
iodine radioisotopes, kinetics, liposomes, peptide fragments metabolism,
phosphatidylcholines chemical synthesis, radioisotope dilution technique,
temperature, viral envelope proteins metabolism.
Webster, R.G. and C.H. Campbell (1972). The in
vivo production of "new" influenza A viruses. II. In vivo isolation
of "new" viruses. Virology 48(2): 528-36. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: orthomyxoviridae isolation and purification,
recombination, genetic, antigens, heterophile, chickens, epitopes, genetics,
microbial, hemagglutination inhibition tests, hemagglutinins viral analysis,
hybridization, genetic, immunization, influenza A virus avian enzymology, avian
immunology, lung, neuraminidase, neutralization tests, orthomyxoviridae enzymology,
orthomyxoviridae immunology, tissue extracts, turkeys, viral vaccines.
Webster, R.G. and C.H. Campbell (1974). Studies on
the origin of pandemic influenza. IV. Selection and transmission of
"new" influenza viruses in vivo. Virology 62(2): 404-13. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: orthomyxoviridae immunology, recombination,
genetic, selection genetics, antibody formation, antigens, viral, chickens,
hemagglutinins viral immunology, immunization, immunization, secondary,
influenza A virus avian immunology, neuraminidase immunology, turkeys.
Webster, R.G., C.H. Campbell, and A. Granoff (1971). The
"in vivo" production of "new" influenza A viruses. I.
Genetic recombination between avian and mammalian influenza viruses. Virology
44(2): 317-28. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: orthomyxoviridae enzymology, orthomyxoviridae
growth and development, orthomyxoviridae immunology, orthomyxoviridae isolation
and purification, orthomyxoviridae pathogenicity, recombination, genetic,
antigens analysis, centrifugation, density gradient, chick embryo, fetal
membranes, fibroblasts, hemagglutination inhibition tests, hemagglutination
tests, hemagglutinins viral analysis, hybridization, genetic, immune sera, influenza
microbiology, influenza A virus avian enzymology, avian growth and development,
avian immunology, avian pathogenicity, lung microbiology, neuraminidase
analysis, rabbits, sucrose, swine, tissue culture, turkeys, virulence, virus
replication.
Webster, R.G., V.S. Hinshaw, W.J. Bean, K.L. Van
Wyke, J.R. Geraci, D.J. St Aubin, and G. Petursson (1981). Characterization
of an influenza A virus from seals. Virology 113(2): 712-24. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus physiology,
orthomyxoviridae infections veterinary, pinnipedia microbiology, seals
microbiology, antigens, viral analysis, birds microbiology, conjunctivitis
etiology, genes viral, influenza A virus avian immunology, influenza A virus
isolation and purification, mammals microbiology, orthomyxoviridae infections
microbiology, RNA viral genetics, virus replication.
Webster, R.G., V.S. Hinshaw, and W.J.J. Bean (1977). Antigenic
shift in myxoviruses. Medical Microbiology and Immunology 164(1-3):
57-68. ISSN: 0300-8584.
Descriptors: antigens, viral genetics, influenza A virus
immunology, disease reservoirs, ducks, epitopes, hemagglutinins viral genetics,
influenza A virus avian genetics, avian immunology, human genetics, human
immunology, porcine genetics, porcine immunology, influenza A virus genetics,
mutation, neuraminidase genetics, recombination, genetic, swine, United States,
variation genetics.
Webster, R.G., Y. Kawaoka, and W.J.J. Bean (1986). Molecular
changes in A/Chicken/Pennsylvania/83 (H5N2) influenza virus associated with
acquisition of virulence. Virology 149(2): 165-73. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: One of the unresolved questions concerning
the acquisition of virulence by the A/Chicken/Pennsylvania/83 (H5N2) influenza
virus is which gene segments other than the hemagglutinin (HA) showed changes
that were relevant. To answer this question, reassortants were made possessing
the hemagglutinin gene of the virulent virus and the seven other genes from the
avirulent parent. Since both the virulent and avirulent H5N2 strains are
antigenically almost indistinguishable, it was necessary to transfer the genes
of interest to a "carrier" virus before the appropriate reassortment
could be selected. The gene compositions of the reassortants was established by
a combination of sequence analysis and migration on polyacrylamide gels. These
analyses established that the avirulent influenza virus present in April 1983
possessed seven of the eight gene segments necessary for virulence; mutation(s)
in the HA gene were required for acquisition of virulence. Other viruses such
as A/Seal/Mass/1/80 (H7N7) could provide the other genes necessary for
virulence. Two changes in the HA have been associated with the acquisition of
virulence; these are at amino acid residues 23 and 78 (H3 numbering) (Y.
Kawaoka and R.G. Webster, Virology, 146, 130-137 (1985]. Isolation of an
amantadine-resistant avirulent revertant virus provided the opportunity to
determine which of the two amino acid changes in HA is critical. Sequence
analysis of the revertant virus revealed amino acid changes at residues 23 in
HA1 and 40 in HA2 (H3 numbering). The change at residue 23 of HA1 is probably
associated with reversion to avirulence, of cleavability of HA, and inability to
plaque in tissue culture without trypsin; while the change at residue 40 of HA2
may be associated with the amantadine-resistant phenotype. These studies
establish that a single critical point mutation in the hemagglutinin gene of
the avirulent A/Chicken/Pennsylvania/1/83 (H5N2) was probably all that was
required to produce the highly virulent Chicken/Pennsylvania virus; the
avirulent virus already possessed the other genes necessary for virulence.
Descriptors: hemagglutinins viral genetics, influenza A virus
avian pathogenicity, amino acid sequence, cultured cells, chick embryo,
chickens, genes viral, avian enzymology, avian genetics, avian immunology,
mutation, neuraminidase genetics, plaque assay, recombination, genetic,
virulence.
Webster, R.G., Y. Kawaoka, J. Taylor, R. Weinberg,
and E. Paoletti (1991). Efficacy of nucleoprotein and haemagglutinin
antigens expressed in fowlpox virus as vaccine for influenza in chickens. Vaccine
9(5): 303-8. ISSN: 0264-410X.
NAL
Call Number: QR189.V32
Abstract: Fowlpox virus (FPV) recombinants expressing
influenza virus H5 haemagglutinin (HA), nucleoprotein (NP) or co-expressing
both of these antigens were tested for vaccine efficacy in chickens.
Immunization with the recombinant FPV-HA was highly efficacious but provided no
cross protection between subtypes. Bursectomy established that immunity against
the H5 subtype was antibody-mediated despite the presence of very low levels of
antibody in the vaccinated birds. Immunization with the recombinant FPV
expressing the cross-reactive NP antigen did not provide protective immunity
despite hyperimmunization and provided no benefit above HA expressed alone. The
results suggest that the kinetics of viral replication outpaces immunity
induced by NP.
Descriptors: antigens, viral administration and
dosage, fowl plague prevention and
control, fowlpox virus immunology, viral vaccines administration and dosage,
chickens, cross reactions, fowlpox virus genetics, hemagglutinins viral immunology,
immunity, cellular, influenza A virus avian genetics, avian immunology,
nucleoproteins immunology, vaccines, synthetic administration and dosage, viral
proteins immunology.
Webster, R.G., B. Tumova, V.S. Hinshaw, and G. Lang
(1976). Characterization of avian influenza viruses. Designation of a newly
recognized haemagglutinin. Bulletin of the World Health Organization
54(5): 555-60. ISSN: 0042-9686.
