Search Antibody Database

Found 21 matching records:

Displaying record number 944

MAb ID	1334-D (1334, 1334D)
HXB2 Location	gp160(303-307)	gp160 Epitope Map
Author Location	gp120( HIV451)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`TRTSV`	Epitope Alignment
Subtype	CRF01_AE
Ab Type	gp120 V3
Neutralizing
Species (Isotype)	human(IgG1κ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, review, subtype comparisons, variant cross-recognition or cross-neutralization

Notes

1334-D: Called 1334. V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using HIV451 gp120. Gorny2004 (antibody binding site definition and exposure)
1334-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
1334-D: Called 1334D -- A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 1334D showed intermediate cross-reactivity. Nyambi2000 (subtype comparisons)
1334-D: Called 1334 -- binds to V3 peptides from MN, SF2, NY5, RF, and CDC4 strains as well as x-reactivity with peptides from A, C, D, F, G, and H subtypes -- was suggested to be IgG1lambda here -- binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- V3 MAbs 447-52D, 838-D, and 1334 bound with a 7-10 fold preference for the oligomer. Gorny2000b (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization, subtype comparisons)
1334-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
1334-D: This MAb was selected using oligomeric gp160 from HIV451. Zolla-Pazner1999b (antibody generation)

References

Zolla-Pazner1999b S. Zolla-Pazner, M. K. Gorny, and P. N. Nyambi. The implications of antigenic diversity for vaccine development. Immunol. Lett., 66:159-64, 1999. PubMed ID: 10203049. Show all entries for this paper.

Zolla-Pazner1999a S. Zolla-Pazner, M. K. Gorny, P. N. Nyambi, T. C. VanCott, and A. Nadas. Immunotyping of human immunodeficiency virus type 1 (HIV): an approach to immunologic classification of HIV. J. Virol., 73:4042-51, 1999. 21 human anti-V3 MAbs were studied with respect to cross-clade reactivity and immunological relationship to other human anti-V3 MAbs. Broad cross-reactivities were observed, and V3 peptides were grouped into immunotypes that contained peptides from several clades. PubMed ID: 10196300. Show all entries for this paper.

Gorny2000b M. K. Gorny, T. C. VanCott, C. Williams, K. Revesz, and S. Zolla-Pazner. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. Virology, 267:220-8, 2000. PubMed ID: 10662617. Show all entries for this paper.

Nyambi2000 P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus type 1 virions of group M. J. Virol., 74:7096-107, 2000. PubMed ID: 10888650. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Gorny2004 Miroslaw K. Gorny, Kathy Revesz, Constance Williams, Barbara Volsky, Mark K. Louder, Christopher A. Anyangwe, Chavdar Krachmarov, Samuel C. Kayman, Abraham Pinter, Arthur Nadas, Phillipe N. Nyambi, John R. Mascola, and Susan Zolla-Pazner. The V3 Loop is Accessible on the Surface of Most Human Immunodeficiency Virus Type 1 Primary Isolates and Serves as a Neutralization Epitope. J. Virol., 78(5):2394-2404, Mar 2004. PubMed ID: 14963135. Show all entries for this paper.

Displaying record number 941

MAb ID	1324-E (1324E)
HXB2 Location	gp160(303-308)	gp160 Epitope Map
Author Location	Env( subtype CRF01)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`TRTSVR`	Epitope Alignment
Subtype	CRF01_AE
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1κ)
Immunogen	HIV-1 infection
Keywords	antibody generation, review, subtype comparisons, variant cross-recognition or cross-neutralization

Notes

1324-E: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
1324-E: Called 1324E -- A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 1324E showed poor cross-reactivity, and was the only MAb tested that was derived from a non-B clade infected patient, an E clade infection was the source of 1324E. Nyambi2000 (subtype comparisons)
1324-E: MAb reacted with peptides from E clade, while B clade derived MAbs could not. Zolla-Pazner1999a (subtype comparisons)
1324-E: E clade stimulated MAb did not cross-react with B clade peptides nor did B clade derived peptides with an E clade V3 loop, but both E and B clade stimulated Abs can cross-react with some peptides from other clades -- this Ab showed strong binding to several E, A and F peptides, one C peptide, and no reactivity with B peptides and most D peptides. Zolla-Pazner1999b (subtype comparisons)
1324-E: A human MAb was derived from an HIV-1 E clade infection from a US service man who had served in Thailand, selected with the consensus V3 peptide from clade E -- cross-reactive with V3 peptides, and gp120 from E, C and A clades, as well as cells infected with a C-clade primary isolate, but not with B and D clade V3 peptides or rgp120 -- neutralizes E clade virus adapted for growth in H9 cells, but not 5 primary E clade isolates, including the autologous isolate -- kinetic parameters were measured, 1324E was comparable to 447-52D. Gorny1998 (antibody generation, variant cross-recognition or cross-neutralization, subtype comparisons)

References

Gorny1998 M. K. Gorny, J. R. Mascola, Z. R. Israel, T. C. VanCott, C. Williams, P. Balfe, C. Hioe, S. Brodine, S. Burda, and S. Zolla-Pazner. A human monoclonal antibody specific for the V3 loop of HIV type 1 clade E cross-reacts with other HIV type 1 clades. AIDS Res. Hum. Retroviruses, 14:213-21, 1998. PubMed ID: 9491911. Show all entries for this paper.

Displaying record number 475

MAb ID	412-D (412-10D, 412, 412D)
HXB2 Location	gp160(304-320)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1κ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, binding affinity, complement, kinetics, review, subtype comparisons, vaccine antigen design, variant cross-recognition or cross-neutralization

Notes

412-D: Called 412: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
412-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
412-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 412-D showed limited reactivity. Nyambi2000 (subtype comparisons)
412-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 391.5, 412 and 418, all selected with MN V3 peptide -- the core amino acids HIGPGR tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
412-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
412-D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- 412-D was bound only to B clade virions and to D clade MAL. Nyambi1998 (subtype comparisons)
412-D: Kinetic parameters were measured, and the association rates were similar, but dissociation rate constants were quite variable for V3 MAbs, 412-D has a relatively fast dissociation, thus low affinity among V3 MAbs. Gorny1998 (kinetics)
412-D: Called 412 -- The tip of the V3 loop was presented in a mucin backbone -- higher valency correlates with higher affinity constant. Fontenot1995 (vaccine antigen design, binding affinity)
412-D: Called 412-10D -- relatively rapid dissociation and weak homologous neutralization. VanCott1994 (binding affinity)
412-D: Mediated deposition of complement component C3 on HIV infected cells, enhanced by second Ab binding, rabbit anti-human IgG. Spear1993 (complement)
412-D: Neutralizes MN, does not bind SF2 or HXB2 -- not reactive with hexa or heptapeptides by Pepscan. Gorny1993 (variant cross-recognition or cross-neutralization)

References

Gorny1993 M. K. Gorny, J.-Y. Xu, S. Karwowska, A. Buchbinder, and S. Zolla-Pazner. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J. Immunol., 150:635-643, 1993. Characterizaton of 12 human MAbs that bind and neutralize the MN isolate with 50% neutralization. Two of these antibodies also bound and neutralized IIIB: 447-52-D and 694/98-D; all others could not bind HXB2 peptides. All but two, 418-D and 412-D could bind to SF2 peptides. PubMed ID: 7678279. Show all entries for this paper.

Spear1993 G. T. Spear, D. M. Takefman, B. L. Sullivan, A. L. Landay, and S. Zolla-Pazner. Complement activation by human monoclonal antibodies to human immunodeficiency virus. J. Virol., 67:53-59, 1993. This study looked at the ability of 16 human MAbs to activate complement. MAbs directed against the V3 region could induce C3 deposition on infected cells and virolysis of free virus, but antibodies to the CD4BS and C-terminal region and two regions in gp41 could induce no complement mediated effects. Pre-treatment with sCD4 could increase complement-mediated effects of anti-gp41 MAbs, but decreased the complement-mediated effects of V3 MAbs. Anti-gp41 MAbs were able to affect IIIB but not MN virolysis, suggesting spontaneous shedding of gp120 on IIIB virions exposes gp41 epitopes. IgG isotype did not appear to have an effect on virolysis or C3 deposition. PubMed ID: 7677959. Show all entries for this paper.

VanCott1994 T. C. VanCott, F. R. Bethke, V. R. Polonis, M. K. Gorny, S. Zolla-Pazner, R. R. Redfield, and D. L. Birx. Dissociation rate of antibody-gp120 binding interactions is predictive of V3-mediated neutralization of HIV-1. J. Immunol., 153:449-459, 1994. Using surface plasmon resonance it was found that the rate of the dissociation of the MAb-gp120 complex, but not the association rate, correlated with MAbs ability to neutralize homologous virus (measured by 50% inhibition of p24 production). Association constants were similar for all MAbs tested, varying less than 4-fold. Dissociation rate constants were quite variable, with 100-fold differences observed. PubMed ID: 7515931. Show all entries for this paper.

Fontenot1995 J. D. Fontenot, T. C. VanCott, B. S. Parekh, C. P. Pau, J. R. George, D. L. Birx, S. Zolla-Pazner, M. K. Gorny, and J. M. Gatewood. Presentation of HIV V3 loop epitopes for enhanced antigenicity, immunogenicity and diagnostic potential. AIDS, 9:1121-1129, 1995. PubMed ID: 8519447. Show all entries for this paper.

Nyambi1998 P. N. Nyambi, M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. Mapping of epitopes exposed on intact human immunodeficiency virus type 1 (HIV-1) virions: a new strategy for studying the immunologic relatedness of HIV-1. J. Virol., 72:9384-91, 1998. 18 human MAbs binding to gp120 and gp41 were tested using a novel assay to test binding to intact HIV-1 virions. The new method involves using MAbs to the host proteins incorporated into virions to bind them to ELIZA plates. Antigenic conservation in epitopes of HIV-1 in clades A, B, D, F, G, and H was studied. MAbs were selected that were directed against V2, V3, CD4bd, C5 or gp41 regions. Antibodies against V2, the CD4BS, and sp41 showed weak and sporadic reactivities, while binding strongly to gp120, suggesting these epitopes are hidden when gp120 is in its native, quaternary structure. PubMed ID: 9765494. Show all entries for this paper.

Displaying record number 467

MAb ID	257-D (257, 257-2-D-IV, 257-D-IV, 257, 257-2D, 257D, ARP3023)
HXB2 Location	gp160(305-309)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KRIHI`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody interactions, antibody sequence variable domain, assay development, binding affinity, co-receptor, complement, dendritic cells, enhancing activity, kinetics, neutralization, review, subtype comparisons, vaccine antigen design, vaccine-specific epitope characteristics, variant cross-recognition or cross-neutralization

Notes

257-D IV: This Ab was shown to inhibit HIV-1 BaL replication in macrophages but not in PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication occurs by an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles. Holl2006 (neutralization, dendritic cells)
257-D: Called 257: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides do not show as much ability to neutralize as V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 257 was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
257-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
257-D: NIH AIDS Research and Reference Reagent Program: 1510.
257-D: UK Medical Research Council AIDS reagent: ARP3023.
257-D: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002 (variant cross-recognition or cross-neutralization)
257-D: Called ARP3023: Herpesvirus saimiri-immortalized CD4+ T lymphocytes (HVS T cells) were used to isolate virus and perform HIV-1 neutralization assays, and compared with a standard PBMC protocol -- neutralization sensitivities to a panel of MAbs and to homologous or heterologous plasma/sera were similar for HVS T cells (CN-2 cells) and PBMCs. Vella2002 (assay development)
257-D: Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding. York2001
257-D: Called 257D -- six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes. Park2000
257-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 257-D showed intermediate reactivity. Nyambi2000 (subtype comparisons)
257-D: Study of a live-vector mucosal vaccine that expresses HIV-1 V3 domains using the bacterium Streptococcus gordonii which can express heterologous Ag and can colonize the oral cavity and vagina of mice -- 268-D and 257-D recognized S. gordonii expressing the V3 domain of MN -- the vaccine stimulated V3-specific IgG2a in mice. Oggioni1999 (vaccine antigen design)
257-D: rgp120 derived from a R5X4 subtype B virus, HIV-1 W61D, was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- 257-D bound rgp120 W61D but could only neutralize the W61D isolate following T-cell line adaptation. Beddows1999 (vaccine antigen design, variant cross-recognition or cross-neutralization, vaccine-specific epitope characteristics)
257-D: MAb peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
257-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
257-D: Called 257D -- deleting the V2 loop of neutralization-resistant HIV-1 isolate SF162 does not abrogate its replication in PBMC or macrophages, but it enhances its neutralization sensitivity to sera from patients with B clade infection up to 170-fold, and also enhances sensitivity to sera from clades A through F -- deletion of V1 or V2 did not enable neutralization by V3 MAbs 391-95D or 257D. Stamatatos1998 (vaccine antigen design, subtype comparisons)
257-D: Kinetic parameters were measured, and the association rates were similar, but dissociation rate constants were quite variable for V3 MAbs, 257-D has a slow dissociation, thus the highest affinity among V3 MAbs. Gorny1998 (kinetics, binding affinity)
257-D: A neutralization assay was developed based on hemi-nested PCR amplification of the LTR (HNPCR) -- LTR-HNPCR consistently revealed HIV DNA and was shown to be a rapid, specific and reliable neutralization assay based on tests with 6 MAbs and 5 isolates. Yang1998 (assay development)
257-D: A T-cell line-adapted (TCLA) derivative of SI primary isolate 168P acquired the ability to be neutralized by anti-V3 MAbs -- the primary isolate could use either CCR5 or CXCR4, and was not neutralized when infection was directed via either pathway, however the TCLA derivative uses CXCR4 only and is neutralized. LaCasse1998 (co-receptor, variant cross-recognition or cross-neutralization)
257-D: Called 257 -- gp120 can inhibit MIP-1alpha from binding to CCR5, but this inhibitory effect is blocked by pre-incubation of gp120 with three anti-V3 MAbs: 447, 257, 1027 -- MAb 670 which binds in the C5 region had no effect. Hill1997 (antibody binding site definition and exposure, co-receptor)
257-D: Binds less extensively than MAb 391-95D on the surface of HIV-1 isolates SF162 and SF128A -- neutralizes less potently than 391-95D -- stronger neutralization of primary macrophage targets than PBMC. Stamatatos1997 (variant cross-recognition or cross-neutralization)
257-D: Neutralized (>90%) an SI-env chimeric virus and enhanced (>200%) an NSI-env chimeric virus. Schutten1997 (enhancing activity, variant cross-recognition or cross-neutralization)
257-D: IIIB neutralizing MAbs in vitro fail to neutralize in a mouse model in vivo. Schutten1996
257-D: 257-D is V H5 -- V-region heavy chain usage was examined and a bias of enhanced V H1 and V H4, and reduced V H3, was noted among HIV infected individuals. Wisnewski1996 (antibody sequence variable domain)
257-D: Comparable affinity for SI and NSI viruses, in contrast to MAb MN215. Schutten1995a (variant cross-recognition or cross-neutralization)
257-D: Only inhibition of SI phenotype virus, and strong enhancement of NSI phenotype chimeric viruses, that incorporated different envs from the same donor. Schutten1995 (enhancing activity, variant cross-recognition or cross-neutralization)
257-D: In serotyping study using flow-cytometry, bound only to virus with KRIHI. Zolla-Pazner1995 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
257-D: Called 257-D-IV -- could neutralize MN and closely related JRCSF, but not 2 B subtype and 1 D subtype primary isolates in a multi-laboratory study involving 11 labs. DSouza1995 (variant cross-recognition or cross-neutralization, subtype comparisons)
257-D: The binding of conformation-dependent anti-V2, anti-V3, and anti-CD4BS MAbs to monomeric and virion-associated gp120 from HIV-1 isolates with differences in cell tropism was studied -- V3 loop epitopes were less accessible to Ab binding on the virion surface than in the gp120 monomer, particularly for macrophage-tropic isolates SF162 and SF128a, relative to T-cell tropic SF2 -- sCD4 association with gp120 better revealed this V3 epitope on TCLA SF2 and dual tropic (MU3) viruses than on macrophage tropic isolates. Stamatatos1995 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
257-D: Potent MN neutralization, slow dissociation constant. VanCott1994 (binding affinity)
257-D: Included a multi-lab study for antibody characterization and assay comparison -- best NAb against MN, but not IIIB. DSouza1994 (variant cross-recognition or cross-neutralization)
257-D: Mediated deposition of complement component C3 on HIV infected cells, enhanced by second Ab binding, rabbit anti-human IgG -- complement mediated virolysis of MN, but not in the presence of sCD4. Spear1993 (complement)
257-D: Additive MN or SF2 neutralization when combined with CD4 binding site MAb F105 -- does not neutralize RF. Cavacini1993 (antibody interactions, variant cross-recognition or cross-neutralization)
257-D: Neutralizes MN -- binds SF2: epitope KSIYI -- specificity: MN, SF2, NY5, RF. Gorny1993 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
257-D: Reacts with MN, NY5, CDC4 and SF2, does not cross-react with RF, WM52, or HXB2. Karwowska1992a (variant cross-recognition or cross-neutralization)
257-D: Called 257-2-D-IV -- potent neutralizing MAb. DSouza1991

References

Gorny1991 M. K. Gorny, J.-Y. Xu, V. Gianakakos, S. Karwowska, C. Williams, H. W. Sheppard, C. V. Hanson, and S. Zolla-Pazner. Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus type 1 envelope glycoprotein. Proc. Natl. Acad. Sci. U.S.A., 88:3238-3242, 1991. PubMed ID: 2014246. Show all entries for this paper.

DSouza1991 M. P. D'Souza, P. Durda, C. V. Hanson, G. Milman, and Collaborating Investigators. Evaluation of monoclonal antibodies to HIV-1 by neutralization and serological assays: an international collaboration. AIDS, 5:1061-1070, 1991. PubMed ID: 1718320. Show all entries for this paper.

Karwowska1992a S. Karwowska, M. K. Gorny, A. Buchbinder, and S. Zolla-Pazner. Type-specific human monoclonal antibodies cross-react with the V3-loop of various HIV-1 isolates. Vaccines 92, :171-174, 1992. Editors: F. Brown, H. S. Ginsberg and R. Lerner, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Show all entries for this paper.

Cavacini1993 L. A. Cavacini, C. L. Emes, J. Power, A. Buchbinder, S. Zolla-Pazner, and M. R. Posner. Human monoclonal antibodies to the V3 loop of HIV-1 gp120 mediate variable and distinct effects on binding and viral neutralization by a human monoclonal antibody to the CD4 binding site. J. Acquir. Immune Defic. Syndr., 6:353-358, 1993. PubMed ID: 8455141. Show all entries for this paper.

DSouza1994 M. P. D'Souza, S. J. Geyer, C. V. Hanson, R. M. Hendry, G. Milman, and Collaborating Investigators. Evaluation of monoclonal antibodies to HIV-1 envelope by neutralization and binding assays: an international collaboration. AIDS, 8:169-181, 1994. PubMed ID: 7519019. Show all entries for this paper.

Stamatatos1995 L. Stamatatos and C. Cheng-Mayer. Structural modulations of the envelope gp120 glycoprotein of human immunodeficiency virus type 1 upon oligomerization and the differential V3 loop epitope exposure of isolates displaying distinct tropism upon viral-soluble receptor binding. J. Virol., 69:6191-6198, 1995. PubMed ID: 7545244. Show all entries for this paper.

DSouza1995 M. P. D'Souza, G. Milman, J. A. Bradac, D. McPhee, C. V. Hanson, and R. M. Hendry. Neutralization of primary HIV-1 isolates by anti-envelope monoclonal antibodies. AIDS, 9:867-874, 1995. Eleven labs tested the 6 human MAbs 1125H, TH9, 4.8D, 257-D-IV, TH1, 2F5, and also HIVIG for neutralization of MN, JRCSF, the two B clade primary isolates 301657 and THA/92/026, and the D clade isolate UG/92/21. 2F5 was the most broadly neutralizing, better than HIVIG. The other MAbs showed limited neutralization of only MN (anti-CD4BS MAbs 1125H, TH9, and 4.8D), or MN and JRCSF (anti-V3 MAbs 257-D-IV and TH1). PubMed ID: 7576320. Show all entries for this paper.

Zolla-Pazner1995 S. Zolla-Pazner, J. O'Leary, S. Burda, M. K. Gorny, M. Kim, J. Mascola, and F. McCutchan. Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry. J. Virol., 69:3807-3815, 1995. A set of 13 human MAbs to a variety of epitopes were tested against a panel of primary isolates of HIV-1, representing different genetic clades. The V3 loop tended to be B clade restricted, and a single gp120 C-terminus binding antibody was clade specific. Two other gp120 C-terminus binding antibodies were group specific. PubMed ID: 7745728. Show all entries for this paper.

Schutten1995 M. Schutten, A. C. Andeweg, M. L. Bosch, and A. D. Osterhaus. Enhancement of Infectivity of a Non-Syncytium Inducing HIV-1 by sCD4 and by Human Antibodies that Neutralize Syncytium Inducing HIV-1. Scand. J. Immunol., 41:18-22, 1995. PubMed ID: 7824885. Show all entries for this paper.

Schutten1995a M. Schutten, J. P. Langedijk, A. C. Andeweg, R. C. Huisman, R. H. Meloen, and A. D. Osterhaus. Characterization of a V3 domain-specific neutralizing human monoclonal antibody that preferentially recognizes non-syncytium-inducing human immunodeficiency virus type 1 strains. J. Gen. Virol., 76:1665-1673, 1995. Characterization of HuMAb MN215. PubMed ID: 9049372. Show all entries for this paper.

Wisnewski1996 A. Wisnewski, L. Cavacini, and M. Posner. Human antibody variable region gene usage in HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 11:31-38, 1996. PubMed ID: 8528730. Show all entries for this paper.

Schutten1996 M. Schutten, K. Tenner-Racz, P. Racz, D. W. van Bekkum, and A. D. Osterhaus. Human antibodies that neutralize primary human immunodeficiency virus type 1 in vitro do not provide protection in an in vivo model. J. Gen. Virol., 77:1667-75, Aug 1996. PubMed ID: 8760413. Show all entries for this paper.

Schutten1997 M. Schutten, A. C. Andeweg, G. F. Rimmelzwaan, and A. D. Osterhaus. Modulation of primary human immunodeficiency virus type 1 envelope glycoprotein-mediated entry by human antibodies. J. Gen. Virol., 78:999-1006, 1997. A series of HIV-1 envelope glycoproteins from related primary virus isolates of different SI phenotypes, together with chimeras of these proteins, were tested in an envelope trans-complementation assay for their sensitivity to either antibody mediated inhibition or enhancement of HIV-1 entry. In contrast to the inhibition of HIV-1 entry, antibody mediated enhancement was not temperature dependent and could not be mediated by F(ab) fragments, implicating cross-linking as an important step. Enhancement or inhibition seemed to be determined by virus isolate rather than by the specificity of the antiserum used. 2F5 was the only MAb that inhibited the entry of all viruses. PubMed ID: 9152416. Show all entries for this paper.

Stamatatos1997 L. Stamatatos, S. Zolla-Pazner, M. K. Gorny, and C. Cheng-Mayer. Binding of antibodies to virion-associated gp120 molecules of primary-like human immunodeficiency virus type 1 (HIV-1) isolates: effect on HIV-1 infection of macrophages and peripheral blood mononuclear cells. Virology, 229:360-9, 1997. PubMed ID: 9126249. Show all entries for this paper.

Hill1997 C. M. Hill, H. Deng, D. Unutmaz, V. N. Kewalramani, L. Bastiani, M. K. Gorny, S. Zolla-Pazner, and D. R. Littman. Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor. J. Virol., 71:6296-6304, 1997. PubMed ID: 9261346. Show all entries for this paper.

Hioe1997b C. E. Hioe, S. Xu, P. Chigurupati, S. Burda, C. Williams, M. K. Gorny, and S. Zolla-Pazner. Neutralization of HIV-1 Primary Isolates by Polyclonal and Monoclonal Human Antibodies. Int. Immunol., 9(9):1281-1290, Sep 1997. PubMed ID: 9310831. Show all entries for this paper.

LaCasse1998 R. A. LaCasse, K. E. Follis, T. Moudgil, M. Trahey, J. M. Binley, V. Planelles, S. Zolla-Pazner, and J. H. Nunberg. Coreceptor utilization by human immunodeficiency virus type 1 is not a primary determinant of neutralization sensitivity. J. Virol., 72:2491-5, 1998. A T-cell line-adapted (TCLA) derivative of SI primary isolate 168P acquired the ability to to be neutralized by anti-V3 MAbs 257-D, 268-D and 50.1. The primary isolate could use either CCR5 or CXCR4, and was not neutralized when infection was directed via either pathway, but the TCLA derivative uses CXCR4 only and is neutralized. Thus coreceptor usage is not the primary determinant of differential neutralization sensitivity in primary versus TCLA strains. PubMed ID: 9499111. Show all entries for this paper.

Yang1998 G. Yang, M. P. D'Souza, and G. N. Vyas. Neutralizing antibodies against HIV determined by amplification of viral long terminal repeat sequences from cells infected in vitro by nonneutralized virions. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 17:27-34, 1998. A neutralization assay was developed based on heminested PCR amplification of the LTR (HNPCR) -- LTR-HNPCR consistently revealed HIV DNA and was shown to be a rapid, specific and reliable neutralization assay based on tests with 6 MAbs and 5 HIV isolates. PubMed ID: 9436755. Show all entries for this paper.

Stamatatos1998 L. Stamatatos and C. Cheng-Mayer. An envelope modification that renders a primary, neutralization- resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades. J. Virol., 72:7840-5, 1998. PubMed ID: 9733820. Show all entries for this paper.

Beddows1999 S. Beddows, S. Lister, R. Cheingsong, C. Bruck, and J. Weber. Comparison of the antibody repertoire generated in healthy volunteers following immunization with a monomeric recombinant gp120 construct derived from a CCR5/CXCR4-using human immunodeficiency virus type 1 isolate with sera from naturally infected individuals. J. Virol., 73:1740-5, 1999. PubMed ID: 9882391. Show all entries for this paper.

Oggioni1999 M. R. Oggioni, D. Medaglini, L. Romano, F. Peruzzi, T. Maggi, L. Lozzi, L. Bracci, M. Zazzi, F. Manca, P. E. Valensin, and G. Pozzi. Antigenicity and immunogenicity of the V3 domain of HIV type 1 glycoprotein 120 expressed on the surface of Streptococcus gordonii. AIDS Res. Hum. Retroviruses, 15:451-9, 1999. PubMed ID: 10195755. Show all entries for this paper.

Park2000 E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031. Show all entries for this paper.

York2001 J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697. Show all entries for this paper.

Vella2002 Cherelyn Vella, Natalie N. Zheng, Philippa Easterbrook, and Rod S. Daniels. Herpesvirus saimiri-Immortalized Human Lymphocytes: Novel Hosts for Analyzing HIV Type 1 in Vitro Neutralization. AIDS Res. Hum. Retroviruses, 18(13):933-946, 1 Sep 2002. PubMed ID: 12230936. Show all entries for this paper.

Zhang2002 Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155. Show all entries for this paper.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Displaying record number 473

MAb ID	311-11-D (311-11D, 311, 311D, 311-D)
HXB2 Location	gp160(305-313)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KRIHIGP`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, complement, review, subtype comparisons

Notes

311-11-D: Called 311: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides do not neutralize as well as V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 311 was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
311-11-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
311-11-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 311-11-D showed weak reactivity. Nyambi2000 (subtype comparisons)
311-11-D: MAb peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
311-11-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
311-11-D: Mediated deposition of complement component C3 on HIV infected cells, enhanced by second Ab binding, rabbit anti-human IgG. Spear1993 (complement)
311-11-D: Neutralizes MN -- binds SF2: KSIYIGP. Gorny1993 (antibody binding site definition and exposure, antibody generation)

References

Displaying record number 474

MAb ID	391/95-D (391-95D, 391.5, 391/95D, 391/95)
HXB2 Location	gp160(305-318)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KRIHIGPGRAFY`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1κ)
Immunogen	HIV-1 infection
Keywords	acute/early infection, antibody binding site definition and exposure, co-receptor, dendritic cells, enhancing activity, neutralization, review, subtype comparisons, vaccine antigen design, variant cross-recognition or cross-neutralization

Notes

391-D: This Ab was shown to inhibit HIV-1 BaL replication in macrophages but not in PHA-stimulated PBMCs. Holl2006 (neutralization, dendritic cells)
391/95-D: Sera from two HIV+ people and a panel of MAbs were used to explore susceptibility to neutralization in the presence or absence of glycans within or adjacent to the V3 loop and within the C2, C4 and V5 regions of HIV-1 SF162 env gp120. The loss of any of the five glycans, within the V3 loop (GM299 V3), C2 (GM292 C2), C3 (GM329 C3), C4 (GM438 C4), or V5 (GM454 V5) made SF162 become sensitive to 391/95-D; SF162 is resistant to 391/95-D neutralization. V3 glycans tended to shield V3 loop, CD4 and co-receptor MAb binding sites, while C4 and V5 glycans shielded V3 loop, CD4, gp41 but not co-receptor MAb binding sites. Selective removal of glycans from a vaccine candidate may enable greater access to neutralization susceptible epitopes. McCaffrey2004 (antibody binding site definition and exposure, vaccine antigen design)
391/95-D: Called 391/95: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides do not show as much ability to neutralize as V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 391/95 was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
391/95-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
391/95-D: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
391/95-D: The phenotype and genotype of viral env sequences were studied over a period of seroconversion in one individual -- Env trans-complementation demonstrated infectivity of clones derived pre-seroconversion were not influenced by MAb 391/95-D, but post-seroconversion clones were enhanced in the presence of 391/95-D, although the V3 binding region was unchanged -- a change in the CD4-binding site was observed (NL43 427 Glu-->Lys) to be present in the post-seroconversion 391/95-D enhanced clone (see Guillon2002a) Lawson2002. Guillon2002a,Lawson2002 (enhancing activity, acute/early infection)
391/95-D: The affect of Ab binding on infectivity was studied by pseudotyping three related envs with different phenotypes -- R5 viruses were preferentially enhanced, not X4 -- the V3 region was the main determinant of Ab-mediated enhancement and modulation of the interaction between CCR5 and gp120 is critical -- tests with MAbs anti-V3 391/95-D and CD4BS-specific GP68 indicate that Ab specificity did not determine whether or not infectivity was enhanced or neutralized, rather the phenotype was determined by Env conformation. Guillon2002a (co-receptor, enhancing activity)
391/95-D: Called 391/95D -- six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes. Park2000 (antibody binding site definition and exposure)
391/95-D: Called 391-95D -- SF162 is a neutralization-resistant HIV-1 isolate -- N-linked glycosylation modifications in the V2 loop of the SF162 gp120 revealed that these sites prevent neutralization by CD4BS MAbs (IgG1b12 and IgGCD4), and protect against neutralization by V3 MAbs (447-D and 391-95D) -- V2-region glycosylation site mutations did not alter neutralization resistance to V2 MAbs (G3.4 and G3.136) or CD4i MAbs (17b and 48d) -- V2 glycosylation site modification allows infection of macrophages, probably due to glycosylated forms requiring fewer CCR5 molecules for viral entry. Ly2000 (antibody binding site definition and exposure)
391/95-D: Called 391.5 -- MAb peptide-reactivity pattern clustered with immunological related MAbs: 391.5, 412 and 418, all selected with MN V3 peptide -- the core amino acids HIGPGR tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
391/95-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
391/95-D: Called 391-95D -- deleting the V2 loop of neutralization-resistant HIV-1 isolate SF162 does not abrogate its replication in PBMC or macrophages, but it enhances its neutralization sensitivity to sera from patients with B clade infection up to 170-fold, and also enhances sensitivity to sera from clades A through F -- deletion of V1 or V2 did not enable neutralization by V3 MAbs 391-95D or 257D. Stamatatos1998 (antibody binding site definition and exposure, subtype comparisons)
391/95-D: Called 391-95D -- binds more extensively than MAb 257-D on the surface of HIV-1 isolates SF162 and SF128A -- neutralizes more potently than 257-D -- stronger neutralization of primary macrophage targets than PBMC -- binding post-gp120-sCD4 association related to anti-V3 Abs neutralizing capacity. Stamatatos1997 (variant cross-recognition or cross-neutralization)
391/95-D: Competition ELISAs with serial deletions estimated the epitope to be KRIHIGPGRAFY -- unconstrained peptide had higher affinity than cyclic. Seligman1996 (antibody binding site definition and exposure)
391/95-D: The binding of conformation-dependent anti-V2, anti-V3, and anti-CD4BS MAbs to monomeric and virion-associated gp120 from HIV-1 isolates with differences in cell tropism was studied -- V3 loop epitopes were less accessible to Ab binding on the virion surface than in the gp120 monomer, particularly for macrophage-tropic isolates SF162 and SF128a, relative to T-cell tropic SF2 -- sCD4 association with gp120 better revealed this V3 epitope on macrophage tropic and dual tropic (MU3) viruses, but not in TCLA SF2. Stamatatos1995 (antibody binding site definition and exposure)
391/95-D: Neutralizes MN -- binds to SF2, not IIIB. Gorny1993

References

Seligman1996 S. J. Seligman, J. M. Binley, M. K. Gorny, D. R. Burton, S. Zolla-Pazner, and K. A. Sokolowski. Characterization by serial deletion competition ELISAs of HIV-1 V3 loop epitopes recognized by monoclonal antibodies. Mol. Immunol., 33:737-745, 1996. PubMed ID: 8811069. Show all entries for this paper.