NAL
Call Number: 449.9 W892B
Descriptors: agglutinins, hemagglutinins, orthomyxoviridae
immunology, birds microbiology, turkeys microbiology.
Wei, D.P., Y.L. Liu, W.X. Shao, J.H. Lu, and X.F. Liu
(2004). Recombinant fowlpox virus expressing F of Newcastle disease virus
and HA of subtype H9N2 of avian influenza virus. Weishengwu Xuebao
44(3): 286-290. ISSN: 0001-6209.
NAL
Call Number: 448.3 Ac83
Descriptors: Newcastle disease, fowlpox, avian influenza
virus, prevention, control, Southern blot, gene sequence analysis, indirect
immunofluorescence assay, polymerase chain reaction, PCR.
Westphal, G., H. Wasicki, U. Zielinski, F.G. Weber,
M. Tonew, and E. Tonew (1977). Potentielle Virostatica. Teil 1: Chinoxaline.
[Potential virostatics. 1. Quinoxalines]. Pharmazie 32(10):
570-1. ISSN: 0031-7144.
Descriptors: antiviral agents chemical synthesis,
quinoxalines chemical synthesis, enterovirus drug effects, herpesvirus 1, suid
drug effects, influenza A virus avian drug effects, quinoxalines pharmacology,
sindbis virus drug effects, vaccinia virus drug effects.
White, J., J. Kartenbeck, and A. Helenius (1982). Membrane
fusion activity of influenza virus. EMBO Journal 1(2): 217-22. ISSN: 0261-4189.
NAL
Call Number: QH506.E46
Abstract: A simple assay is described to monitor fusion
between fowl plague virus (FPV, an avian influenza A virus) and liposomes which
allows the simultaneous quantitation of both lytic and non-lytic fusion events.
As in fusion between viruses and the plasma membrane and in FPV-induced
cell-cell fusion, the reaction only occurs at pH 5.5 or below, and it is fast,
highly efficient, and essentially non-lytic when fresh virus and liposomes are
used. The fusion occurs over a broad temperature range, and has no requirement
for divalent cations. The fusion factor of influenza virus is a hemagglutinin
(HA) spike which protrudes from the virus membrane and which is also
responsible for virus binding to the host cell. The finding that fusion occurs
as efficiently with liposomes containing or lacking virus receptor structures,
further emphasizes the remarkable division of labor in the HA molecule: the
receptor-binding sites are located in the globular HA1 domains and the fusion
activation peptide is found at the N-terminal of HA2 in the stem region of the
protein. The mechanism of fusion is discussed in terms of the three-dimensional
structure of the HA and the conformational change which the protein undergoes
at the fusion pH optimum.
Descriptors: influenza A virus avian physiology,
liposomes, membrane fusion, chick embryo, hemagglutinins viral, hydrogen-ion
concentration, microscopy, electron, temperature, time factors, trypsin
metabolism, trypsin inhibitor, kunitz soybean pharmacology.
White, J., K. Matlin, and A. Helenius (1981). Cell
fusion by Semliki Forest, influenza, and vesicular stomatitis viruses. Journal of Cell Biology 89(3): 674-9. ISSN: 0021-9525.
NAL
Call Number: 442.8 J828
Abstract: Representatives of three families of
enveloped viruses were shown to fuse tissue culture cells together. These were:
Semliki Forest virus (SFV, a togavirus), vesicular stomatitis virus (a
rhabdovirus), and two myxoviruses, fowl plaque virus and Japan influenza virus
(Japan)/A/305/57). Unlike paramyxoviruses, whose fusion activity is known to
occur over a broad pH range, fusion by these viruses was restricted to mildly
acidic pH. The pH thresholds for the four viruses were 6.0, 6.1, 5.5, and 5.1,
respectively. The precursor form of Japan influenza, which is not infectious
and which contains the uncleaved hemagglutinin, had no fusion activity. This
result suggested a role for the influenza hemagglutinin in the low-pH-dependent
membrane fusion activity. Taken together, our results show that low-pH-induced
fusion is a widespread property of enveloped animal viruses and that it may
play a role in the infective process. The fusion reactions with all four
viruses were fast, efficient, and easy to induce. With UV-inactivated SFV, the
fusion was shown to be nonlytic and the polykaryons were viable for at least 12
h. 30 ng of SFV/1 x 10(6) BHK-21 cells were required for 50% fusion, and 250 ng
sufficed to fuse the entire culture into a single polykaryon.
Descriptors: cell fusion, influenza A virus avian
physiology, human physiology, Semliki Forest virus physiology, vesicular
stomatitis Indiana virus physiology, cell line, cell survival, hamsters,
hemagglutinins viral, hydrogen-ion concentration.
Widjaja, L., S.L. Krauss, R.J. Webby, T. Xie, and
R.G. Webster (2004). Matrix gene of influenza a viruses isolated from wild
aquatic birds: ecology and emergence of influenza A viruses. Journal of
Virology 78(16): 8771-9. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Wild aquatic birds are the primary reservoir
of influenza A viruses, but little is known about the viruses' gene pool in
wild birds. Therefore, we investigated the ecology and emergence of influenza
viruses by conducting phylogenetic analysis of 70 matrix (M) genes of influenza
viruses isolated from shorebirds and gulls in the Delaware Bay region and from
ducks in Alberta, Canada, during >18 years of surveillance. In our analysis,
we included 61 published M genes of isolates from various hosts. We showed that
M genes of Canadian duck viruses and those of shorebird and gull viruses in the
Delaware Bay shared ancestors with the M genes of North American poultry
viruses. We found that North American and Eurasian avian-like lineages are
divided into sublineages, indicating that multiple branches of virus evolution
may be maintained in wild aquatic birds. The presence of non-H13 gull viruses
in the gull-like lineage and of H13 gull viruses in other avian lineages
suggested that gulls' M genes do not preferentially associate with the H13
subtype or segregate into a distinct lineage. Some North American avian
influenza viruses contained M genes closely related to those of Eurasian avian
viruses. Therefore, there may be interregional mixing of the two clades.
Reassortment of shorebird M and HA genes was evident, but there was no correlation
among the HA or NA subtype, M gene sequence, and isolation time. Overall, these
results support the hypothesis that influenza viruses in wild waterfowl contain
distinguishable lineages of M genes.
Descriptors: animals, wild virology, birds virology, ecology,
evolution, molecular, influenza A virus, avian genetics, viral matrix proteins
genetics, ducks virology, avian classification, avian isolation and
purification, molecular sequence data, phylogeny, sequence analysis, DNA.
Wiegers, K.J. and R. Drzeniek (1973). Ribonuclease
present in myxoviruses. Zeitschrift Fur Naturforschung. Teil C
Biochemie, Biophysik, Biologie, Virologie 28(5): 346-50. ISSN: 0341-0471.
NAL
Call Number: QH301.Z4
Descriptors: orthomyxoviridae enzymology, ribonucleases
analysis, deoxyribonucleases metabolism, hemagglutination, influenza A virus
avian enzymology, Newcastle disease virus enzymology, polioviruses enzymology,
ribonucleases metabolism.
Williams, J.G. and I.A. Macpherson (1973). The
differential effect of actinomycin D in normal and virus-transformed cells.
Journal of Cell Biology 57(1): 148-58.
ISSN: 0021-9525.