Ly2000 A. Ly and L. Stamatatos. V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies [In Process Citation]. J. Virol., 74:6769-76, 2000. PubMed ID: 10888615. Show all entries for this paper.

Guillon2002a Christophe Guillon, Carel A. van Baalen, Patrick H. M. Boers, Esther J. Verschuren, Rob A. Gruters, and Albert D. M. E. Osterhaus. Construction and Characterisation of Infectious Recombinant HIV-1 Clones Containing CTL Epitopes from Structural Proteins in Nef. J Virol Methods, 99(1-2):115-121, Jan 2002. PubMed ID: 11684309. Show all entries for this paper.

Lawson2002 Victoria A. Lawson, Robert Oelrichs, Christophe Guillon, Allison A. Imrie, David A. Cooper, Nicholas J. Deacon, and Dale A. McPhee. Adaptive Changes after Human Immunodeficiency Virus Type 1 Transmission. AIDS Res. Hum. Retroviruses, 18(8):545-556, 20 May 2002. PubMed ID: 12036484. Show all entries for this paper.

McCaffrey2004 Ruth A McCaffrey, Cheryl Saunders, Mike Hensel, and Leonidas Stamatatos. N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of gp120 Protects Human Immunodeficiency Virus Type 1 SF162 from Neutralization by Anti-gp120 and Anti-gp41 Antibodies. J. Virol., 78(7):3279-3295, Apr 2004. PubMed ID: 15016849. Show all entries for this paper.

Displaying record number 940

MAb ID	838-D (838)
HXB2 Location	gp160(307-311)	gp160 Epitope Map
Author Location	Env( RF)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KSITK`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, review, subtype comparisons, variant cross-recognition or cross-neutralization

Notes

838-D: Called 838: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
838-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (variant cross-recognition or cross-neutralization, review)
838-D: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002
838-D: Called 838 -- Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A(CD4BS) , 4117C (plus others, V3) and 697D (and SC258, V2) were used as controls. He2002
838-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 838-D showed intermediate reactivity. Nyambi2000 (subtype comparisons)
838-D: Binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- V3 MAbs 447-52D, 838-D, and 1334 bound with a 7-10 fold preference for the oligomer. Gorny2000b (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
838-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 838, 782, 1027, 908, and 1006, all selected with RF V3 peptide -- the core amino acids KSITK tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
838-D: Review of clade specificity and anti-V3 HIV-1-Abs -- this Ab showed strong binding to many A, B, C and F peptides, poor binding to D and E. Zolla-Pazner1999b (review, subtype comparisons)
838-D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- 838-D bound B clade virions but had limited cross-reactivity with other clades, with low levels of binding to A and D virions. Nyambi1998 (subtype comparisons)
838-D: Four primary isolates showed distinct patterns of sensitivity to neutralization by polyclonal sera or plasma and MAbs -- BZ167 was the only isolate inhibited by all polyclonal sera and plasma tested, and was also neutralized by 8/17 MAbs, in particular anti-V3 loop (419-D, 447-52D, 782-D, and 838-D), anti-CD4bd (559/64-D, 654-D and 830-D and a cluster II of gp41 directed MAb (98-6) -- isolates 92HT593 and 91US056 were neutralized by V3 loop (419-D, and 447-52D)and cluster II gp41 (98-6) MAbs at higher concentrations -- US4 was neutralized by some of the polyclonal sera/plasma tested and not at all by MAbs individually or by a cocktail of ten MAbs consisting of 419-D, 447-52D, 782-D, 838-D, 559/64-D, 654-D, 450-D, 670-D, 1281-D and 98-6. Hioe1997b (variant cross-recognition or cross-neutralization)
838-D: Five human MAbs against were derived from HIV-infected North American subjects after selection by the V3 RF peptide -- 838-D was cross-reactive with V3 peptides from clade A and C, and could bind to 5/8 B clade V3 peptides -- 50% neutralization of RF was obtained. Gorny1997 (antibody generation, variant cross-recognition or cross-neutralization, subtype comparisons)

References

Gorny1997 Miroslaw K. Gorny, Thomas C. VanCott, Catarina Hioe, Zimra R. Israel, Nelson L. Michael, Anthony J. Conley, Constance Williams, Joseph A. Kessler II, Padmasree Chigurupati, Sherri Burda, and Susan Zolla-Pazner. Human Monoclonal Antibodies to the V3 Loop of HIV-1 With Intra- and Interclade Cross-Reactivity. J. Immunol., 159:5114-5122, 1997. PubMed ID: 9366441. Show all entries for this paper.

He2002 Yuxian He, William J. Honnen, Chavdar P. Krachmarov, Michael Burkhart, Samuel C. Kayman, Jose Corvalan, and Abraham Pinter. Efficient Isolation of Novel Human Monoclonal Antibodies with Neutralizing Activity Against HIV-1 from Transgenic Mice Expressing Human Ig Loci. J. Immunol., 169(1):595-605, 1 Jul 2002. PubMed ID: 12077293. Show all entries for this paper.

Displaying record number 939

MAb ID	782-D (782)
HXB2 Location	gp160(307-312)	gp160 Epitope Map
Author Location	Env( RF)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KSITKG`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, review, subtype comparisons, variant cross-recognition or cross-neutralization

Notes

782-D: Called 782: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
782-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (variant cross-recognition or cross-neutralization, review)
782-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 782-D showed intermediate reactivity. Nyambi2000 (subtype comparisons)
782-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 838, 782, 1027, 908, and 1006, all selected with RF V3 peptide -- the core amino acids KSITK tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
782-D: Review of clade specificity and anti-V3 HIV-1-Abs -- this Ab showed strong binding to several B and F peptides, one C peptide, and some reactivity with A and D peptides. Zolla-Pazner1999b (variant cross-recognition or cross-neutralization, review, subtype comparisons)
782-D: Four primary isolates showed distinct patterns of sensitivity to neutralization by polyclonal sera or plasma and MAbs -- BZ167 was the only isolate inhibited by all polyclonal sera and plasma tested, and was also neutralized by 8/17 MAbs, in particular anti-V3 loop (419-D, 447-52D, 782-D, and 838-D), anti-CD4bd (559/64-D, 654-D and 830-D and a cluster II of gp41 directed MAb (98-6) -- isolates 92HT593 and 91US056 were neutralized by V3 loop (419-D, and 447-52D)and cluster II gp41 (98-6) MAbs at higher concentrations -- US4 was neutralized by some of the polyclonal sera/plasma tested and not at all by MAbs individually or by a cocktail of ten MAbs consisting of 419-D, 447-52D, 782-D, 838-D, 559/64-D, 654-D, 450-D, 670-D, 1281-D and 98-6. Hioe1997b (variant cross-recognition or cross-neutralization)
782-D: Five human MAbs against were derived from HIV-infected North American subjects after selection by the V3 RF peptide -- 782-D was not cross-reactive with V3 peptides from clade A or E, but could bind to 3/8 B clade V3 peptides, and 1/2 C clade V3 peptides -- 50% neutralization of RF was obtained. Gorny1997 (antibody generation, variant cross-recognition or cross-neutralization, subtype comparisons)

References

Displaying record number 945

MAb ID	1006-15D (1006)
HXB2 Location	gp160(307-312)	gp160 Epitope Map
Author Location	gp120( RF)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KSITKG`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	no
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, review, subtype comparisons, variant cross-recognition or cross-neutralization

Notes

1006-15D: The neutralization potency of this Ab against 7 HIV-1 primary isolates was compared to the neutralization potency of the Ab KD-247. Same Ab concentrations were needed for neutralization of the N-NIID and 92TH022 isolates, while higher concentrations of 1006-15D were needed for the neutralization of the rest of the HIV-1 isolates suggesting 1006-15D has lower neutralization potency. Eda2006a (variant cross-recognition or cross-neutralization)
1006-15D: Called 1006-15: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
1006-15D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
1006-15D: Called 1006 -- Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A(CD4BS) , 4117C (plus others, V3) and 697D (and SC258, V2) were used as controls. He2002
1006-15D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 1006-15D showed strong cross-reactivity. Nyambi2000 (subtype comparisons)
1006-15D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 838, 782, 1027, 908, and 1006, all selected with RF V3 peptide -- the core amino acids KSITK tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
1006-15D: Review of clade specificity and anti-V3 HIV-1-Abs -- this Ab showed strong binding to several B and F peptides, one C peptide, and some reactivity with A peptides -- no binding was observed with D and E peptides. Zolla-Pazner1999b (review, subtype comparisons)
1006-15D: Five human MAbs against were derived from HIV-infected North American subjects after selection by the V3 RF peptide -- was somewhat cross-reactive with V3 peptides from clade A, C and other B clade V3 peptides, but not E clade. Gorny1997 (antibody generation, subtype comparisons)

References

Eda2006a Yasuyuki Eda, Mari Takizawa, Toshio Murakami, Hiroaki Maeda, Kazuhiko Kimachi, Hiroshi Yonemura, Satoshi Koyanagi, Kouichi Shiosaki, Hirofumi Higuchi, Keiichi Makizumi, Toshihiro Nakashima, Kiyoshi Osatomi, Sachio Tokiyoshi, Shuzo Matsushita, Naoki Yamamoto, and Mitsuo Honda. Sequential Immunization with V3 Peptides from Primary Human Immunodeficiency Virus Type 1 Produces Cross-Neutralizing Antibodies against Primary Isolates with a Matching Narrow-Neutralization Sequence Motif. J. Virol., 80(11):5552-5562, Jun 2006. PubMed ID: 16699036. Show all entries for this paper.

Displaying record number 946

MAb ID	908-D (908, 908-12D)
HXB2 Location	gp160(307-312)	gp160 Epitope Map
Author Location	gp120( RF)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KSITKG`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, review, subtype comparisons

Notes

908-D: Called 908: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
908-D:This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
908-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross -reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 908-D showed strong cross-reactivity, but achieved only 50% neutralization on 2/5 isolates tested. Nyambi2000 (subtype comparisons)
908-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 838, 782, 1027, 908, and 1006, all selected with RF V3 peptide -- the core amino acids KSITK tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
908-D: Review of clade specificity and anti-V3 HIV-1-Abs -- this Ab showed strong binding to several A, B, C and F peptides, and poor binding to E and D peptides. Zolla-Pazner1999b (review, subtype comparisons)
908-D: Five human MAbs against were derived from HIV-infected North American subjects after selection by the V3 RF peptide -- 908-D was not cross-reactive with V3 peptides from clade E, but could bind to 6/8 B clade V3 peptides, 2/4 A clade, and 1/2 C clade -- 50% neutralization of RF was obtained. Gorny1997 (antibody binding site definition and exposure, antibody generation, subtype comparisons)

References

Displaying record number 938

MAb ID	1027-15D (1027, 1027-D, 1027D, 1027-15)
HXB2 Location	gp160(307-313)	gp160 Epitope Map
Author Location	Env( RF)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`KSITKGP`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	no
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, review, subtype comparisons

Notes

1027-15S: Called 1027-15: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
1027-15D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
1027-15D: Called 1027-D -- A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002 (antibody binding site definition and exposure)
1027-15D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 1027-15D showed strong cross-reactivity. Nyambi2000 (subtype comparisons)
1027-15D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 838, 782, 1027, 908, and 1006, all selected with RF V3 peptide -- the core amino acids KSITK tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
1027-15D: Review of clade specificity and anti-V3 HIV-1-Abs -- this Ab showed moderate binding to several B and F peptides, one C peptide, and was not reactivity with A, D and E peptides. Zolla-Pazner1999b (review, subtype comparisons)
1027-15D: Five human MAbs against were derived from HIV-infected North American subjects after selection by the V3 RF peptide -- 1027-15D was not cross-reactive with V3 peptides from clade A or E, but could bind to 3/8 B clade V3 peptides, and 1/2 C clade V3 peptides. Gorny1997 (antibody binding site definition and exposure, antibody generation, subtype comparisons)

References

Displaying record number 470

MAb ID	453-D (453)
HXB2 Location	gp160(309-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`IHIGPGR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, binding affinity, review, subtype comparisons, vaccine antigen design, variant cross-recognition or cross-neutralization

Notes

453-D: Called 453: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
453-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (variant cross-recognition or cross-neutralization)
453-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 453-D showed intermediate reactivity. Nyambi2000 (subtype comparisons)
453-D : MAb peptide-reactivity pattern clustered with immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group -- MAb 268, with a previously defined core epitope identical to 453 (HIGPGR), was not part of this reactivity group, illustrating that context can be critical. Zolla-Pazner1999a (antibody binding site definition and exposure)
453-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
453-D : Called 453, epitope described as KRIHIGPGR -- the tip of the V3 loop was presented in a mucin backbone -- higher valency correlates with stronger affinity constant. Fontenot1995 (antibody binding site definition and exposure, vaccine antigen design)
453-D: Moderate homologous neutralization, moderately slow dissociation rate. VanCott1994 (binding affinity)
453-D: Neutralizes MN -- binds SF2: IYIGPGR -- specificity: MN, SF2, NY5, RF. Gorny1993 (antibody binding site definition and exposure)

References

Displaying record number 471

MAb ID	504-D (504, 504-10D)
HXB2 Location	gp160(309-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`IHIGPGR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1κ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, review, subtype comparisons

Notes

504-D: Called 504: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
504-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
504-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 504-D showed weak reactivity. Nyambi2000 (subtype comparisons)
504-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
504-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review)
504-D -- Neutralizes MN -- binds SF2: IYIGPGR. Gorny1993 (antibody binding site definition and exposure)

References

Displaying record number 497

MAb ID	419-D (419, 419D)
HXB2 Location	gp160(309-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`IHIGPGR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, complement, mimotopes, review, subtype comparisons, superinfection, variant cross-recognition or cross-neutralization

Notes

419-D: Called 419: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (mimotopes, superinfection)
419-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
419-D: Called 419 -- Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A(CD4BS) , 4117C (plus others, V3) and 697D (and SC258, V2) were used as controls. He2002
419-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 419-D showed intermediate reactivity, and no neutralization when tested against five strains -- discrepancy between the epitope as described in earlier papers and as described here, KRIHIGP. Nyambi2000 (subtype comparisons)
419-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
419-D: Review of clade specificity and anti-V3 HIV-1-Abs -- epitope is described as KRIHIGP. Zolla-Pazner1999b (antibody binding site definition and exposure, review)
419-D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- 419-D bound to 3/4 B clade virions, and to D clade MAL. Nyambi1998 (subtype comparisons)
419-D: Four primary isolates showed distinct patterns of sensitivity to neutralization by polyclonal sera or plasma and MAbs -- BZ167 was the only isolate inhibited by all polyclonal sera and plasma tested, and was also neutralized by 8/17 MAbs, in particular anti-V3 loop (419-D, 447-52D, 782-D, and 838-D), anti-CD4bd (559/64-D, 654-D and 830-D and a cluster II of gp41 directed MAb (98-6) -- isolates 92HT593 and 91US056 were neutralized by V3 loop (419-D, and 447-52D)and cluster II gp41 (98-6) MAbs at higher concentrations -- US4 was neutralized by some of the polyclonal sera/plasma tested and not at all by MAbs individually or by a cocktail of ten MAbs consisting of 419-D, 447-52D, 782-D, 838-D, 559/64-D, 654-D, 450-D, 670-D, 1281-D and 98-6. Hioe1997b (variant cross-recognition or cross-neutralization)
419-D: Mediated deposition of complement component C3 on HIV infected cells, enhanced by second Ab binding, rabbit anti-human IgG. Spear1993 (complement)
419-D: Neutralizes MN -- binds SF2: IYIGPGR. Gorny1993 (variant cross-recognition or cross-neutralization)
419-D: MN, NY5 and SF2 strain specific, does not cross-react with RF, CDC4, WM52 or HXB2. Karwowska1992a (variant cross-recognition or cross-neutralization)

References

Displaying record number 485

MAb ID	268-D (268-11-D-IV, 268D, 268, 268-11D, 268-10D, MAb 268, 268-10-D, ARP)
HXB2 Location	gp160(310-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`HIGPGR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, dendritic cells, neutralization, review

Notes

268-D IV: This Ab was shown to inhibit HIV-1 BaL replication in macrophages but not in PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication occurs by an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles. Holl2006 (neutralization, dendritic cells)
268-D: The epitope for the MAb D19 is conserved and embedded in V3. D19 is unique in that for R5 viruses, it was cryptic and did not bind without exposure to sCD4, and for X4 and R5X4 isolates it was constitutively exposed. It had an overlapping binding region with MAbs 447-52D, B4e8, and 268-D, but different reactivity patterns and fine specificity. Lusso2005
268-D: Called 268: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4 induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides do not show as much ability to neutralize as V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 268 was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
268-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, while many neutralize some TCLA strains, a subset can also neutralize some primary isolates. Gorny2003 (review)
268-D: NIH AIDS Research and Reference Reagent Program: 1511.
268-D: UK Medical Research Council AIDS reagent: ARP3024.
268-D: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera---2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5---thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002
268-D: Called ARP3024: Herpesvirus saimiri-immortalized CD4+ T lymphocytes (HVS T cells) were used to isolate virus and perform HIV-1 neutralization assays, and compared with a standard PBMC protocol -- neutralization sensitivities to a panel of MAbs and to homologous or heterologous plasma/sera were similar for HVS T cells (CN-2 cells) and PBMCs. Vella2002
268-D: Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding -- one of the TCLA V3 viruses 320SI-C3.3 shows reduced binding with this MAb, the sequence of the epitope in 320SI is HIGPGR and in 320SI-C3.3 is RIGPGR. York2001
268-D: Called 268D -- six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes. Park2000
268-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 268-D showed weak reactivity. Nyambi2000
268-D: Ab responses, because of their capacity to alter antigen uptake and processing, can influence helper T cell responses -- CD4BS MAbs or serum Ig from HIV+ individuals inhibited proliferative responses of gp120 specific T cells -- V3 MAbs 447-52-D and 268-10-D did not effect proliferation. Hioe2000
268-D: Called MAb 268 -- To identify potential mimotopes of V3, a hexapeptide phage library was screened with MAb 268 -- two hexamers were identified, HLGPGR or KAIHRI that bind to 268 with the same binding site as the V3 loop and inhibit 268 MN gp120 -- KLH conjugated hexamer KAIHRI stimulates Abs in rabbits that cross-react with ML gp120. Laisney1999
268-D: Called 268-11D -- Study of a live-vector mucosal vaccine that expresses HIV-1 V3 domains using the bacterium Streptococcus gordonii which can express heterologous Ag and can colonize the oral cavity and vagina of mice -- 268-D and 257-D recognized S. gordonii expressing the V3 domain of MN -- the vaccine stimulated V3-specific IgG2a in mice. Oggioni1999
268-D: rgp120 derived from a R5X4 subtype B virus, HIV-1 W61D, was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- 268-D bound rgp120 W61D but could only neutralize the W61D isolate following T-cell line adaptation. Beddows1999
268-D: Peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group -- MAb 453, with an identical core epitope to 268 based on prior experiments (HIGPGR), was not part of this reactivity group, illustrating that context can be critical. Zolla-Pazner1999a
268-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b
268-D: A T-cell line-adapted (TCLA) derivative of SI primary isolate 168P acquired the ability to be neutralized by anti-V3 MAbs -- the primary isolate could use either CCR5 or CXCR4, and was not neutralized when infection was directed via either pathway, however the TCLA derivative uses CXCR4 only and is neutralized. LaCasse1998
268-D: Poor reactivity against HIV-1 isolates SF162 and SF128A and no neutralization, in contrast to MAbs 391/95-D and 257-D. Stamatatos1997
268-D: 268-D is V H4 -- V-region heavy chain usage was examined and a bias of enhanced V H1 and V H4, and reduced V H3, was noted among HIV infected individuals. Wisnewski1996
268-D: Failed to neutralize HXB2 and chimeric virus with gp120 from primary isolates in an HXB2 background. McKeating1996b
268-D: The binding of conformation-dependent anti-V2, anti-V3, and anti-CD4BS MAbs to monomeric and virion-associated gp120 from HIV-1 isolates with differences in cell tropism was studied -- V3 loop epitopes were less accessible to Ab binding on the virion surface than in the gp120 monomer, particularly for macrophage-tropic isolates SF162 and SF128a, relative to T-cell tropic SF2 -- sCD4 association with gp120 did not influence the binding of 268-D to virion-associated gp120, although sCD4 binding did alter epitope exposure for other anti-V3 MAbs. Stamatatos1995
268-D: Serotyping study using flow-cytometry, if H of HIGPGR was substituted in virus, 268-D did not bind. Zolla-Pazner1995
268-D: Moderate dissociation rate and homologous neutralization titer. VanCott1994
268-D: Mediated deposition of complement component C3 on HIV infected cells, but not in the presence of sCD4. Spear1993
268-D: Neutralizes MN -- binds SF2: YIGPGR -- specificity: MN, SF2, NY5, RF, CDC4. Gorny1993
268-D: Reacts with MN, NY5, CDC4, RF and SF2, does not cross-react with WM52 or HXB2. Karwowska1992a
268-D: Called 268-11-D-IV -- strain specific weakly neutralizing. DSouza1991

References

McKeating1996b J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395. Show all entries for this paper.

Laisney1999 I. L. Laisney and A. D. Strosberg. Dual specificity of a human neutralizing monoclonal antibody, specific for the V3 loop of GP120 (HIV-1). Immunol. Lett., 67:185-92, 1999. PubMed ID: 10369125. Show all entries for this paper.

Hioe2000 C. E. Hioe, G. J. Jones, A. D. Rees, S. Ratto-Kim, D. Birx, C. Munz, M. K. Gorny, M. Tuen, and S. Zolla-Pazner. Anti-CD4-binding domain antibodies complexed with HIV type 1 glycoprotein 120 inhibit CD4+ T cell-proliferative responses to glycoprotein 120 [In Process Citation]. AIDS Res. Hum. Retroviruses, 16:893-905, 2000. PubMed ID: 10875615. Show all entries for this paper.

Lusso2005 Paolo Lusso, Patricia L. Earl, Francesca Sironi, Fabio Santoro, Chiara Ripamonti, Gabriella Scarlatti, Renato Longhi, Edward A. Berger, and Samuele E. Burastero. Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains. J. Virol., 79(11):6957-6968, Jun 2005. PubMed ID: 15890935. Show all entries for this paper.

Displaying record number 491

MAb ID	386-D (386, 386-10D, 386D)
HXB2 Location	gp160(310-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`HIGPGR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, binding affinity, isotype switch, review, subtype comparisons

Notes

386-D: Called 386: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides do not show as much ability to neutralize as V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 386 was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
386-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
386-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 386-D showed intermediate reactivity. Nyambi2000 (isotype switch, subtype comparisons)
386-D: Peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
386-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
386-D: Slow dissociation rate, potent homologous neutralization. VanCott1994 (binding affinity)
386-D: Neutralizes MN -- binds SF2: YIGPGR -- specificity: MN, SF2, NY5, RF, CDC4. Gorny1993 (antibody binding site definition and exposure)

References

Displaying record number 472

MAb ID	418-D (418, 418D)
HXB2 Location	gp160(310-316)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`HIGPGRA`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1κ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, review, subtype comparisons, variant cross-recognition or cross-neutralization

Notes

418-D: Called 418: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. 418 was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
418-D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
418-D: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002
418-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 418-D showed intermediate reactivity. Nyambi2000 (variant cross-recognition or cross-neutralization, subtype comparisons)
418-D: Called 418 -- MAb peptide-reactivity pattern clustered with immunological related MAbs: 391.5, 412 and 418, all selected with MN V3 peptide -- the core amino acids HIGPGR tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure)
418-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
418-D: Neutralizes MN, does not bind to SF2 or HXB2. Gorny1993 (variant cross-recognition or cross-neutralization)
418-D: MN strain specific, does not cross-react with SF2, NY5, RF, CDC4 WM52 or HXB2. Karwowska1992a (variant cross-recognition or cross-neutralization)

References

Displaying record number 498

MAb ID	537-D (537)
HXB2 Location	gp160(311-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`IGPGR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure

Notes

537-D: Called 537: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
537-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 537-D showed weak reactivity. Nyambi2000
537-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group. Zolla-Pazner1999a
537-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b
537-D: Moderate homologous neutralization, relatively rapid dissociation constant. VanCott1994
537-D: MN type specific neutralization observed -- binds SF2, also IGPGR. Gorny1992,Gorny1993
537-D: Reacts with MN, NY5, CDC4, RF, WM52 and SF2, but does not cross-react with HXB2. Karwowska1992a

References

Gorny1992 M. K. Gorny, A. J. Conley, S. Karwowska, A. Buchbinder, J.-Y. Xu, E. A. Emini, S. Koenig, and S. Zolla-Pazner. Neutralization of diverse human immunodeficiency virus type 1 variants by an anti-V3 human monoclonal antibody. J. Virol., 66:7538-7542, 1992. PubMed ID: 1433529. Show all entries for this paper.

Displaying record number 500

MAb ID	447-52D (447/52-DII, 447-52-D, 447d, 447-52-D, 447-D, 447, 447D)
HXB2 Location	gp160(312-315)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Dr. Susan Zolla-Pazner, NYU Med Center NY, NY; Veteran Affairs Med Center NY, NY; or Cellular Products Inc, Buffalo, NY,
Epitope	`GPXR`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L P
Species (Isotype)	human(IgG3λ)
Immunogen	HIV-1 infection
Keywords	acute/early infection, ADCC, antibody binding site definition and exposure, antibody interactions, antibody sequence variable domain, assay development, assay standardization/improvement, binding affinity, co-receptor, complement, dendritic cells, enhancing activity, escape, kinetics, mimotopes, neutralization, review, structure, subtype comparisons, Th2, vaccine antigen design, vaccine-specific epitope characteristics, variant cross-recognition or cross-neutralization, viral fitness and reversion