NAL
Call Number: 442.8 J828
Descriptors: cell transformation, neoplastic drug effects,
dactinomycin pharmacology, cell line, cell nucleus metabolism, clone cells,
dactinomycin metabolism, hamsters, influenza A virus avian growth and
development, kidney, RNA antagonists and inhibitors, RNA biosynthesis, RNA,
neoplasm biosynthesis, tritium, uridine
metabolism, virus replication drug effects.
Wolstenholme, A.J., T. Barrett, S.T. Nichol, and B.W.
Mahy (1980). Influenza virus-specific RNA and protein syntheses in cells
infected with temperature-sensitive mutants defective in the genome segment
encoding nonstructural proteins. Journal of Virology 35(1):
1-7. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Virus-specific protein and RNA syntheses have
been analyzed in chicken embryo fibroblast cells infected with two group IV
temperature-sensitive (ts) mutants of influenza A (fowl plague) virus in which the
ts lesion maps in RNA segment 8 (J. W. Almond, D. McGeoch, and R. D. Barry,
Virology 92:416-427, 1979), known to code to code for two nonstructural
proteins, NS1 and NS2. Both mutants induced the synthesis of similar amounts of
all the early virus-specific proteins (P1, P2, P3, NP, and NS1) at temperatures
that were either permissive (34 degrees C) or nonpermissive (40.5 degrees C)
for replication. However, the synthesis of M protein, which normally
accumulates late in infection, was greatly reduced in ts mutant-infected cells
at 40.5 degrees C compared to 34 degrees C. The NS2 protein was not detected at
either temperature in cells infected with one mutant (mN3), and was detected
only at the permissive temperature in cells infected with mutant ts47. There
was no overall reduction in polyadenylated (A+) complementary RNA, which
functions as mRNA, in cells infected with these mutants at 40.5 degrees C
compared to 34 degrees C, nor was there any evidence of selective accumulation
of this type of RNA within the nucleus at the nonpermissive temperature. No
significant differences in ts mutant virion RNA transcriptase activity were
detected by assays in vitro at 31 and 40.5 degrees C compared to wild-type
virus. Virus-specific non-polyadenylated (A-) complementary RNA, which is
believed to act as the template for new virion RNA production, accumulated
normally in cells at both 34 and 40.5 degrees C, but at 40.5 degrees C
accumulation of new virion RNA was reduced by greater than 90% when compared to
accumulation at 34 degrees C.
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, viral proteins biosynthesis, chick embryo, chromosome mapping,
DNA directed RNA polymerases metabolism, fibroblasts, avian genetics, mutation,
temperature, viral nonstructural proteins.
Wood, G.W., J. Banks, J.W. McCauley, and D.J.
Alexander (1994). Deduced amino acid sequences of the haemagglutinin of H5N1
avian influenza virus isolates from an outbreak in turkeys in Norfolk, England.
Archives of Virology 134(1-2): 185-94.
ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The deduced amino acid sequences of the
haemagglutinins of avian influenza viruses, isolated from an outbreak in
turkeys in Norfolk, England in 1991/92, were determined by PCR amplification
and cycle sequencing. Both the highly pathogenic and avirulent isolates had the
same cleavage site sequence with multiple-basic amino acids, which normally
would be expected only for the former. Clones derived by plaque picking from
the highly pathogenic isolate ranged from low to very high pathogenicity in
vivo and these, and the original isolates, showed nucleotide and amino acid
variation at one or more of five possible sites, none of which were at the
cleavage site. None of these site variations correlated with pathogenicity,
suggesting that the factor responsible for the suppression of the expected
effects of the multiple-basic amino acid haemagglutinin cleavage site in the
avirulent isolate may not have been part of the haemagglutinin amino acid
sequence.
Descriptors: disease outbreaks veterinary, fowl plague
microbiology, hemagglutinins viral genetics, influenza A virus avian genetics,
poultry diseases microbiology, turkeys microbiology, amino acid sequence, base
sequence, DNA, viral, England epidemiology, fowl plague epidemiology,
hemagglutinin glycoproteins, influenza virus, molecular sequence data, poultry
diseases epidemiology, RNA.
Wood, G.W., J. Banks, I. Strong, G. Parsons, and D.J.
Alexander (1996). An avian influenza of H10 subtype that is highly
pathogenic for chickens, but lacks multiple basic amino acids at the
haemagglutinin cleavage. Avian Pathology 25(4): 799-806. ISSN: 0307-9457.
NAL
Call Number: SF995.A1A9
Abstract: Avian influenza virus isolate A/mandarin
duck/Singapore/805/F-72/7/93 was found to be consistently highly pathogenic by
recognised in vivo testing procedures although it was of a subtype (H10) not
usually associated with high pathogenicity. The virus was also not typical of highly
pathogenic influenza viruses in that it was not pathogenic when administered
intra-nasally, did not possess a haemagglutinin cleavage site with multiple
basic amino acids and did not replicate in the brains of chickens after
intravenous inoculation. A re-examination of the earlier H10 isolate
A/turkey/England/384/79 suggested that it was similarly pathogenic. The
pathogenicity may have been associated with replication in the kidney.
Descriptors: chickens, avian influenza virus,
pathogenicity, amino acids, nucleotide sequences, amino acid sequences, viral
replication, animal tissues, molecular sequence data.
Wood, G.W., J.W. McCauley, J.B. Bashiruddin, and D.J.
Alexander (1993). Deduced amino acid sequences at the haemagglutinin
cleavage site of avian influenza A viruses of H5 and H7 subtypes. Archives of Virology 130(1-2):
209-17. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The amino acid sequences at the
haemagglutinin cleavage sites of 9 avian influenza A viruses of H5 subtype (5
high and 4 low pathogenicity for chickens) and 21 of H7 subtype (13 high and 8
low pathogenicity for chickens) were determined by direct RNA sequencing, PCR
amplification sequencing or both. None of the viruses of low pathogenicity had
multiple basic amino acids at the cleavage site. All highly pathogenic viruses
had an insert of basic amino acids at the cleavage site, except
A/chicken/Scotland/59 (H5N1) for which the multiple basic amino acids appeared
as substitutions and not insertions. All highly pathogenic viruses examined
conformed to the amino acid motif of R-X-R/K-R at the cleavage site which is
considered to be essential for high pathogenicity in chickens, with the notable
exception of highly pathogenic virus A/turkey/England/50-92/91 (H5N1) which had
the sequence R-K-R-K-T-R adjacent to the cleavage site.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, amino acid sequence, base sequence, birds, chick embryo,
chickens, hemagglutinin glycoproteins, influenza virus, avian classification,
molecular sequence data, oligodeoxyribonucleotides, polymerase chain reaction,
sequence homology, amino acid, sequence homology, nucleic acid, turkeys, viral
envelope proteins genetics.
Wood, G.W., G. Parsons, and D.J. Alexander (1995). Replication
of influenza A viruses of high and low pathogenicity for chickens at different
sites in chickens and ducks following intranasal inoculation. Avian Pathology 24(3): 545-551. ISSN: 0307-9457.
NAL
Call Number: SF995.A1A9
Abstract: Ten specific pathogen free light breed
chickens and 10 commercial layer ducks were inoculated intranasally with one of
five avian influenza A viruses which had been characterised as showing high or
low pathogenicity for chickens. Recovery of the two viruses of low pathogenicity
was restricted to the respiratory tract and gut of both species. Highly
pathogenic viruses were recovered from all organs sampled. With two of the
highly pathogenic viruses, A/duck/Ireland/113/83 (H5N8) and
A/chicken/Victoria/85 (H7N7), the sites of recovery in ducks were similar to
those seen in chickens except that virus was absent from the brain, apart from
low levels detected in brain samples taken on day 5 from ducks infected with
A/duck/Ireland/113/83. The levels recovered from organs of ducks for these two
viruses were also similar to those in chickens, except for lower levels in
kidney and liver for ducks infected with A/chicken/Victoria/85, and a delayed
peak of recovery of both viruses in ducks. The third highly pathogenic virus,
A/turkey/England/50-92/91 (H5N1), could not be recovered from any site in
ducks. For all three highly pathogenic viruses mortality and morbidity were
rapid and complete in chickens but absent in ducks.
Descriptors: animal husbandry, digestive system,
infection, methods and techniques, nervous system, respiratory system, urinary
system, veterinary medicine, brain gut kidney liver morbidity mortality
pathogenicity respiratory tract.
Woyciniuk, P., M. Linder, and C. Scholtissek (1995). The
methyltransferase inhibitor Neplanocin A interferes with influenza virus
replication by a mechanism different from that of 3-deazaadenosine. Virus
Research 35(1): 91-9. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: Neplanocin A (NeplA) and 3-deazaadenosine
(3DA-Ado) are both inhibitors of methyltransferases, and both interfere with
influenza virus replication. Their modes of action, however, are different. In
chicken embryo cells NeplA inhibits only in media depleted of or low in
methionine, while 3DA-Ado acts independently of the concentration of
methionine. While homocysteine partially reverses the effect of NeplA, it
strongly potentiates the effect of 3DA-Ado. While NeplA inhibits the synthesis
of all viral proteins to nearly the same extent, 3DA-Ado interferes only with
the production of late proteins (Fischer et al. (1990) Virology 177, 523-531).
In NeplA-pretreated cells there is an extreme accumulation of
S-adenosylhomocysteine, independent of the concentration of methionine in the
medium, although NeplA inhibits influenza virus replication only in
methionine-depleted medium. Therefore an accumulation of this intermediate by
NeplA cannot account for the inhibitory effect, as has been implicated in the
inhibition of the replication of other viruses. Our results indicate that at
least two different methyltransferases are involved in influenza virus
replication.
Descriptors: adenosine analogs and derivatives, influenza
A virus avian drug effects, human drug effects, methyltransferases antagonists
and inhibitors, tubercidin pharmacology, virus replication drug effects,
adenosine antagonists and inhibitors, adenosine pharmacology,
adenosylhomocysteinase, chick embryo, drug synergism, homocysteine
pharmacology, hydrolases antagonists and inhibitors, avian physiology, human physiology,
methionine metabolism, RNA caps metabolism, RNA viral metabolism,
S-adenosylhomocysteine metabolism, viral proteins biosynthesis, viral proteins
genetics.
Wu QingMin, Gao QiYu, Zhang ZhongZhi, and Chen
FuYong (1999). Preparation of
nucleoprotein gene probe for avian influenza virus and its preliminary
application. Chinese Journal of
Veterinary Medicine 25(10): 5-9.
NAL
Call Number: SF604.C485
Descriptors: avian influenza virus, strains, restriction
endonuclease analysis, China, poultry, Galliformes.
Wurzer, W.J., C. Ehrhardt, S. Pleschka, F. Berberich
Siebelt, T. Wolff, H. Walczak, O. Planz, and S. Ludwig (2004). NF-kappaB-dependent
induction of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)
and Fas/FasL is crucial for efficient influenza virus propagation. Journal
of Biological Chemistry 279(30): 30931-7.
ISSN: 0021-9258.
NAL
Call Number: 381 J824
Abstract: Activation of the transcription factor
NF-kappaB is a hallmark of infections by viral pathogens including influenza
viruses. Because gene expression of many proinflammatory and antiviral
cytokines is controlled by this factor, the concept emerged that NF-kappaB and
its upstream regulator IkappaB kinase are essential components of the innate
antiviral immune response to infectious pathogens. In contrast to this common
view we report here that NF-kappaB activity promotes efficient influenza virus
production. On a molecular level this is due to NF-kappaB-dependent viral
induction of the proapoptotic factors tumor necrosis factor-related
apoptosis-inducing ligand (TRAIL) and FasL, which enhance virus propagation in
an autocrine and paracrine fashion. Thus, NF-kappaB acts both proapoptotically
and provirally in the context of an influenza virus infection.
Descriptors: antigens, cd95 biosynthesis, influenza A
virus, avian physiology, human physiology, membrane glycoproteins biosynthesis,
NF-kappaB metabolism, tumor necrosis factor alpha biosynthesis, cell line,
cercopithecus aethiops, dogs, mutation, protein serine threonine kinases
genetics, protein serine threonine kinases metabolism, signal transduction,
vero cells, virus replication.
Xie Jing, Wang YongKun, Yan WeiWei, Zhuang GuoHong,
Zhou JiHong, Wang JianYe, Liu HuaLei, Yu Bing, and Zhu GuoQiang (2001). Cloning,
sequence analysizing of hemagglutinin gene of an avian influenza viruses
isolated from Muscovy. Journal of Yangzhou University, Natural Science
Edition, Yangzhou, China 4(3): 51-54.
ISSN: 1007-824X.
NAL
Call Number: Q4.Y36
Descriptors: DNA cloning, genes, nucleotide sequences,
avian influenza virus, Muscovy ducks.
Xu, C., W. Fan, R. Wei, and H. Zhao (2004). Isolation
and identification of swine influenza recombinant A/Swine/Shandong/1/2003(H9N2)
virus. Microbes and Infection Institut Pasteur 6(10): 919-25. ISSN: 1286-4579.
NAL
Call Number: QR180.M53
Abstract: Ten influenza virus isolates were obtained
from infected pigs from different places in Shandong province showing clinical
symptoms from October 2002 to January 2003. All 10 isolates were identified in
China's National Influenza Research Center as influenza A virus of H9N2
subtype. The complete genome of one isolate, designated A/Swine/Shandong/1/2003(H9N2),
was sequenced and compared with sequences available in GenBank. The results of
analyses indicated that the sequence of A/Swine/Shandong/1/2003(H9N2) was
similar to those of several chicken influenza viruses and duck influenza
viruses recently prevalent in South China. According to phylogenetic analysis
of the complete gene sequences, A/Swine/Shandong/1/2003(H9N2) possibly
originated from the reassortment of chicken influenza viruses and duck
influenza viruses. It was found that the amino acid sequence at the HA cleavage
site in Sw/SD/1/2003 is R-S-L-R-G, differing clearly from that of other H9N2
subtype isolates of swine influenza and avian influenza, which is R-S-S-R-G.
Descriptors: influenza veterinary, influenza A virus,
porcine genetics, swine diseases virology, amino acid sequence, base sequence,
chick embryo, guinea pigs, influenza virology, porcine chemistry, porcine
isolation and purification, molecular sequence data, phylogeny, RNA, viral
chemistry, viral genetics, rats, reverse transcriptase polymerase chain
reaction veterinary, sequence analysis, DNA, sequence homology, nucleic acid,
swine.