Notes

447-52D: 29 subtype B V3 peptides were designed and used for immunization of guinea pigs. Peptides that induced Abs that neutralized more than 3 HIV isolates were shown to bind to this Ab better than peptides unable to induce neutralization of any of the HIV-1 primary isolates. Haynes2006 (neutralization, binding affinity)
447-52D: Cloned Envs (clades A, B, C, D, F1, CRF01_AE, CRF02_AG, CRF06_cpx and CRF11_cpx) derived from donors either with or without broadly cross-reactive neutralizing antibodies were shown to be of comparable susceptibility to neutralization by 447-52D. Cham2006 (neutralization, variant cross-recognition or cross-neutralization, subtype comparisons)
447-52D: Guinea-pigs were immunized with 447-52D epitope inserted at three different surface V3 loop locations in the small Escherichia coli Trx protein in order to generate a competent immunogen. Only one complex was shown to successfully generate anti-V3 Abs capable of out-competing 447-52D binding to gp120 and recognizing the same epitope as this Ab. However, these 447-52D-like Abs were not able to affect neutralization of JRFL and BAL. Chakraborty2006 (neutralization, vaccine antigen design, variant cross-recognition or cross-neutralization, binding affinity)
447-52D: The ability of this Ab to inhibit viral growth was increased when macrophages and immature dendritic cells (iDCs) were used as target cells instead of PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication by this Ab for macrophages and iDCs can occur by two distinct mechanisms, neutralization of infectivity involving only the Fab part of the IgG, and, an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles. Holl2006 (dendritic cells)
447-52D: Inhibition of R5 HIV replication by monoclonal and polyclonal IgGs and IgAs in iMDDCs was evaluated. The neutralizing activity of 447-52D was observed to be higher in iMDDCs than in PBLs and PHA-stimulated PBMCs. A 90% reduction of HIV infection was observed without induction of MDDC maturation by this mAb. It was also demonstrated that binding of this mAb to HIV-1 was necessary for inhibition of iMDDC infection. Increased expression of FcγRI on iMDDCs increased inhibition of HIV by 447-52D, suggesting the involvment of this receptor in the HIV-inhibitory activity of this mAb. Holl2006a (neutralization, dendritic cells)
447-52D: The neutralization potency of this Ab against 7 HIV-1 primary isolates was compared to the neutralization potency of the anti-V3 MAb KD-247. Same Ab concentrations were needed for neutralization of the MN, N-NIID, and 92TH022 isolates, while higher concentrations of 447-52D were needed for the neutralization of the rest of the HIV-1 isolates suggesting KD-247 is more potent. Eda2006a
447-52D: In this study the neutralization breadth of F425 B4e8 was assessed using a panel of 40 primary HIV-1 isolates, and 447-52D was found to have a similar profile, and was used as a control to gauge the effects of the amino acid substitutions in the V3 region. As expected, replacing Arg 315 with Ala or Gln and Pro 313 with Ala reduced binding affinity of this 447-52D substantially. Ala substitutions of residues in positions 304-309 and 319-320 also unexpectedly resulted in diminished binding affinity of the Ab. Pantophlet2007 (antibody binding site definition and exposure, subtype comparisons)
447-52D: Z13e1, a high affinity variant of Fab Z13, was identified through targeted mutagenesis and affinity selection against gp41 and an MPER peptide. Z13e1 showed 100-fold improvement in binding affinity for MPER antigens over Z13. 447-52D was used as a control in this study. 447-52D was shown to clearly bind to monomers of gp120-gp41 while trimer binding was negligible, in accordance with its modest neutralization potency against HIV-1 JR-FL. Nelson2007 (vaccine antigen design)
447-52D: G1 and G2 recombinant gp120 proteins, consisting of 2F5 and 4E10, and 4E10 epitopes, respectively, engrafted into the V1/V2 region of gp120, were tested as an immunogen to see if they could elicit MPER antibody responses. Deletion of V1/V2 from gp120, or its replacement with G1 and G2 grafts, did not greatly affect binding of 447-52D to gp120. Shortening of the N and C termini of the V3 loop enhanced the binding of 447-52D. Law2007 (vaccine antigen design)
447-52D: This review describes the effectiveness of the current HIV-1 immunogens in eliciting neutralizing antibody responses to different clades of HIV-1. It also summarizes different evasion and antibody escape mechanisms, as well as the most potent neutralizing MAbs and their properties. MAbs reviewed in this article are: 2G12, IgG1b12, 2F5, 4E10, A32, 447-52D and, briefly, D50. Novel immunogen design strategies are also discussed. Haynes2006a (neutralization)
447-52D: Viruses from early and late infection of a macaque with SHIV SF162P4 were resistant to contemporaneous serum that had broadly reactive NAbs. SF162 was highly susceptible to neutralization by anti-V3 MAbs 447D and P3E1, as well as anti-V1 MAb P3C8, while envelopes cloned from this animal at 304 days and at 643 days (time of death) post infection had developed resistance to all three of these antibodies. Kraft2007 (neutralization, escape)
447-52D: This Ab was used to help define the antigenic profile of envelopes used in serum depletion experiments to attempt to define the neutralizing specificities of the broadly cross-reactive neutralizing serum. Peptides containing epitopes for 447-52D did not inhibit neutralization by broadly neutralizing sera from two clade B and one clade A infected asymptomatic individuals, indicating that the V3 epitope for this MAb did not account for the broad neutralizing activity observed. 447-52D bound to JR-FL and JR-CSF gp120 monomers but not to core JR-CSF gp120 monomer. Dhillon2007 (antibody binding site definition and exposure, neutralization)
447-52D: Antigens were designed to attempt to target immune responses toward the IgG1b12 epitope, while minimizing antibody responses to less desirable epitopes. One construct had a series of substitutions near the CD4 binding site (GDMR), the other had 7 additional glycans (mCHO). The 2 constructs did not elicit b12-like neutralizing antibodies, but both antigens successfully dampened other responses that were intended to be dampened while not obscuring b12 binding. V3 MAbs (447-52D, 19b, F245-B4e8 and 39F) bound to the GDMR antigen, but either did not bind or had diminished binding to mCHO. Selvarajah2005 (vaccine-specific epitope characteristics, Th2)
447-52D: This study is about the V2 MAb C108g, which is type-specific and neutralizes BaL and HXB2. JR-FL is a neutralization resistant strain; modification of JRFL at V2 positions 167 and 168 (GK->DE) created a C108g epitope, and C108g could potently neutralize the modified JR-FL. The modification in V2 also increased neutralization sensitivity to V3 MAbs 4117c, 2219, 2191, and 447-52D (447-52D was the only one of the 4 V3 MAbs that could neutralize the unmodified JRFL); but only had minor effects on neutralization by CD4BS MAb 5145A, and broadly neutralizing MAbs IgG1b12, 2G12, and 2F5. Pinter2005 (antibody binding site definition and exposure)
447-52D: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication in microglial cells. Bori-15 had increased replication in microglial cells and a robust syncytium-forming phenotype, ability to use low levels of CD4 for infection, and increased sensitivity to neutralization by sCD4 and 17b. Four amino acid changes in gp120 V1-V2 were responsible for this change. Protein functionality and integrity of soluble, monomeric gp120-molecules derived from parental HIV-1 Bori and microglial-adapted HIV-1 Bori-15 was assessed in ELISA binding assays using CD4BS MAbs F105 and IgG1b12, glycan-specific 2G12, and V3-specific 447-52D, and were unchanged. Association rates of sCD4 and 17b were not changed, but dissociation rates were 3-fold slower for sCD4 and 14-fold slower for 17b. Martin-Garcia2005 (antibody binding site definition and exposure)
447-52D: The epitope for the MAb D19 is conserved and embedded in V3. D19 is unique in that for R5 viruses, it was cryptic and did not bind without exposure to sCD4, and for X4 and R5X4 isolates it was constitutively exposed. It had an overlapping binding region with MAbs 447-52D, B4e8, and 268-D, but different reactivity patterns and fine specificity. While B4e8 and 447-52D could bind to the R5 virus BaL in the absence of sCD4, treatment with sCD4 did increase the binding of both B4e8 and 447-52D, but did not impact their ability to neutralize BaL. Lusso2005 (antibody binding site definition and exposure)
447-52D: Sera from subtype A infected individuals from Cameroon have antibodies that react strongly with subtype A and subtype B V3 loops in fusion proteins, and neutralize SF162 pseudotypes, while sera from 47 subtype B infected individuals reacted only with subtype B. Sera from Cameroon did not neutralize primary A or B isolates, due to indirect masking by the V1/V2 domain rather than due to loss of the target epitope. Neutralization by anti-V3 B clade specific MAbs 447-52D and 4117C was fully blocked by a clade V3 loop fusion protein, but not an A clade fusion protein, while Cameroonian sera neutralization was fully blocked by both A and B clade fusion proteins. Krachmarov2005 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization, subtype comparisons)
447-52D: Of 35 Env-specific MAbs tested, only 2F5, 4E10, IgG1b12, and two CD4BS adjacent MAbs (A32 and 1.4G) and gp41 MAbs (2.2B and KU32) had binding patterns suggesting polyspecific autoreactivity, and similar reactivities may be difficult to induce with vaccines because of elimination of such autoreactivity. 447-52D has no indication of polyspecific autoreactivity. Haynes2005 (antibody binding site definition and exposure)
447-52d: 2909 is a human anti-Env NAb that was selected by a neutralization assay and binds to the quaternary structure on the intact virion. ELISA-based competition assays and subsequent mutational analysis determined that the CD4BS and V2 and V3 loops contribute to the 2909 epitope: 2909 binding was inhibited by MAbs 447-52d (anti-V3), 830A (anti-V2), and IgG1b12 (anti-CD4BS) and sCD4. 2909 was not inhibited by MAbs 670, 1418, nor 2G12. Gorny2005
447-52D: By adding N-linked glycosylation sites to gp120, epitope masking of non-neutralizing epitopes can be achieved leaving the IgG1b12 binding site intact. This concept was originally tested with the addition of four glycosylation sites, but binding to b12 was reduced. It was modified here to exclude the C1 N-terminal region, and to include only three additional glycosylation sites. This modified protein retains full b12 binding affinity and it masks other potentially competing epitopes, and does not bind to 21 other MAbs to 7 epitopes on gp120, including 447-52D. Pantophlet2004 (vaccine antigen design)
447-52D: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. Neutralization outside of the B clade was very rare, and seemed to depend on the presence of a GPGR V3 tip, which is rare outside of the B clade. Binley2004 (variant cross-recognition or cross-neutralization, subtype comparisons)
447-52D: Analysis of the conformation of 447-52D in complex with the V3MN18 peptide (gp12 aa 310-329, KRKRIHIGPGRAFYTTKN) was undertaken using solid state NMR. The bound peptide had a well defined constrained structure that was in good agreement with solution NMR and crystallographic studies. Sharpe2004 (structure)
447-52D: A primary isolate, CC1/85, was passaged 19 times in PBMC and gradually acquired increased sensitivity to FAb b12 and sCD4 that was attributed to changes in the the V1V2 loop region, in particular the loss of a potential glycosylation site. The affinity for sCD4 was unchanged in the monomer, suggesting that the structural impact of the change was manifested at the level of the trimer. The passaged virus, CCcon19, retained an R5 phenotype and its neutralization susceptibility to other Abs was essentially the same as CC1/85. 447-52D did not neutralize the primary or passaged variant. Pugach2004 (variant cross-recognition or cross-neutralization, viral fitness and reversion)
447-52D: V1V2 was determined to be the region that conferred the neutralization phenotype differences between two R5-tropic primary HIV-1 isolates, JRFL and SF162. JRFL is resistant to neturalization by many sera and MAbs, while SF162 is sensitive. All MAbs tested, anti-V3, -V2, -CD4BS, and -CD4i, (except the broadly neutralizing MAbs IgG1b12, 2F5, and 2G12, which neutralized both strains), neutralized the SF162 pseudotype but not JRFL, and chimeras that exchanged the V1V2 loops transferred the neutralization phenotype. 5/6 anti-V3 MAbs, including 447-52D, had similar binding affinity to soluble SF162 and JR-FL rgp120s, although the V3 loop differs at three positions (HigpgrafyTtgE for JR-FL and TigpgrafyAtgD for SF162). Pinter2004 (variant cross-recognition or cross-neutralization)
447-52D: Sera from two HIV+ people and a panel of MAbs were used to explore susceptibility to neutralization in the presence or absence of glycans within or adjacent to the V3 loop and within the C2, C4 and V5 regions of HIV-1 SF162 env gp120. The loss of the any of three glycans within or adjacent to the V3 loop (GM299 V3), C2 (GM292 C2), C3 (GM329 C3) increased neutralization susceptibility to 447-52D, but C4 (GM438 C4) or V5 (GM454 V5) removal did not make SF162 more sensitive. V3 glycans tended to shield V3 loop, CD4 and co-receptor MAb binding sites, while C4 and V5 glycans shielded V3 loop, CD4, gp41 but not co-receptor MAb binding sites. Selective removal of glycans from a vaccine candidate may enable greater access to neutralization susceptible epitopes. McCaffrey2004 (antibody binding site definition and exposure, vaccine antigen design)
447-52D: The role of serine proteases on HIV infection was explored. Trypsin decreased the binding of most Env MAb tested and diminished cell fusion of H9 cells infected with HIV-1 LAI virus (H9/IIIB) to MAGI cells. In contrast, thrombin increased the binding of MAbs to gp120 epitopes near the CD4 and CCR5 binding sites, and increased cell fusion. Binding of the V3 MAbs 694-98D and 447-52D, that both bind near the tip of the loop, was decreased by both thrombin and trypsin. Ling2004 (antibody binding site definition and exposure)
447-52D: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides, but was an exception in that it is cross-neutralizing. 447-52D neutralized 12/13 clade B viruses. Gorny2004 (antibody binding site definition and exposure)
447-52D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. The set that can cross-neutralize primary isolates (2182, 2191, 2219, 2412, 2442, 2456) bind V3 but are conformationally senstitive, suggesting some structural conservation despite sequence variation. These MAbs have distinct epitopes relative to 447-52D, a MAb directed at the tip of the V3 loop that also can neutralize many primary isolates. Although 447-52D was selected using a peptide, it has conformational characteristics. Inter-clade cross-neutralization by anti-V3 conformation-dependent MAbs is reduced. Gorny2003 (antibody binding site definition and exposure, review)
447-52D: This paper attempts to engineer a gp120 molecule that would focus the immune response onto the IgG1b12 epitope. Adding a glycosylation sequon (P313N) to the V3 loop knocked out binding to anti-V3 MAbs loop 2, 19b and 447-52-D. Pantophlet2003b (vaccine antigen design)
447-52D: scFv 4KG5 reacts with a conformational epitope that is formed by the V1V2 and V3 loops and the bridging sheet (C4) region of gp120 and is influenced by carbohydrates. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120 JRFL. MAbs to the following regions diminished 4KG5 binding: V2 loop, V3 loop, V3-C4 region, CD4BS. MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected by these loops. This was one of the V3 MAbs used. Zwick2003 (antibody interactions)
447-52D: The Fv fragment (composed of just the light and heavy variable regions, and the smallest intact binding unit of an Ab) of 447-52 D was expressed and purified. Preliminary NMR with the peptide epitope indicates that an NMR structure determination is feasible. Kessler2003 (antibody sequence variable domain, structure)
447-52D: The SOS mutant envelope protein introduces a covalent disulfide bond between gp120 surface and gp41 transmembrane proteins into the R5 isolate JR-FL by adding cysteines at residues 501 and 605. Pseudovirions bearing this protein bind to CD4 and co-receptor bearing cells, but do not fuse until treatment with a reducing agent, and are arrested prior to fusion after CD4 and co-receptor engagement. 447-52D was able to neutralize the SOS protein better than the wildtype, but did not neutralize SOS well when added post-attachment, as the V3 loop is involved in co-receptor engagement. Binley2003 (vaccine antigen design)
447-52D: Virion capture assays are not a good predictor of neutralization, and the presentation of epitopes using this assay seems to be different from that of functional Envelope spikes on primary isolates -- F105 and b6 could efficiently block the b12-mediated capture of infectious virions in a virus capture, but did not inhibit b12 neutralization -- Ab 447-52D was able to potently neutralize 89.6 and to neutralize JR-CSF at a high concentration but poorly neutralized ADA -- b12 was potent at neutralizing the three primary virions JR-CSF, ADA, and 89.6, but anti-V3 Abs 447-52D and 19b, which did not neutralize JR-CSF and ADA, captured amounts of p24 equal to or higher than the amounts captured by the neutralizing Ab b12. Poignard2003 (antibody binding site definition and exposure, assay development, variant cross-recognition or cross-neutralization)
447-52D: Review of NAbs. Ferrantelli2002
447-52D: Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A(CD4BS) , 4117C (plus others, V3) and 697D (and SC258, V2) were used as controls. He2002
447-52D: Conformation-dependent anti-V3 loop Abs may be more cross-reactive, so six new V3 MAbs were generated -- the six new MAbs all bind to the tip of the V3 loop and cross-compete with the MAb 447-52D and are conformationally sensitive -- MAbs showed cross-clade binding to native, intact virions of clades A(N=2), B(N=4), and F(N=2), limited binding to C(N=3) and D(N=3), and did not bind to CRF01(subtype E, N=2) -- the strength binding was highly correlated with percent neutralization using the ghost cell or PHA blast assay -- five well-characterized MAbs were used as controls: anti-V3 447-52D (anti-V3 MAb for competition and neutralization studies), 654 (anti-CD4BS used as a conformation-sensitive MAb control), 1331A (anti-C5 used as a linear binding site MAb control), MAb 246 (anti-gp41 MAb that bound to primary isolates of all clades) -- 447-52D bound to primary isolates from all clades except CRF01 (E), was conformationally sensitive and showed the some of the most potent neutralizing activity. Gorny2002 (variant cross-recognition or cross-neutralization)
447-52D: The feasibility of determining the NMR structure of the V3(MN) peptide bound to the 447-52D Fab fragment was tested and a general strategy for obtaining NMR structures of V3 peptide-Fab fragments developed -- preliminary NMR spectra for 447-52D complexed to a 23 amino acid V3 peptide was obtained. Sharon2002 (structure)
447-52D: Oligomeric gp140 (o-gp140) derived from R5 primary isolate US4 was characterized for use as a vaccine reagent---antigen capture ELISA was used to compare the antigenicity of gp120 and o-gp140 using a panel of well characterized MAbs---447-D recognized the gp120 monomer much more readily than o-gp140, suggesting the V3 loop is less exposed on o-gp140 and on intact virions. Srivastava2002 (antibody binding site definition and exposure, vaccine antigen design)
447-52D: A panel of 12 MAbs was used to identify those that could neutralize the dual-tropic primary isolate HIV-1 89.6 -- six gave significant neutralization at 2 to 10 ug/ml: 2F5, 50-69, IgG1b12, 447-52D, 2G12, and 670-D six did not have neutralizing activity: 654-D, 4.8D, 450-D, 246-D, 98-6, and 1281 -- no synergy, only additive effects were seen for pairwise combinations of MAbs, and antagonism was noted between gp41 MAbs 50-69 and 98-6, as well as 98-6 and 2F5. Verrier2001 (antibody interactions, variant cross-recognition or cross-neutralization)
447-52D: Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding -- the dissociation constant, Kd of 447-52D for the cell associated primary and TCLA Envs was equal, 3nM. York2001 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization, binding affinity)
447-52D: Six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes. Park2000 (antibody binding site definition and exposure)
447-52D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 447-52D showed the highest cross-reactivity, bound to 24/26 viruses tested, but achieved 90% neutralization only against MN, 50% against CA5, and no neutralization was observed for 3 other isolates tested. Nyambi2000 (subtype comparisons)
447-52D: Called 447D -- SF162 is a neutralization-resistant HIV-1 isolate -- N-linked glycosylation modifications in the V2 loop of the SF162 gp120 revealed that these sites prevent neutralization by CD4BS MAbs (IgG1b12 and IgGCD4), and protect against neutralization by V3 MAbs (447D and 391-95D) -- V2-region glycosylation site mutations did not alter neutralization resistance to V2 MAbs (G3.4 and G3.136) or CD4i MAbs (17b and 48d) -- V2 glycosylation site modification allows infection of macrophages, probably due to glycosylated forms requiring fewer CCR5 molecules for viral entry. Ly2000 (antibody binding site definition and exposure)
447-52D: Ab responses, because of their capacity to alter antigen uptake and processing, can influence helper T cell responses -- CD4BS MAbs or serum Ig from HIV+ individuals inhibited proliferative responses of gp120 specific T cells -- V3 MAbs 447-52-D and 268-10-D did not effect proliferation. Hioe2000
447-52D: To determine the antigenicity of virus killed by thermal and chemical inactivation, retention of conformation-dependent neutralization epitopes was examined, and exposure of CD4BS epitopes was found to be enhanced (MAbs IgG1b12, 205-46-9, and 205-43-1) -- binding to 2G12 and 447-52D epitopes was essentially unaltered -- the 17b CD4i epitope was also exposed. Grovit-Ferbas2000 (vaccine antigen design)
447-52D: Binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- V3 MAbs 447-52D, 838-D, and 1334 bound with a 7-10 fold preference for the oligomer. Gorny2000b (antibody binding site definition and exposure)
447-52D: rgp120 derived from a R5X4 subtype B virus, HIV-1 W61D, was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- TCLA strains showed enhanced 447-52D neutralization sensitivity relative to PBMC-adapted lines (32X increase between HIV-1(M2424/PBMC(p0)) and HIV-1(M2424/H9(p9)) and a >128X increase between HIV-1(W61D/PBMC) and HIV-1(W61D/SupT1) isolates) Beddows1999 (variant cross-recognition or cross-neutralization)
447-52D: The presence of leukocyte function-associated molecule 1 (LFA-1) promotes virus infectivity and hinders neutralization, and anti-LFA-1 MAbs can enhance the neutralizing effect of anti-HIV V3 MAb 447-52D and anti-HIV CD4BS MAb IgG1b12 -- non-neutralizing anti-HIV CD4BS MAb 654-D did not become neutralizing in the presence of anti-LFA-1 MAbs. Hioe1999
447-52D: MAb peptide-reactivity pattern clustered with the immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group -- 447 reacted with peptides containing GPGR, but also with many lacking this sequence (GPGQ, for example), and it failed to react with 2/14 peptides containing GPGR, illustrating the importance of context. Zolla-Pazner1999a (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
447-52D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
447-52D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- 447-52D was the most potent and cross-reactive of 18 human MAbs tested and was the only MAb which bound to virions from isolates CA20 (subtype F), CA13 (subtype H), and VI526 (subtype G) Nyambi1998 (subtype comparisons)
447-52D: Kinetic parameters were measured, and the association rates were similar, but dissociation rate constants were quite variable for V3 MAbs, 1324E was comparable to 447-52D. Gorny1998 (kinetics)
447-52D: Ab from gp120 vaccinated individuals prior to infection, who subsequently became HIV infected, could not achieve 90% neutralization of the primary virus by which the individuals were ultimately infected -- these viruses were not particularly refractive to neutralization, as determined by their susceptibility to neutralization by MAbs 2G12, IgG1b12, 2F5 and 447-52D. Connor1998
447-52D: The MAb and Fab binding to the oligomeric form of gp120 and neutralization were highly correlated -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope. Parren1998 (antibody binding site definition and exposure)
447-52D: Called 447-52-D -- The tip of the MN V3 loop was inserted into cold causing human rhinovirus 14 (HRV14) -- chimeras were immunoselected, and chimeric viruses were neutralized by anti-V3 loop antibodies, and 447-52D was among the Abs used -- chimeric viruses elicited potent NAbs in guinea pigs against ALA-1 and MN. Smith1998 (vaccine antigen design)
447-52D: Inhibits binding of Hx10 to both CD4 positive and negative HeLa cells. Mondor1998 (variant cross-recognition or cross-neutralization)
447-52D: Called 447-D -- 447-D resistance took longer to acquire in virus with the M184V substituted RT, and had the form (AAC N to TAC Y) at position 5 of the V3 loop, rather than the GPGR to GPGR resistance found with wildtype RT. Inouye1998
447-52D: Used as a control for comparison to five V3 RF selected antibodies -- 447-52D was reactive with A, B, and C clade peptides, but not E. Gorny1997 (subtype comparisons)
447-52D: Abs that recognize discontinuous epitopes can identify mimotopes from a phage peptide display library -- 447-52D has an epitope involving the tip of the V3 loop, that was previously studied with this method Keller1993 -- in Keller et al., with no competition, LxGPxR was the most common six-mer, 38% of the peptides -- after competition with a gp120 IIIB ligand (QRGPGR)i, RGPxR was the most common and one peptide had the sequence QRGPGR, showing type specific mimotopes can be enriched by strain specific ligand competition protocols Boots1997. Boots1997,Keller1993 (antibody binding site definition and exposure, mimotopes)
447-52D: Called 447 -- gp120 can inhibit MIP-1alpha from binding to CCR5, but this inhibitory effect is blocked by pre-incubation of gp120 with three anti-V3 MAbs: 447, 257, 1027 -- MAb 670 which binds in the C5 region had no effect. Hill1997 (co-receptor)
447-52D: Neutralizes TCLA strains but not primary isolates. Parren1997 (variant cross-recognition or cross-neutralization)
447-52D: Viral binding inhibition by 447-D was correlated with neutralization (all other neutralizing MAbs tested showed some correlation except 2F5) Ugolini1997 (antibody binding site definition and exposure)
447-52D: Four primary isolates showed distinct patterns of sensitivity to neutralization by polyclonal sera or plasma and MAbs -- BZ167 was the only isolate inhibited by all polyclonal sera and plasma tested, and was also neutralized by 8/17 MAbs, in particular anti-V3 loop (419-D, 447-52D, 782-D, and 838-D), anti-CD4bd (559/64-D, 654-D and 830-D and a cluster II of gp41 directed MAb (98-6) -- isolates 92HT593 and 91US056 were neutralized by V3 loop (419-D, and 447-52D)and cluster II gp41 (98-6) MAbs at higher concentrations -- US4 was neutralized by some of the polyclonal sera/plasma tested and not at all by MAbs individually or by a cocktail of ten MAbs consisting of 419-D, 447-52D, 782-D, 838-D, 559/64-D, 654-D, 450-D, 670-D, 1281-D and 98-6. Hioe1997b (variant cross-recognition or cross-neutralization)
447-52D: Tested using a resting cell neutralization assay. Hioe1997 (assay standardization/improvement)
447-52D: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 447-52D bound monomer, oligomer, and neutralized JRFL. Fouts1997 (antibody binding site definition and exposure)
447-52D: In a multilaboratory blinded study, failed to consistently neutralize any of nine B clade primary isolates -- many of these isolates had the GPGR motif at the apex of the V3 loop. DSouza1997 (variant cross-recognition or cross-neutralization, assay standardization/improvement)
447-52D: Review: called 447-52-D -- only four epitopes have been described which can stimulate a useful neutralizing response to a broad spectrum of primary isolates, represented by the binding sites of MAbs: 447-52-D, 2G12, Fab b12, and 2F5. Sattentau1996 (variant cross-recognition or cross-neutralization, review)
447-52D: Neutralizes JR-FL -- strongly inhibits gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study. Trkola1996b (co-receptor, variant cross-recognition or cross-neutralization)
447-52D: Called 447-52-D -- The sulfated polysaccharide curdlan sulfate (CRDS) binds to the Envelope of T-tropic viruses and neutralizes virus -- CRDS inhibits 447-52D binding. Jagodzinski1996 (antibody binding site definition and exposure)
447-52D: Neutralizing (- complement), no ADCC activity, and no viral enhancing activity. Forthal1995 (ADCC, complement, enhancing activity)
447-52D: Review: the V3 loop motif GPGR is not common outside subtype B isolates, MAb 19b is more cross-reactive than 447-52D. Moore1995c (variant cross-recognition or cross-neutralization)
447-52D: Binding affected by identity of amino acids flanking GPGR core -- poor breadth of primary virus neutralization. Moore1995b (variant cross-recognition or cross-neutralization)
447-52D: Neutralization of primary and prototype laboratory HIV-1 isolates using a resting cell assay enhances sensitivity. Zolla-Pazner1995a (assay development, variant cross-recognition or cross-neutralization)
447-52D: Serotyping study using flow-cytometry -- bound only to GPGR V3 loop tips. Zolla-Pazner1995 (antibody binding site definition and exposure)
447-52D: Ab-mediated activation of complement on HIV+ cells is higher than Ab independent activation---what has been termed ``Ab independent'' in fact results in part from IgM in normal human serum that is HIV-cross-reactive. Saarloos1995 (complement)
447-52D: Called 447 -- The tip of the V3 loop was presented in a mucin backbone -- higher valency correlates with stronger affinity constant. Fontenot1995 (vaccine antigen design)
447-52D: Called 447d -- Formalin inactivation of virus at 0.1% formalin for 10 hours at 4 degrees was optimal for inactivation of virus while maintaining epitope integrity. Sattentau1995 (vaccine antigen design)
447-52D: Competition studies with human sera from seroconverting individuals showed that anti-CD4 BS antibodies can arise very early in infection, comparable or prior to anti-V3 antibodies. Moore1994d (acute/early infection)
447-52D: Mild oxidation of carbohydrate moieties does not alter binding. Gorny1994 (antibody binding site definition and exposure)
447-52D: GPGQ in MAL resulted in enhanced dissociation -- GPGQ in CM234 or K14T did not bind -- binding affected by identity of amino acids flanking GPGR core. VanCott1994 (antibody binding site definition and exposure)
447-52D: Neutralization synergy in combination with CD4 binding domain MAbs. Laal1994 (antibody interactions)
447-52D: Requires GPxR at the tip of the V3 loop, common in B clade -- neutralized primary isolates. Conley1994 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
447-52D: Complement mediated virolysis of IIIB, but not in the presence of sCD4. Spear1993 (complement)
447-52D: Additive neutralization of MN and SF2 when combined with CD4 binding site MAb F105 -- supra-additive neutralization of RF. Cavacini1993 (antibody interactions)
447-52D: Peptide phage library showed that any of the residues ADGLMNQRS in the X position tolerated in peptides that react well with the antibody. Keller1993 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)
447-52D: Neutralizes MN and IIIB: GPGR, and binds SF2: GPGR. Gorny1993 (variant cross-recognition or cross-neutralization)
447-52D: Reacts with MN, NY5, CDC4, SF2, RF, WM52, and HXB2. Karwowska1992a (variant cross-recognition or cross-neutralization)
447-52D: 60-fold increase in neutralization potency when combined 1:1 with human MAb 588-D. Buchbinder1992 (antibody interactions)
447-52D: Requires GPXR at the tip of the V3 loop -- neutralizes a broad array of B clade lab isolates. Gorny1992 (antibody binding site definition and exposure, variant cross-recognition or cross-neutralization)

References

Buchbinder1992 A. Buchbinder, S. Karwowska, M. K. Gorny, S. T. Burda, and S. Zolla-Pazner. Synergy Between Human Monoclonal Antibodies to HIV Extends Their Effective Biologic Activity Against Homologous and Divergent Strains. AIDS Res. Hum. Retroviruses, 8:425-427, 1992. The anti-gp120 V3 MAb 447-D and the anti- gp120 CD4 BS MAb 588-D showed synergistic neutralization. PubMed ID: 1466965. Show all entries for this paper.

Keller1993 P. M. Keller, B. A. Arnold, A. R. Shaw, R. L. Tolman, F. Van Middlesworth, S. Bondy, V. K. Rusiecki, S. Koenig, S. Zolla-Pazner, P. Conard, E. A. Emini, and A. J. Conley. Identification of HIV vaccine candidate peptides by screening random phage epitope libraries. Virology, 193:709-716, 1993. A library of 15 mers was screened for reactivity with 447-52D. 100s of 15 mers reacted, of which 70 were sequenced. All but one contained the motif GPXR. PubMed ID: 7681612. Show all entries for this paper.

Conley1994 A. J. Conley, M. K. Gorny, J. A. Kessler II, L. J. Boots, M. Ossorio-Castro, S. Koenig, D. W. Lineberger, E. A. Emini, C. Williams, and S. Zolla-Pazner. Neutralization of primary human immunodeficiency virus type 1 isolates by the broadly reactive anti-V3 monoclonal antibody 447-52D. J. Virol., 68:6994-7000, 1994. PubMed ID: 7933081. Show all entries for this paper.

Laal1994 S. Laal, S. Burda, M. K. Gorny, S. Karwowska, A. Buchbinder, and S. Zolla-Pazner. Synergistic neutralization of human immunodeficiency virus type 1 by combinations of human monoclonal antibodies. J. Virol., 68:4001-4008, 1994. Antibodies to the C-terminal part of gp120 and the V3 loop were shown to act synergistically with anti-CD4 binding site MAbs in terms of neutralization. C-terminal antibodies did not synergize V3 loop MAb neutralization. PubMed ID: 9424674. Show all entries for this paper.

Gorny1994 M. K. Gorny, J. P. Moore, A. J. Conley, S. Karwowska, J. Sodroski, C. Williams, S. Burda, L. J. Boots, and S. Zolla-Pazner. Human anti-V2 monoclonal antibody that neutralizes primary but not laboratory isolates of human immunodeficiency virus type 1. J. Virol., 68:8312-8320, 1994. Detailed characterization of the MAb 697-D. PubMed ID: 7525987. Show all entries for this paper.

Moore1994d J. P. Moore, Y. Cao, D. D. Ho, and R. A. Koup. Development of the anti-gp120 antibody response during seroconversion to human immunodeficiency virus type 1. J. Virol., 68:5142-5155, 1994. Three seroconverting individuals were studied. The earliest detectable anti-gp120 antibodies were both conformational and anti-V3 loop, and could be detected only after the peak viremia has passed. No uniform pattern of autologous neutralizing anti-CD4BS or anti-V3 MAbs was observed. PubMed ID: 8035514. Show all entries for this paper.

Sattentau1995b Q. J. Sattentau. Conservation of HIV-1 gp120 neutralizing epitopes after formalin inactivation. AIDS, 9:1383-1385, 1995. PubMed ID: 8605064. Show all entries for this paper.

Saarloos1995 M. N. Saarloos, T. F. Lint, and G. T. Spear. Efficacy of HIV-specific and 'antibody-independent' mechanisms for complement activation by HIV-infected cells. Clin. Exp. Immunol., 99:189-195, 1995. PubMed ID: 7851010. Show all entries for this paper.

Sattentau1995 Q. J. Sattentau, S. Zolla-Pazner, and P. Poignard. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology, 206:713-717, 1995. Most gp41 epitopes are masked when associated with gp120 on the cell surface. Weak binding of anti-gp41 MAbs can be enhanced by treatment with sCD4. MAb 2F5 binds to a membrane proximal epitope which binds in the presence of gp120 without sCD4. PubMed ID: 7530400. Show all entries for this paper.

Zolla-Pazner1995a S. Zolla-Pazner and S. Sharpe. A resting cell assay for improved detection of antibody-mediated neutralization of HIV type 1 primary isolates. AIDS Res. Hum. Retroviruses, 11:1449-1458, 1995. PubMed ID: 8679288. Show all entries for this paper.

Moore1995b J. P. Moore, Y. Cao, L. Qing, Q. J. Sattentau, J. Pyati, R. Koduri, J. Robinson, C. F. Barbas III, D. R. Burton, and D. D. Ho. Primary isolates of human immunodeficiency virus type I are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120. J. Virol., 69:101-109, 1995. A panel of anti-gp120 MAbs and sera from HIV-1 infected individuals was tested for its ability to neutralize primary isolates. Most MAbs bound with high affinity to gp120 monomers from the various isolates, but were not effective at neutralizing. The MAb IgG1b12, which binds to a discontinuous anti-CD4 binding site epitope, was able to neutralize most of the primary isolates. PubMed ID: 7527081. Show all entries for this paper.

Moore1995c J. P. Moore and D. D. Ho. HIV-1 neutralization: the consequences of adaptation to growth on transformed T-cells. AIDS, 9 suppl A:S117-S136, 1995. This review considers the relative importance of a neutralizing antibody response for the development of a vaccine, and for disease progression during the chronic phase of HIV-1 infection. It suggests that T-cell immunity may be more important. The distinction between MAbs that can neutralize primary isolates, and those that are effective at neutralizing only laboratory adapted strains is discussed in detail. Alternative conformations of envelope and non-contiguous interacting domains in gp120 are discussed. The suggestion that soluble monomeric gp120 may serve as a viral decoy that diverts the humoral immune response it in vivo is put forth. PubMed ID: 8819579. Show all entries for this paper.

Forthal1995 D. N. Forthal, G. Landucci, M. K. Gorny, S. Zolla-Pazner, and W. E. Robinson, Jr. Functional activities of 20 human immunodeficiency virus type 1 (HIV-1)-specific human monoclonal antibodies. AIDS Res. Hum. Retroviruses, 11:1095-1099, 1995. A series of tests were performed on 20 human monoclonal antibodies to assess their potential therapeutic utility. Antibodies were tested for potentially harmful complement-mediated antibody enhancing activity (C-ADE), and for potentially beneficial neutralizing activity and antibody dependent cellular cytotoxicity ADCC. PubMed ID: 8554906. Show all entries for this paper.