Xu, X., Subbarao, N.J. Cox, and Y. Guo (1999). Genetic characterization of the pathogenic
influenza A/Goose/Guangdong/1/96 (H5N1) virus: similarity of its hemagglutinin
gene to those of H5N1 viruses from the 1997 outbreaks in Hong Kong. Virology
261(1): 15-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Analysis of the sequences of all eight RNA
segments of the influenza A/Goose/Guangdong/1/96 (H5N1) virus, isolated from a
sick goose during an outbreak in Guangdong province, China, in 1996, revealed
that the hemagglutinin (HA) gene of the virus was genetically similar to those
of the H5N1 viruses isolated in Hong Kong in 1997. However, the remaining genes
showed greater similarity to other avian influenza viruses. Notably, the
neuraminidase gene did no have the 19-amino-acid deletion in the stalk region
seen in the H5N1 Hong Kong viruses and the NS gene belonged to allele B, while
that of the H5N1 Hong Kong viruses belonged to allele A. These data suggest
that the H5N1 viruses isolated from the Hong Kong outbreaks derived their HA
genes from a virus similar to the A/Goose/Guangdong/1/96 virus or shared a
progenitor with this goose pathogen.
Descriptors: geese virology, hemagglutinin glycoproteins,
influenza virus genetics, influenza virology, influenza A virus avian genetics,
human genetics, chickens virology, DNA, viral chemistry, DNA, viral genetics,
disease outbreaks, fowl plague epidemiology, fowl plague virology, genes viral,
Hong Kong epidemiology, influenza epidemiology, avian classification, avian
isolation and purification, human classification, molecular sequence data,
neuraminidase genetics, phylogeny, sequence analysis, DNA, viral nonstructural
proteins genetics.
Yamada, A., L.E. Brown, and R.G. Webster (1985). Antigenic
analysis of H2 influenza virus haemagglutinin with monoclonal antibodies. Vaccine
3(3 Suppl.): 195-8. ISSN: 0264-410X.
NAL
Call Number: QR189.V32
Abstract: Antigenic analysis of human and avian H2
influenza virus was carried out with monoclonal antibodies to the HA molecules
of H2 influenza viruses isolated in the early stage of an H2 pandemic. The
study revealed antigenic differences between inhibitor sensitive (Japan+/57,
RI+57) and inhibitor resistant strains (Japan-/57, Ri-/57). This indicates that
the receptor-binding specificity of the haemagglutinin can markedly influence
the antigenic analysis obtained with monoclonal antibodies in HI test. Minor
antigenic differences (microheterogeneity) could be detected between different
H2 influenza viruses isolated in 1957. Minor antigenic variation continued in
the H2 viruses until 1961, but significant antigenic drift occurred in 1962 so
that viruses isolated after that date reacted with few monoclonal antibodies.
Analysis of avian H2 influenza viruses suggested antigenic differences between
the different avian H2 haemagglutinin, but no correlation between the year of
isolation and the progressive antigenic drift similar to that seen in the human
strains was found.
Descriptors: antigens, viral immunology, hemagglutinins
viral immunology, influenza A virus avian immunology, human immunology,
antibodies, monoclonal immunology, antigens, viral genetics, genes viral,
hemagglutinins viral genetics, avian genetics, human genetics, variation
genetics.
Yamane, N., T. Odagiri, J. Arikawa, and N. Ishida
(1981). Reversed single-radial-immunodiffusion test: the method for the
assay of the antibody to influenza A nucleoprotein. Tohoku Journal of
Experimental Medicine 133(3): 245-55.
ISSN: 0040-8727.
Abstract: The reversed single-radial-immunodiffusion
(r-SRD) test using the avian-origin influenza A virus, A/chicken/Germany
"N'/49 (Hav2Neql) disrupted with 1.0% sarkosyl, was established as the
quantitative method for the assay of a type-specific antibody, particularly of
an anti-nucleoprotein antibody, in human sera. Under the test conditions, human
sera produced a definite opalescent zone around the well and the annulus area
was found to have a high correlation to the antibody level of type A influenza
nucleoprotein. The specificity of the opalescent zone produced in the test
plate was confirmed with the specific antisera to each viral polypeptide and
the adsorption procedures with the purified nucleoprotein. During an epidemic
of H3N2 and H1N1 viruses, the r-SRD test was employed to estimate the infection
ratio in junior high school students. The results demonstrated its convenience
and high sensitivity in detecting the antibody rise to influenza A
nucleoprotein. In addition, the age-distribution of the antibody level to
influenza A nucleoprotein was examined and discussed. The results obtained
strongly suggested that the r-SRD technique using the avian-origin influenza A
virus provided a simple and reproducible method for the assay of the antibody
level to influenza A nucleoprotein in a large scale seroepidemiology and in the
serodiagnosis of influenza A virus infection.
Descriptors: antibodies, viral analysis, immunodiffusion
methods, influenza A virus immunology, nucleoproteins immunology, viral
proteins immunology, adolescent, adult, age factors, aged, child, complement
fixation tests, hemagglutination inhibition tests, influenza immunology, middle
aged.
Yamnikova, S.S., A.S. Gambaryan, A.B. Tuzikov, N.V.
Bovin, M.N. Matrosovich, I.T. Fedyakina, A.A. Grinev, V.M. Blinov, D.K. Lvov,
D.L. Suarez, and D.E. Swayne (2003). Differences between HA receptor-binding
sites of avian influenza viruses isolated from Laridae and Anatidae. Avian
Diseases 47(Special Issue): 1164-1168.
ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: A comparative study of the hemagglutinin (HA)
receptor binding site (RBS) of a number of H13 influenza viruses isolated from
Laridae family of birds (gulls) and other influenza viruses obtained from the
Anatidae family (ducks) was conducted. The affinity of all viruses to alpha
N-acetylneuraminic acid (Neu5Acalpha), 3'sialyllactose (3'SL), and
sialylglycopolymers bearing 3'-sialyl(N-acetyllactosamine) (3'SLN-PAA),
(Neu5Acalpha(2-3)Galbeta(1-4))(-Fucalpha(1-3))GlcNAcbeta (SLex-PAA), and
(Neu5Acalpha(2-3)Galbeta(1-3))(-Fucalpha(1-4))GlcNAcbeta (SLea-PAA), was
determined. The last three polymer glycoconjugates were synthesized for
determining the contribution of carbohydrate chains after the galactose link to
the binding with the receptor. The difference in affinity between 3'SL and
Neu5Acalpha in all studied H13 viruses is small, which indicates a less
significant role of the galactose moiety in the binding to the receptor. The
results of virus binding with polymer sialylglycoconjugates indicates that the
method of linking, the third monosaccharide moiety, and the presence of an
extra fucose substitute in this moiety may influence the binding considerably.
For viruses isolated from ducks, the suitable polymer is SLea-PAA (i.e., a 1-3
linkage between galactose and glucosamine is optimal). This finding is in
accord with the data that H13 viruses isolated from the gulls differ based on
their ability to interact with polymer sialylglycoconjugates. The affinity to
all three polymers is uniform, and the presence of GlcNAc-linked fucose does
not prevent the binding. A comparative analysis of six sequenced HA H13 viruses
and other subtype viruses showed presence of substantial differences in the
composition of amino acids of this region in H13 viruses.
Descriptors: biochemistry and molecular biophysics,
infection, virology, avian influenza, infectious disease, respiratory system
disease, viral disease, viral binding affinity.
Yao, Y., L.J. Mingay, J.W. McCauley, and W.S. Barclay
(2001). Sequences in influenza A virus PB2 protein that determine productive
infection for an avian influenza virus in mouse and human cell lines. Journal
of Virology 75(11): 5410-5. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: Reverse genetics was used to analyze the host
range of two avian influenza viruses which differ in their ability to replicate
in mouse and human cells in culture. Engineered viruses carrying sequences
encoding amino acids 362 to 581 of PB2 from a host range variant productively
infect mouse and human cells.