Jagodzinski1996 P. P. Jagodzinski, J. Wustner, D. Kmieciak, T. J. Wasik, A. Fertala, A. L. Sieron, M. Takahashi, T. Tsuji, T. Mimura, M. S. Fung, M. K. Gorny, M. Kloczewiak, Y. Kaneko, and D. Kozbor. Role of the V2, V3, and CD4-binding domains of GP120 in curdlan sulfate neutralization sensitivity of HIV-1 during infection of T lymphocytes. Virology, 226:217-227, 1996. PubMed ID: 8955041. Show all entries for this paper.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. Show all entries for this paper.

Sattentau1996 Q. J. Sattentau. Neutralization of HIV-1 by antibody. Curr. Opin. Immunol., 8:540-545, 1996. Review. PubMed ID: 8794008. Show all entries for this paper.

DSouza1997 M. P. D'Souza, D. Livnat, J. A. Bradac, S. H. Bridges, the AIDS Clinical Trials Group Antibody Selection Working Group, and Collaborating Investigators. Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: performance criteria for selecting candidate antibodies for clinical trials. J. Infect. Dis., 175:1056-1062, 1997. Five laboratories evaluated neutralization of nine primary B clade isolates by a coded panel of seven human MAbs to HIV-1 subtype B envelope. IgG1b12, 2G12, 2F5 showed potent and broadly cross-reactive neutralizing ability; F105, 447/52-D, 729-D, 19b did not neutralize the primary isolates. PubMed ID: 9129066. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Fouts1997 T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632. Show all entries for this paper.

Hioe1997 C. Hioe, S. Burda, P. Chigurupati, S. Xu, and S. Zolla-Pazner. Resting cell neutralization assay for HIV-1 primary isolates. Methods: A companion to Methods in Enzymology, 12:300-5, 1997. A technique is described for detecting the activity of neutralizing polyclonal or MAbs against HIV-1 primary isolates, using unstimulated PBMC as the target cell. PubMed ID: 9245610. Show all entries for this paper.

Boots1997 L. J. Boots, P. M. McKenna, B. A. Arnold, P. M. Keller, M. K. Gorny, S. Zolla-Pazner, J. E. Robinson, and A. J. Conley. Anti-human immunodeficiency virus type 1 human monoclonal antibodies that bind discontinuous epitopes in the viral glycoproteins can identify mimotopes from recombinant phage peptide display libraries. AIDS Res. Hum. Retroviruses, 13:1549-59, 1997. PubMed ID: 9430247. Show all entries for this paper.

Parren1997 P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the antibody response against human immunodeficiency virus type 1 Envelope to vaccine design [corrected and republished article originally printed in Immunol Lett 1997 Jun 1;57(1-3):105-12]. Immunol. Lett., 58:125-32, 1997. PubMed ID: 9271324. Show all entries for this paper.

Ugolini1997 S. Ugolini, I. Mondor, P. W. H. I Parren, D. R. Burton, S. A. Tilley, P. J. Klasse, and Q. J. Sattentau. Inhibition of virus attachment to CD4+ target cells is a major mechanism of T cell line-adapted HIV-1 neutralization. J. Exp. Med., 186:1287-1298, 1997. PubMed ID: 9334368. Show all entries for this paper.

Inouye1998 P. Inouye, E. Cherry, M. Hsu, S. Zolla-Pazner, and M. A. Wainberg. Neutralizing antibodies directed against the V3 loop select for different escape variants in a virus with mutated reverse transcriptase (M184V) than in wild-type human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 14:735-40, 1998. The M184V substitution in RT yields high level resistance to 3TC and low level resistance to ddI and ddC, and alters the properties of RT. Virus containing the wt form of RT grown in the presence of the MAb 447-D develops 447-D resistance in 36 days, with the GPGR to GPGK substitutions (AGA(R) to AAA(K)). 447-D resistance took longer to acquire in virus with the M184V substituted RT, and had the form CTRPN to CTRPY (AAC(N) to TAC(Y)) at position 5 of the V3 loop. PubMed ID: 9643373. Show all entries for this paper.

Mondor1998 I. Mondor, S. Ugolini, and Q. J. Sattentau. Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans. J. Virol., 72:3623-34, 1998. PubMed ID: 9557643. Show all entries for this paper.

Smith1998 A. D. Smith, S. C. Geisler, A. A. Chen, D. A. Resnick, B. M. Roy, P. J. Lewi, E. Arnold, and G. F. Arnold. Human rhinovirus type 14:human immunodeficiency virus type 1 (HIV-1) V3 loop chimeras from a combinatorial library induce potent neutralizing antibody responses against HIV-1. J. Virol., 72:651-9, 1998. The tip of the MN V3 loop, IGPGRAFYTTKN, was inserted into cold-causing human rhinovirus 14 (HRV14) and chimeras were immunoselected using MAbs 447-52-D, 694/98-D, NM-01, and 59.1, for good presentation of the V3 antigenic region. The selected chimeric viruses were neutralized by anti-V3 loop MAbs. The chimeric viruses elicited potent NAbs against ALA-1 and MN in guinea pigs. PubMed ID: 9420270. Show all entries for this paper.

Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.

Connor1998 R. I. Connor, B. T. Korber, B. S. Graham, B. H. Hahn, D. D. Ho, B. D. Walker, A. U. Neumann, S. H. Vermund, J. Mestecky, S. Jackson, E. Fenamore, Y. Cao, F. Gao, S. Kalams, K. J. Kunstman, D. McDonald, N. McWilliams, A. Trkola, J. P. Moore, and S. M. Wolinsky. Immunological and virological analyses of persons infected by human immunodeficiency virus type 1 while participating in trials of recombinant gp120 subunit vaccines. J. Virol., 72:1552-76, 1998. No gp120-vaccine induced antibodies in a human trial of gp120 MN and SF2 could neutralize the primary viruses that infected the vaccinees. The primary isolates from the infected vaccinees were shown not to be particularly refractive to neutralization by their susceptibility to a panel of neutralizing MAbs. PubMed ID: 9445059. Show all entries for this paper.

Hioe1999 C. E. Hioe, J. E. Hildreth, and S. Zolla-Pazner. Enhanced HIV type 1 neutralization by human anti-glycoprotein 120 monoclonal antibodies in the presence of monoclonal antibodies to lymphocyte function-associated molecule 1. AIDS Res. Hum. Retroviruses, 15:523-31, 1999. PubMed ID: 10221529. Show all entries for this paper.

Grovit-Ferbas2000 K. Grovit-Ferbas, J. F. Hsu, J. Ferbas, V. Gudeman, and I. S. Chen. Enhanced binding of antibodies to neutralization epitopes following thermal and chemical inactivation of human immunodeficiency virus type 1. J. Virol., 74(13):5802-9, Jul 2000. URL: http://jvi.asm.org/cgi/content/full/74/13/5802. PubMed ID: 10846059. Show all entries for this paper.

Verrier2001 F. Verrier, A. Nadas, M. K. Gorny, and S. Zolla-Pazner. Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6. J. Virol., 75(19):9177--86, Oct 2001. URL: http://jvi.asm.org/cgi/content/full/75/19/9177. PubMed ID: 11533181. Show all entries for this paper.

Srivastava2002 Indresh K. Srivastava, Leonidas Stamatatos, Harold Legg, Elaine Kan, Anne Fong, Stephen R. Coates, Louisa Leung, Mark Wininger, John J. Donnelly, Jeffrey B. Ulmer, and Susan W. Barnett. Purification and Characterization of Oligomeric Envelope Glycoprotein from a Primary R5 Subtype B Human Immunodeficiency Virus. J. Virol., 76(6):2835-2847, Mar 2002. URL: http://jvi.asm.org/cgi/content/full/76/6/2835. PubMed ID: 11861851. Show all entries for this paper.

Sharon2002 Michal Sharon, Matthias G\"orlach, Rina Levy, Yehezkiel Hayek, and Jacob Anglister. Expression, Purification, and Isotope Labeling of a gp120 V3 Peptide and Production of a Fab from a HIV-1 Neutralizing Antibody for NMR Studies. Protein Expr Purif, 24(3):374-383, Apr 2002. PubMed ID: 11922753. Show all entries for this paper.

Gorny2002 Miroslaw K. Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Sandra Cohen, Victoria R. Polonis, William J. Honnen, Samuel C. Kayman, Chavdar Krachmarov, Abraham Pinter, and Susan Zolla-Pazner. Human Monoclonal Antibodies Specific for Conformation-Sensitive Epitopes of V3 Neutralize Human Immunodeficiency Virus Type 1 Primary Isolates from Various Clades. J. Virol., 76(18):9035-9045, Sep 2002. PubMed ID: 12186887. Show all entries for this paper.

Ferrantelli2002 Flavia Ferrantelli and Ruth M. Ruprecht. Neutralizing Antibodies Against HIV --- Back in the Major Leagues? Curr. Opin. Immunol., 14(4):495-502, Aug 2002. PubMed ID: 12088685. Show all entries for this paper.

Poignard2003 Pascal Poignard, Maxime Moulard, Edwin Golez, Veronique Vivona, Michael Franti, Sara Venturini, Meng Wang, Paul W. H. I. Parren, and Dennis R. Burton. Heterogeneity of Envelope Molecules Expressed on Primary Human Immunodeficiency Virus Type 1 Particles as Probed by the Binding of Neutralizing and Nonneutralizing Antibodies. J. Virol., 77(1):353-365, Jan 2003. PubMed ID: 12477840. Show all entries for this paper.

Binley2003 James M. Binley, Charmagne S. Cayanan, Cheryl Wiley, Norbert Schülke, William C. Olson, and Dennis R. Burton. Redox-Triggered Infection by Disulfide-Shackled Human Immunodeficiency Virus Type 1 Pseudovirions. J. Virol., 77(10):5678-5684, May 2003. PubMed ID: 12719560. Show all entries for this paper.

Kessler2003 Naama Kessler, Anat Zvi, Min Ji, Michal Sharon, Osnat Rosen, Rina Levy, Miroslaw Gorny, Suzan Zolla-Pazner, and Jacob Anglister. Expression, Purification, and Isotope Labeling of the Fv of the Human HIV-1 Neutralizing Antibody 447-52D for NMR Studies. Protein. Expr. Purif., 29(2):291-303, Jun 2003. PubMed ID: 12767822. Show all entries for this paper.

Zwick2003 Michael B. Zwick, Paul W. H. I. Parren, Erica O. Saphire, Sarah Church, Meng Wang, Jamie K. Scott, Philip E. Dawson, Ian A. Wilson, and Dennis R. Burton. Molecular Features of the Broadly Neutralizing Immunoglobulin G1 b12 Required for Recognition of Human Immunodeficiency Virus Type 1 gp120. J. Virol., 77(10):5863-5876, May 2003. PubMed ID: 12719580. Show all entries for this paper.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. Show all entries for this paper.

Binley2004 James M. Binley, Terri Wrin, Bette Korber, Michael B. Zwick, Meng Wang, Colombe Chappey, Gabriela Stiegler, Renate Kunert, Susan Zolla-Pazner, Hermann Katinger, Christos J. Petropoulos, and Dennis R. Burton. Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal Antibodies. J. Virol., 78(23):13232-13252, Dec 2004. PubMed ID: 15542675. Show all entries for this paper.

Ling2004 Hong Ling, Peng Xiao, Osamu Usami, and Toshio Hattori. Thrombin Activates Envelope Glycoproteins of HIV Type 1 and Enhances Fusion. Microbes Infect., 6(5):414-420, Apr 2004. PubMed ID: 15109955. Show all entries for this paper.

Pantophlet2004 R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540. Show all entries for this paper.

Pinter2004 Abraham Pinter, William J. Honnen, Yuxian He, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The V1/V2 Domain of gp120 Is a Global Regulator of the Sensitivity of Primary Human Immunodeficiency Virus Type 1 Isolates to Neutralization by Antibodies Commonly Induced upon Infection. J. Virol., 78(10):5205-5215, May 2004. PubMed ID: 15113902. Show all entries for this paper.

Pugach2004 Pavel Pugach, Shawn E. Kuhmann, Joann Taylor, Andre J. Marozsan, Amy Snyder, Thomas Ketas, Steven M. Wolinsky, Bette T. Korber, and John P. Moore. The Prolonged Culture of Human Immunodeficiency Virus Type 1 in Primary Lymphocytes Increases its Sensitivity to Neutralization by Soluble CD4. Virology, 321(1):8-22, 30 Mar 2004. PubMed ID: 15033560. Show all entries for this paper.

Sharpe2004 Simon Sharpe, Naama Kessler, Jacob A. Anglister, Wai-Ming Yau, and Robert Tycko. Solid-State NMR Yields Structural Constraints on the V3 Loop from HIV-1 Gp120 Bound to the 447-52D Antibody Fv Fragment. J. Am. Chem. Soc., 126(15):4979-4990, 21 Apr 2004. PubMed ID: 15080704. Show all entries for this paper.

Gorny2005 Miroslaw K. Gorny, Leonidas Stamatatos, Barbara Volsky, Kathy Revesz, Constance Williams, Xiao-Hong Wang, Sandra Cohen, Robert Staudinger, and Susan Zolla-Pazner. Identification of a New Quaternary Neutralizing Epitope on Human Immunodeficiency Virus Type 1 Virus Particles. J. Virol., 79(8):5232-5237, Apr 2005. PubMed ID: 15795308. Show all entries for this paper.

Haynes2005 Barton F. Haynes, Judith Fleming, E. William St. Clair, Herman Katinger, Gabriela Stiegler, Renate Kunert, James Robinson, Richard M. Scearce, Kelly Plonk, Herman F. Staats, Thomas L. Ortel, Hua-Xin Liao, and S. Munir Alam. Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies. Science, 308(5730):1906-1908, 24 Jun 2005. Comment in Science 2005 Jun 24;308(5730):1878-9. PubMed ID: 15860590. Show all entries for this paper.

Krachmarov2005 Chavdar Krachmarov, Abraham Pinter, William J. Honnen, Miroslaw K. Gorny, Phillipe N. Nyambi, Susan Zolla-Pazner, and Samuel C. Kayman. Antibodies That Are Cross-Reactive for Human Immunodeficiency Virus Type 1 Clade A and Clade B V3 Domains Are Common in Patient Sera from Cameroon, but Their Neutralization Activity Is Usually Restricted by Epitope Masking. J. Virol., 79(2):780-790, Jan 2005. PubMed ID: 15613306. Show all entries for this paper.

Martin-Garcia2005 Julio Martín-García, Simon Cocklin, Irwin M. Chaiken, and Francisco González-Scarano. Interaction with CD4 and Antibodies to CD4-Induced Epitopes of the Envelope gp120 from a Microglial Cell-Adapted Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 79(11):6703-6713, Jun 2005. PubMed ID: 15890908. Show all entries for this paper.

Pinter2005 Abraham Pinter, William J. Honnen, Paul D'Agostino, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The C108g Epitope in the V2 Domain of gp120 Functions as a Potent Neutralization Target When Introduced into Envelope Proteins Derived from Human Immunodeficiency Virus Type 1 Primary Isolates. J. Virol., 79(11):6909-6917, Jun 2005. PubMed ID: 15890930. Show all entries for this paper.

Selvarajah2005 Suganya Selvarajah, Bridget Puffer, Ralph Pantophlet, Mansun Law, Robert W. Doms, and Dennis R. Burton. Comparing Antigenicity and Immunogenicity of Engineered gp120. J. Virol., 79(19):12148-12163, Oct 2005. PubMed ID: 16160142. Show all entries for this paper.

Haynes2006a Barton F. Haynes and David C. Montefiori. Aiming to Induce Broadly Reactive Neutralizing Antibody Responses with HIV-1 Vaccine Candidates. Expert Rev. Vaccines, 5(4):579-595, Aug 2006. PubMed ID: 16989638. Show all entries for this paper.

Holl2006a Vincent Holl, Maryse Peressin, Sylvie Schmidt, Thomas Decoville, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Efficient Inhibition of HIV-1 Replication in Human Immature Monocyte-Derived Dendritic Cells by Purified Anti-HIV-1 IgG without Induction of Maturation. Blood, 107(11):4466-4474, 1 Jun 2006. PubMed ID: 16469871. Show all entries for this paper.

Dhillon2007 Amandeep K. Dhillon, Helen Donners, Ralph Pantophlet, Welkin E. Johnson, Julie M. Decker, George M. Shaw, Fang-Hua Lee, Douglas D. Richman, Robert W. Doms, Guido Vanham, and Dennis R. Burton. Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors. J. Virol., 81(12):6548-6562, Jun 2007. PubMed ID: 17409160. Show all entries for this paper.

Kraft2007 Zane Kraft, Nina R. Derby, Ruth A. McCaffrey, Rachel Niec, Wendy M. Blay, Nancy L. Haigwood, Eirini Moysi, Cheryl J. Saunders, Terri Wrin, Christos J. Petropoulos, M. Juliana McElrath, and Leonidas Stamatatos. Macaques Infected with a CCR5-Tropic Simian/Human Immunodeficiency Virus (SHIV) Develop Broadly Reactive Anti-HIV Neutralizing Antibodies. J. Virol., 81(12):6402-6411, Jun 2007. PubMed ID: 17392364. Show all entries for this paper.

Law2007 Mansun Law, Rosa M. F. Cardoso, Ian A. Wilson, and Dennis R. Burton. Antigenic and Immunogenic Study of Membrane-Proximal External Region-Grafted gp120 Antigens by a DNA Prime-Protein Boost Immunization Strategy. J. Virol., 81(8):4272-4285, Apr 2007. PubMed ID: 17267498. Show all entries for this paper.

Nelson2007 Josh D. Nelson, Florence M. Brunel, Richard Jensen, Emma T. Crooks, Rosa M. F. Cardoso, Meng Wang, Ann Hessell, Ian A. Wilson, James M. Binley, Philip E. Dawson, Dennis R. Burton, and Michael B. Zwick. An Affinity-Enhanced Neutralizing Antibody against the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 gp41 Recognizes an Epitope between Those of 2F5 and 4E10. J. Virol., 81(8):4033-4043, Apr 2007. PubMed ID: 17287272. Show all entries for this paper.

Pantophlet2007 Ralph Pantophlet, Rowena O. Aguilar-Sino, Terri Wrin, Lisa A. Cavacini, and Dennis R. Burton. Analysis of the Neutralization Breadth of the Anti-V3 Antibody F425-B4e8 and Re-assessment of its Epitope Fine Specificity by Scanning Mutagenesis. Virology, 364(2):441-453, 1 Aug 2007. PubMed ID: 17418361. Show all entries for this paper.

Chakraborty2006 Kausik Chakraborty, Venuka Durani, Edward Roshan Miranda, Michael Citron, Xiaoping Liang, William Schleif, Joseph G. Joyce, and Raghavan Varadarajan. Design of Immunogens That Present the Crown of the HIV-1 V3 Loop in a Conformation Competent to Generate 447-52D-Like Antibodies. Biochem. J., 399(3):483-491, 1 Nov 2006. PubMed ID: 16827663. Show all entries for this paper.

Cham2006 Fatim Cham, Peng Fei Zhang, Leo Heyndrickx, Peter Bouma, Ping Zhong, Herman Katinger, James Robinson, Guido van der Groen, and Gerald V. Quinnan, Jr. Neutralization and Infectivity Characteristics of Envelope Glycoproteins from Human Immunodeficiency Virus Type 1 Infected Donors Whose Sera Exhibit Broadly Cross-Reactive Neutralizing Activity. Virology, 347(1):36-51, 30 Mar 2006. PubMed ID: 16378633. Show all entries for this paper.

Haynes2006 Barton F. Haynes, Benjiang Ma, David C. Montefiori, Terri Wrin, Christos J. Petropoulos, Laura L. Sutherland, Richard M. Scearce, Cathrine. Denton, Shi-Mao Xia, Bette T. Korber, and Hua-Xin Liao. Analysis of HIV-1 Subtype B Third Variable Region Peptide Motifs for Induction of Neutralizing Antibodies against HIV-1 Primary Isolates. Virology, 345(1):44-55, 5 Feb 2006. PubMed ID: 16242749. Show all entries for this paper.

Displaying record number 506

MAb ID	694/98-D (694/98, 694.8, 694/98D)
HXB2 Location	gp160(314-317)	gp160 Epitope Map
Author Location	gp120( IIIB)
Research Contact	Dr. Zolla-Pazner, Veterans Affairs Center, NY, NY. zollas01@endeavor.med.nyu.edu
Epitope	`GRAF`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3
Neutralizing	L
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody interactions, review, variant cross-recognition or cross-neutralization

Notes

694-98D: The role of serine proteases on HIV infection was explored. Trypsin decreased the binding of most Env MAb tested and diminished cell fusion of H9 cells infected with HIV-1 LAI virus (H9/IIIB) to MAGI cells. In contrast, thrombin increased the binding of MAbs to gp120 epitopes near the CD4 and CCR5 binding sites, and increased cell fusion. Binding of the V3 MAbs 694-98D and 447-52D, that both bind near the tip of the loop, was decreased by both thrombin and trypsin. Ling2004 (antibody binding site definition and exposure)
694/98-D: Called 694/98. V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using IIIB gp120. Gorny2004 (antibody binding site definition and exposure)
694/98D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (variant cross-recognition or cross-neutralization, review)
694/98D: scFv 4KG5 reacts with a conformational epitope that is formed by the V1V2 and V3 loops and the bridging sheet (C4) region of gp120 and is influenced by carbohydrates. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120 JRFL. MAbs to the following regions diminished 4KG5 binding: V2 loop, V3 loop, V3-C4 region, CD4BS. MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected by these loops. This was one of the V3 MAbs used. Zwick2003 (antibody interactions)
694/98-D: Called 694 -- Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A(CD4BS) , 4117C (plus others, V3) and 697D (and SC258, V2) were used as controls. He2002
694/98-D: Called 694/98D -- Truncation of the gp41 cytoplasmic domain of X4, R5, and X4R5 viruses forces a conformation that more closely resembles the CD4 bound state of the external Envelope, enhancing binding of CD4i MAbs 17b and 48d and of CD4BS MAbs F105, b12, and in most cases of glycosylation site dependent MAb 2G12 and the anti-gp41 MAb 246D -- in contrast, binding of the anti-V2 MAb 697D and the anti-V3 MAb 694/98D were not affected -- viruses bearing the truncation were more sensitive to neutralization by MAbs 48d, b12, and 2G12 -- the anti-C5 MAb 1331A was used to track levels of cell surface expression of the mutated proteins. EdwardsBH2002
694/98-D: Called 694/98D -- six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes. Park2000
694/98-D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 694/98-D showed intermediate reactivity. Nyambi2000
694/98-D: A Semliki Forest virus (SFV) expression system carrying BX08 env was used to study the conformation of gp120 -- intracytoplasmic gp120 was recognized by the anti-V3 MAbs K24 and F5.5, while gp120 at the plasma membrane was detected only by conformation dependent MAbs 2G12, 670-D and 694/98D and not linear V3 MAbs -- expression in rat brain also showed that surface-expressed Env was recognized only by the conformation-dependent antibodies and not by anti-V3 antibodies. Altmeyer1999
694/98-D: MAb peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group. Zolla-Pazner1999a
694/98-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b
694/98-D: In a study of the influence of the glycan at position 306 of the V3 loop on MAb recognition, anti-V3 MAbs were found to neutralize an HIV-BRU mutant virus that lacks the V3 loop glycan more efficiently than HIV-BRU. Schonning1998
694/98-D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- 694/98-D bound only to B and D clade virions and had limited cross reactivity. Nyambi1998
694/98-D: Neutralization synergy was observed when the MAbs 694/98-D (V3), 2F5 (gp41), and 2G12 (gp120 discontinuous) were used in combination, and even greater neutralizing potential was seen with the addition of a fourth MAb, F105 (CD4 BS) Li1998
694/98-D: The tip of the MN V3 loop was inserted into cold causing human rhinovirus 14 (HRV14) -- chimeras were immunoselected, and chimeric viruses were neutralized by anti-V3 loop antibodies, and 694/98-D was among the Abs used -- chimeric viruses elicited potent NAbs in guinea pigs against ALA-1 and MN. Smith1998
694/98-D: Used to study pre- and post-exposure prophylaxis Hu-PBL-SCID mice infected by an intraperitoneal injection of HIV-1 LAI -- MAb half-life in plasma in mice is 9 days -- 2 hours post-694/98-D mice were challenged with LAI, and at an Ab concentration of 1.32 mg/Kg, 50% of the mice were infected -- one of the infected mice carried the resistant form GRTF rather than GRAF (critical amino acids for binding are GRA) -- post-exposure prophylaxis was effective if delivered 15 min post-exposure, but declined to 50% if delivered 60 min post-exposure, and similar time constraints have been observed for HIVIG, 2F5 and 2G12, in contrast to MAb BAT123 that could protect delivered 4 hours post infection. Andrus1998
694/98-D: One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB env -- could only achieve 50% neutralization alone -- all Ab combinations tested showed synergistic neutralization -- 694/98-D has synergistic response with MAbs F105, 15e, b12, 2F5, 17b, 2G12, and 48d, and with HIVIG. Li1997
694/98-D: ADCC activity, and no viral enhancing activity. Forthal1995
694/98-D: Serotyping study using flow-cytometry -- bound GRAX bearing virus in 10/11 cases -- somewhat conformation dependent. Zolla-Pazner1995
694/98-D: Human HIV-1 infected sera and MAb 694/98 have high reactivity to MN and RF infected H9 cells, but Genentech rec gp120 IIIB vaccine recipients do not. VanCott1995
694/98-D: MAbs against the glycosphingolipid GalCer block HIV infection of normally susceptible CD4 negative cells from the brain and colon -- V3 MAbs can inhibit gp120 binding to GalCer in vitro -- binding of GalCer to gp120 inhibited but did not completely block MAb binding. Cook1994
694/98-D: GRVY did not alter peptide binding -- GRVI and GQAW enhanced dissociation -- GQVF and GQAL did not bind. VanCott1994
694/98-D: Potent neutralization of IIIB -- no neutralization synergy in combination with CD4 binding domain MAbs. Laal1994
694/98-D: 50% neutralization of HIV-IIIB at a concentration of 0.15mug/ml. Gorny1994
694/98-D: Called 694-D -- complement mediated virolysis of IIIB, but not in the presence of sCD4. Spear1993
694/98-D: Neutralizes MN and IIIB (GRAF) -- binds SF2 (GRAF) -- binding reactivity: MN, IIIB, SF2, NY5, RF, CDC4, WM52. Gorny1993
694/98-D: Type-specific lab isolate neutralization was observed -- binds with 1-3 fold greater affinity to gp120 than to peptides. Gorny1992
694/98-D: This MAb was first described here. Skinner1988

References

Skinner1988 M. A. Skinner, R. Ting, A. J. Langlois, K. J. Weinhold, H. K. Lyerly, K. Javaherian, and T. J. Matthews. Characteristics of a neutralizing monoclonal antibody to the HIV envelope glycoprotein. AIDS Res. Hum. Retroviruses, 4:187-197, 1988. PubMed ID: 2456088. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of human immunodeficiency virus type 1 HIV-1 gp120 to Galactosylceramide (GalCer): relationship to the V3 loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

VanCott1995 T. C. VanCott, F. R. Bethke, D. S. Burke, R. R. Redfield, and D. L. Birx. Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines. J. Immunol., 155:4100-4110, 1995. The Ab response in both HIV-1 infected and uninfected volunteers immunized with HIV-1 rec envelope subunit vaccines (Genentech gp120IIIB, MicroGeneSys gp160IIIB, or ImmunoAG gp160IIIB) preferentially induced Abs reactive only to the denatured form of gp120. This may explain the inability of the vaccinee sera to neutralize primary HIV-1 isolates. PubMed ID: 7561123. Show all entries for this paper.

Li1997 A. Li, T. W. Baba, J. Sodroski, S. Zolla-Pazner, M. K. Gorny, J. Robinson, M. R. Posner, H. Katinger, C. F. Barbas III, D. R. Burton, T.-C. Chou, and R. M Ruprecht. Synergistic neutralization of a chimeric SIV/HIV type 1 virus with combinations of human anti-HIV type 1 envelope monoclonal antibodies or hyperimmune globulins. AIDS Res. Hum. Retroviruses, 13:647-656, 1997. Multiple combinations of MAbs were tested for their ability to synergize neutralization of a SHIV construct containing HIV IIIB env. All of the MAb combinations tried were synergistic, suggesting such combinations may be useful for passive immunotherapy or immunoprophylaxis. Because SHIV can replicate in rhesus macaques, such approaches can potentially be studied in an it in vivo monkey model. PubMed ID: 9168233. Show all entries for this paper.

Zolla-Pazner1997 S. Zolla-Pazner, C. Alving, R. Belshe, P. Berman, S. Burda, P. Chigurupati, M. L. Clements ML, A. M. Duliege, J. L. Excler, C. Hioe, J. Kahn, M. J. McElrath, S. Sharpe, F. Sinangil, K. Steimer, M. C. Walker, N. Wassef, and S. Xu. Neutralization of a clade B primary isolate by sera from human immunodeficiency virus-uninfected recipients of candidate AIDS vaccines. J. Infect. Dis., 175:764-774, 1997. Comment in J Infect Dis 1997 Nov;176(5):1410-2. Clade B primary isolate BZ167 was neutralized, using a new assay, by sera from HIV-uninfected volunteers in vaccine trials. PubMed ID: 9086128. Show all entries for this paper.

Li1998 A. Li, H. Katinger, M. R. Posner, L. Cavacini, S. Zolla-Pazner, M. K. Gorny, J. Sodroski, T. C. Chou, T. W. Baba, and R. M. Ruprecht. Synergistic neutralization of simian-human immunodeficiency virus SHIV- vpu+ by triple and quadruple combinations of human monoclonal antibodies and high-titer anti-human immunodeficiency virus type 1 immunoglobulins. J. Virol., 72:3235-40, 1998. PubMed ID: 9525650. Show all entries for this paper.

Andrus1998 L. Andrus, A. M. Prince, I. Bernal, P. McCormack, D. H. Lee, M. K. Gorny, and S. Zolla-Pazner. Passive immunization with a human immunodeficiency virus type 1- neutralizing monoclonal antibody in Hu-PBL-SCID mice: isolation of a neutralization escape variant. J. Infect. Dis., 177:889-97, 1998. PubMed ID: 9534960. Show all entries for this paper.

Schonning1998 K. Schonning, A. Bolmstedt, J. Novotny, O. S. Lund, S. Olofsson, and J. E. Hansen. Induction of antibodies against epitopes inaccessible on the HIV type 1 envelope oligomer by immunization with recombinant monomeric glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:1451-6, 1998. PubMed ID: 9824323. Show all entries for this paper.

Altmeyer1999 R. Altmeyer, E. Mordelet, M. Girard, and C. Vidal. Expression and detection of macrophage tropic HIV-1 gp120 in the brain using conformation-dependent antibodies. Virology, 259:314-21, 1999. PubMed ID: 10388656. Show all entries for this paper.

EdwardsBH2002 Bradley H. Edwards, Anju Bansal, Steffanie Sabbaj, Janna Bakari, Mark J. Mulligan, and Paul A. Goepfert. Magnitude of Functional CD8+ T-cell responses to the Gag Protein of Human Immunodeficiency Virus Type 1 Correlates Inversely with Viral Load in Plasma. J. Virol., 76(5):2298-2305, Mar 2002. PubMed ID: 11836408. Show all entries for this paper.

Displaying record number 947

MAb ID	1108
HXB2 Location	Env	Env Epitope Map
Author Location	Env( 987)
Epitope
Subtype	B
Ab Type	gp120 V3 mimotope
Neutralizing	P
Species (Isotype)	human(IgG1λ)
Immunogen	HIV-1 infection
Keywords	antibody binding site definition and exposure, antibody generation, mimotopes, review

Notes

1108: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides. Gorny2004 (antibody binding site definition and exposure)
1108: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. Gorny2003 (review)
1108: The sequence of peptide 987, used to select MAb 1108, is ADGAWRSVHLGPGRGSGSGMGK. Zolla-Pazner1999b (antibody binding site definition and exposure, antibody generation)
1108: Selected with peptide 987, a mimotope of anti-V3 MAb 447-D -- MAb peptide reactivity pattern clustered with immunological related MAbs: 1108, 386, 268, 311, 257, 694.8 -- the amino acids HI tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site definition and exposure, antibody generation, mimotopes)