Descriptors: influenza A virus avian genetics, viral
proteins genetics, cell line, genes viral, avian chemistry, avian
pathogenicity, mice, sequence analysis, protein, species specificity,
transfection.
Yilmaz, A., U. Heffels Redmann, and T. Redmann (
2004). Evaluation of the virucidal efficacy of two chemical disinfectants
against avian influenza virus A at different temperatures. Archiv Fur Geflugelkunde
68(2): 50-56. ISSN: 0003-9098.
NAL
Call Number: 47.8 Ar2
Descriptors: avian influenza virus, disinfectants,
formaldehyde, formic acid, potency, temperature, poultry.
Yoden, S. (1983). Avian influenza viruses in which
infectivity is neutralized by antisera lacking hemagglutination-inhibition
activity. Japanese Journal of Veterinary Research 31(2): 99. ISSN: 0047-1917.
NAL
Call Number: 41.8 V6446
Descriptors: avian influenza virus, immune serum,
hemagglutination, inhibition, antisera.
Zakstel'skaia, L.I.A., V.T. Ivanova, and E.V. Molibog
(1977). Elektroforeticheskaia kharakteristika belkov i preparativnoe
poluchenie neiraminidazy shtamma A/indiuk/Viskonsin/66 (Hav6N2) virusa grippa
ptits. [Electrophoretic characteristics of the proteins and the preparative
production of neuraminidase from the A/turkey/Wisconsin/66 (Hav6N2) strain of
the avian influenza virus]. Voprosy Virusologii (5): 551-7. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: A combination of electrophoresis in a single
plate of polyacrylamide gel with preparative production of subunits upon
electrophoresis in acetate cellulose was used for the analysis of the
polypeptide composition of the A/turkey/Wisconsin/66 strain. Seven classes of
proteins with certain functional significance and 4 minor components were
detected. A preparation of neuraminidase could be obtained which has enzymatic
and antigenic activity, and a molecular mass of 68,000 daltons. Some features
of the polypeptide composition were revealed, including the presence of
uncleaved hemagglutinin under reducing conditions and a decreased content of
the light chain of hemagglutinin.
Descriptors: influenza A virus avian analysis,
neuraminidase isolation and purification, viral proteins analysis,
electrophoresis, cellulose acetate, electrophoresis, polyacrylamide gel,
hemagglutination, viral, avian enzymology, molecular weight, peptides analysis.
Zakstel'skaia, L.I.A., E.V. Molibog, S.V. Khliustov,
and V.A. Isachenko (1977). Shtammovye razlichiia v spetsifichnosti
neiraminidazy podtipa N 1. [Strain differences in the neuraminidase specificity
of subtype N 1]. Voprosy Virusologii (6): 279-82. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Nine strains having neuraminidase of subtype
N1 and two strains in which the appurtenance of neuraminidase to subtype N1 was
determined in the course of the study were examined for the antigenic specificity
of the functional center of the enzyme in the cross neuraminidase activity
inhibition test. Neuraminidase of the strains A/Swine/Tatarstan/64 and
A/Swine/Ikshurminsk was shown to belong to the subtype N1 but to differ from
neuraminidase of the strain A/Swine/Iowa/15/30. Neuraminidase of the strain
A/Chicken/USSR/314/67 differs from neuraminidases of A/PR8/34, A/WS/33, and
A/Swine/Iowa/15/30 but is related to neuraminidases of the strains A/New
Jersey/8/76, A/duck/Germany/1868/68 and A/Chicken/Scotland/59. The A/New
Jersey/8/76 neuraminidase is not related to neuraminidases of the strains
A/PR8/34 and A/WS/33 but is related to neuraminidases of strains isolated from
swine and domestic fowl. The disclosed considerable strain variations in the
antigenic specificity of neuraminidases attest to heterogeneity of the subtype
N1 and the possibility of its subdivision into groups.
Descriptors: antigens, viral, influenza A virus
enzymology, binding sites, antibody, epitopes, avian enzymology, human
enzymology, influenza A virus, porcine enzymology, influenza A virus
immunology, species specificity.
Zakstel'skaia, L.I.A., S.F. Shenderovich, M.A.
Iakhno, V.A. Isachenko, and V.M. Zhdanov (1980). Issledovanie antigennoi
obshchnosti gemaggliutininov virusov grippa A cheloveka i zhivotnykh metodom
immunoadsorbtsii. [Antigenic similarity of the hemagglutinins of human and
animal influenza A viruses studied by immunoadsorption]. Voprosy
Virusologii 3: 287-90. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Antigenic relationships between human
influenza A viruses containing hemagglutinins of HO and H1 subtypes and animal
and avian influenza viruses Hsw1 and Hav5 were studied by immunoadsorption
using inorganic base of the sorbent. Direct and indirect relations due to the
presence in hemagglutinin of common antigenic determinants and hapten groups
were revealed. The strains representing drift variations within one subtype
differed by the spectrum of hapten determinants typical of other subtypes. No
common determinant typical for all members of this group was isolated.
Descriptors: antigens, viral analysis, hemagglutinins
viral analysis, influenza A virus avian immunology, human immunology, porcine
immunology, influenza A virus
immunology, epitopes analysis, hemagglutination inhibition tests, immunosorbent
techniques.
Zavada, J. (1969). A host-cell DNA function
involved in the replication of avian tumour viruses and of fowl-plague virus.
Journal of General Virology 4(4): 571-6.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: alpharetrovirus, DNA, viral biosynthesis,
influenza A virus avian drug effects, avian radiation effects, sarcoma viruses,
avian, cell line metabolism, cell line radiation effects, cell transformation,
neoplastic, chick embryo, DNA metabolism, dactinomycin pharmacology, hamsters,
kidney, virus replication.
Zavada, J. and M. Rosenbergova (1968). Double
neutralization of fowl plague virus reproduced in chick myeloblasts. Acta
Virologica 12(3): 282-4. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: influenza A virus avian immunology, leukosis
virus, avian immunology, avian leukosis, chickens, neutralization tests, tissue
culture.
Zavada, J. and M. Rosenbergova (1972). Phenotypic
mixing of vesicular stomatitis virus with fowl plague virus. Acta
Virologica 16(2): 103-14. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: hybridization, genetic, influenza A virus
avian immunology, phenotype, vesicular stomatitis Indiana virus immunology,
antigens, viral analysis, cattle, centrifugation, density gradient, chick
embryo, genetics, microbial, heat, hemolytic plaque technique, immune sera,
avian growth and development, avian isolation and purification, neutralization
tests, rabbits, sucrose, tissue culture, vesicular stomatitis Indiana virus
growth and development, vesicular stomatitis Indiana virus isolation and
purification, virus cultivation.
Zeng, Y.B., X.A. Jiao, Z.M. Pan, J.L. Huang, P.H.
Zhang, S.H. Zhang, Q.Y. Sun, and X.F. Liu (2004). [Preparation and
characterization of monoclonal antibodies against the hemagglutinin of H9
subtype of avian influenza virus]. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi.
Chinese Journal of Cellular and Molecular Immunology 20(6): 702-4. ISSN: 1007-8738.
Abstract: AIM: To prepare monoclonal antibodies (mAb)
against the hemagglutinin(HA) of H9 subtype of avian influenza virus (AIV).
METHODS: 8 week-old female BALB/c mice were immunized with the inactivated
vaccine of H9 subtype of AIV. Splenocytes from the immunized mice were fused
with Sp2/0 myeloma cells, and positive hybridoma clones were screened by
indirect ELISA and hemagglutination inhibition test (HI). The specificity of
the mAb was characterized by ELISA, HI test, indirect immunofluorescence (IF)
staining and Western blot. RESULTS: Three hybridoma cell lines named 2H1, 2A3
and 1C8 against HA of AIV H9 were obtained. The HI titers of 3 mAbs were 1 x
2(8)-1 x 2(13), and the ELISA titers were 1 x 10(-7), 1 x 10(-5) and 5 x
10(-6), respectively. The immunoglobulin subclass of all 3 mAbs was IgG1.
Western blot analysis confirmed that mAb 2H1 could recognize HA and reacted to
31 out of 32 isolates of H9 subtype of AIV. CONCLUSION: Three mAbs recognizing HA
of H9 subtype of AIV were obtained, which may provide an useful tool for the
antigenic analysis, the serological diagnosis, the epidemiological survey and
the evaluation of AIV vaccine.
Descriptors: characterization, H9, avian influenza, virus,
monoclonal antibodies, mAb, HA, AIV, subtype, ELISA, titers, vaccine.
Zhang, Z.Z., W.S. Hong, and K.S. Li (2004). Cloning
and construction of prokaryotic expression vector of NS1 gene of influenza A
virus. Virologica Sinica 19(5): 449-453. ISSN: 1003-5125.
NAL
Call Number: QR355.P5
Descriptors: SDS polyacrylamide gel electrophoresis
analysis, SDS page analysis, Western blot analysis, affinity chromatography,
prokaryotic expression vector construction, reverse transcription polymerase
chain reaction, RT PCR, scan analysis, sequence analysis, pGEX-4T-3 vector,
pGEX-4T-3, NS1 cDNA plasmid.
Zhdanov, V.M. (1966). The third type of
nucleic-acid-directed protein synthesis. Lancet 1(7445):
1017-8. ISSN: 0140-6736.
NAL
Call Number: 448.8 L22
Descriptors: nucleic acids biosynthesis, nucleoproteins
biosynthesis, orthomyxoviridae metabolism, RNA viral biosynthesis, carbon
isotopes, dactinomycin pharmacology, influenza A virus avian metabolism,
Newcastle disease virus metabolism, nucleosides, parainfluenza virus 1, human
metabolism, tissue culture, tritium, uridine.
Zhirnov, O. and A.G. Bukrinskaya (1984). Nucleoproteins
of animal influenza viruses, in contrast to those of human strains, are not
cleaved in infected cells. Journal of General Virology 65(Pt. 6):
1127-34. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: We previously reported that nucleoproteins
(NPs) of human influenza viruses are cleaved in infected cells and, as a
result, two forms of NP, uncleaved (mol. wt. 56000) and cleaved (mol. wt. 53000)
were accumulated late in infection. Here, we report that NPs of animal
influenza viruses of non-human origin (isolated from pigs, equids, seals,
whales, birds) exhibited proteolytic resistance in infected cells and did not
undergo a change in mol. wt. in the course of infection. The resistance of the
animal virus NPs to proteolytic cleavage was shown to be a virus-specific
property and not the consequence of a low level of proteolysis in infected
cells. Influenza A/H3N2 viruses isolated from swine in Hong Kong in 1976 were
found to have a cleavable NP like that of 'human' viruses, supporting the
hypothesis concerning the 'human' origin of these strains. The NP of human
influenza virus (A/Aichi/2/68) adapted to an animal host (mouse) retained
susceptibility to limited intracellular proteolysis. Thus, NP resistance to
cleavage seems to be a stable viral characteristic enabling the NP56 ---- NP53
modification to be used as an indication of the origin of influenza viruses.
Descriptors: influenza microbiology, influenza A virus
human metabolism, nucleoproteins metabolism, orthomyxoviridae metabolism, viral
proteins metabolism, chick embryo, influenza metabolism, avian metabolism,
porcine metabolism, peptide hydrolases metabolism, peptides analysis, peptides
metabolism, virus cultivation.
Zhirnov, O.P. and A.G. Bukrinskaia (1983). Razlichie
shtammov virusa grippa po intensivnosti proteoliticheskoi modifikatsii
osnovnogo nukleokapsidnogo belka NP56 K NP53 v zarazhennykh kletkakh. [Difference
in influenza virus strains in the intensity of the proteolytic modification of
the base nucleocapsid protein NP56 to NP53 in infected cells]. Voprosy
Virusologii (3): 273-8. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Proteolytic cleavage of NP56 leads to NP53
protein of various influenza virus strains of human, avian, and animal origin
in tissue culture was studied. A considerable portion of NP virus protein
synthesized in human influenza virus-infected cells was modified by cellular proteases,
and as early as 10 hours postinfection both intact (NP56) and cleaved (NP53)
protein could be found in the cells. No proteolytic modification of NP protein
was demonstrated in cells infected with 11 avian and animal influenza virus
strains under study. Even 24 hours postinfection the cells contained intact
(NP56) protein alone. Different resistance of NP protein of virus strains to
cellular proteases allows the phenomenon of proteolytic modification of the
nucleocapsid protein NP56 leads to NP53 to be used as a genetic marker of
influenza virus strains.
Descriptors: capsid metabolism, influenza enzymology,
influenza A virus metabolism, peptide hydrolases metabolism, viral proteins
metabolism, capsid analysis, chick embryo, electrophoresis, polyacrylamide gel,
avian metabolism, human metabolism, virus cultivation.
Zhirnov, O.P., T.E. Konakova, W. Garten, and H. Klenk
(1999). Caspase-dependent N-terminal cleavage of influenza virus
nucleocapsid protein in infected cells. Journal of Virology 73(12):
10158-63. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The nucleocapsid protein (NP) (56 kDa) of
human influenza A viruses is cleaved in infected cells into a 53-kDa form.
Likewise, influenza B virus NP (64 kDa) is cleaved into a 55-kDa protein with a
62-kDa intermediate (O. P. Zhirnov and A. G. Bukrinskaya, Virology 109:174-179,
1981). We show now that an antibody specific for the N terminus of influenza A
virus NP reacted with the uncleaved 56-kDa form but not with the truncated NP53
form, indicating the removal of a 3-kDa peptide from the N terminus. Amino acid
sequencing revealed the cleavage sites ETD16*G for A/Aichi/68 NP and sites
DID7*G and EAD61*V for B/Hong Kong/72 NP. With D at position -1, acidic amino
acids at position -3, and aliphatic ones at positions -2 and +1, the NP
cleavage sites show a recognition motif typical for caspases, key enzymes of
apoptosis. These caspase cleavage sites demonstrated evolutionary stability and
were retained in NPs of all human influenza A and B viruses. NP of avian
influenza viruses, which is not cleaved in infected cells, contains G instead
of D at position 16. Oligopeptide DEVD derivatives, specific caspase
inhibitors, were shown to prevent the intracellular cleavage of NP. All three
events, the NP cleavage, the increase of caspase activity, and the development
of apoptosis, coincide in cells infected with human influenza A and B viruses.
The data suggest that intracellular cleavage of NP is exerted by host caspases
and is associated with the development of apoptosis at the late stages of
infection.
Descriptors: caspases metabolism, influenza A virus human
metabolism, influenza B virus metabolism, nucleocapsid proteins metabolism,
amino acid sequence, apoptosis, caspases antagonists and inhibitors, cell line,
dogs, molecular sequence data, oligopeptides pharmacology, swine.
Zhirnov, O.P., A.V. Ovcharenko, A.G. Bukrinskaia,
and V.M. Zhdanov (1983). Ingibitory proteaz blokiruiut disseminatsiiu virusa
grippa v organizme zarazhennykh zhivotnykh. [Protease inhibitors block the
spread of the influenza virus in the body of infected animals]. Doklady
Akademii Nauk SSSR 270(6): 1483-5.
ISSN: 0002-3264.
NAL
Call Number: 511 P444A
Descriptors: chickens, fowl plague drug therapy, influenza
A virus avian drug effects, protease inhibitors therapeutic use, chick embryo,
drug evaluation, preclinical, fowl plague microbiology, avian growth and
development, time factors, virus activation drug effects.
Zhou, N.N., D.A. Senne, J.S. Landgraf, S.L. Swenson,
G. Erickson, K. Rossow, L. Liu, K. Yoon, S. Krauss, and R.G. Webster (1999). Genetic reassortment
of avian, swine, and human influenza A viruses in American pigs. Journal
of Virology 73(10): 8851-6. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: In late summer through early winter of 1998,
there were several outbreaks of respiratory disease in the swine herds of North
Carolina, Texas, Minnesota, and Iowa. Four viral isolates from outbreaks in
different states were analyzed genetically. Genotyping and phylogenetic
analyses demonstrated that the four swine viruses had emerged through two
different pathways. The North Carolina isolate is the product of genetic
reassortment between H3N2 human and classic swine H1N1 influenza viruses, while
the others arose from reassortment of human H3N2, classic swine H1N1, and avian
viral genes. The hemagglutinin genes of the four isolates were all derived from
the human H3N2 virus circulating in 1995. It remains to be determined if either
of these recently emerged viruses will become established in the pigs in North
America and whether they will become an economic burden.
Descriptors: genome, viral, influenza A virus avian
genetics, human genetics, porcine genetics, reassortant viruses, amino acid
sequence, birds virology, molecular sequence data, swine virology.
Zilske, E., R. Sinnecker, and H. Sinnecker (1981). Neuraminidasehemmende
Antikorper gegen aviare Influenzabirus- Subtypen in Humanseren.
[Neuraminidase-Inhibiting Antibodies to Avian Influenza Virus Subtypes in Human
Sera (author's transl)]. Zentralblatt Fur Bakteriologie, Mikrobiologie
Und Hygiene. 1. Abt. Originale A, Medizinische Mikrobiologie,
Infektionskrankheiten Und Parasitologie
International Journal of Microbiology and Hygiene. A 250(1-2): 34-41. ISSN: 0174-3031.
NAL
Call Number: 448.3 C33 (1)
Abstract: 400 human sera were tested both in
hemagglutination inhibition (HI) and neuraminidase inhibition (NI) tests for
antibodies to avian and animal influenza virus subtypes. In the H1 test we only
found antibodies to the avian subtype Hav 7 and the animal subtypes Hsw 1 and
Heq 2 whereby the latter was mainly demonstrated in elderly persons 60 to 100
years old. The findings of Hav 7 are due to H 3 antibodies and reflect the
relationship between both antigens. In the NI test we obtained positive results
in 21.8% of the human sera with the neuraminidase subtype N 3 (Nav 2/3) with a
peak in persons who were 60 to 70 years old. 11.0% of the sera contained
antibodies to the neuraminidase subtype N 8 (Neq 2) and were found exclusively
in people 60 to 100 years old, and 9.3% of sera showed positive reactions with
the subtype N5 (Nav 5). Until now an immunological relationship between the
neuraminidase subtypes N 1, N 2, and N 3 is not known, and could'nt be found in
our own studies. Contaminations of antigens can also be excluded. The possible
origin of these antibodies to avian neuraminidase subtypes is discussed.
Descriptors: antibodies, viral analysis, influenza A virus
avian immunology, neuraminidase immunology, adolescent, adult, aged, child,
preschool, Germany, East, hemagglutination inhibition tests, infant, porcine
immunology, middle aged, serologic tests methods.
Zopel, P., E. Tonew, and H. Ulbricht (1978). Elektronenoptische
Untersuchungen zur Wirkung von
1-[p-(Methylnitrosamino)-benzylidenamino]-adamantan auf das Fowl-Plague-Virus
(FPV) in Zellkultur. [Electronoptical studies of the effect of
1-[p-(methylnitrosamino)-benzylidenamino]-adamantane on the fowl plague virus
(FPV) in cell culture]. Zeitschrift Fur Allgemeine Mikrobiologie
18(7): 501-10. ISSN: 0044-2208.
NAL
Call Number: QR1.Z4
Abstract: The adamantanamine derivative
1-[p-(methylnitrosamino)-benzylidenamino]-adamantane (MBAA) at a concentration
of 40 microgram/ml demonstrated no effect on adsorption of fowl plague virus
(FPV) on chick embryonal cells. The penetration of the virions took place by
means of pinocytosis. In the final stages of penetration the virions became
gradually disintegrated. Under the influence of MBAA, after break-down of the
membrane of pinocytic vesicles a swollen part of the virus core remained in
cytoplasm. The morphologically visible replication stages were completely
blocked by MBAA. From these results it was concluded that the antiviral action
of MBAA most probably depends on a block of virus replication between the final
stages of the penetration process and the beginning of production of virus
specific structural antigens.
Descriptors: adamantane pharmacology, bridged compounds
pharmacology, influenza A virus avian drug effects, nitrosamines pharmacology,
adamantane analogs and derivatives, adsorption, cell membrane microbiology,
cell nucleus microbiology, chick embryo, cytoplasm microbiology, avian growth
and development, avian ultrastructure, pinocytosis, tissue culture, virus
replication drug effects.
Zuev, V.A., E.P. Mirchink, V.V. Peters, and E.A.
Isaeva (1975). Prostoi sposob prigotovleniia poluzhidkoi sredy pokrytiia s
metiltselliulozoi dlia opredeleniia bliashkoobrazuiushchei sposobnosti virusov [Simple
method of preparation of a semifluid coating medium with methylcellulose for
the determination of the plaque-forming abilities of viruses]. Laboratornoe
Delo (1): 56-7. ISSN: 0023-6748.
Descriptors: methylcellulose, plaque assay methods,
viruses isolation and purification, influenza A virus avian isolation and
purification, vaccinia virus isolation and purification.
Zuev, V.A., E.P. Mirchink, V.K. Vishnichenko, N.B.
Azadova, and L.M. Mentkevich (1974). Priroda i mekhaniz, virusnogo
persistirovaniia v kul'turakh kletok, latentno infitsirovannykh virusom grippa
ptits [Nature and mechanism of viral persistence in cell cultures latently
infected by the avian influenza virus]. Voprosy Virusologii (4):
450-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: cultured cells microbiology, influenza A
virus avian pathogenicity, centrifugation, density gradient, chick embryo,
clone cells microbiology, fibroblasts microbiology, fluorescent antibody
technique, avian isolation and purification, interferons analysis, l cells cell
line microbiology, nucleoproteins analysis, RNA viral analysis, time factors,
virus cultivation, virus replication.