Karamov E, Ulmasov KA, Blinov VM; International Conference on AIDS.
Int Conf AIDS. 1993 Jun 6-11; 9: 181 (abstract no. PO-A14-0277).
D.I. Ivanovsky Institute of Virology, Moscow, Russia.
HSP assist other proteins in folding, translocation and assemble. The cell may exploit these functions of HSP to help protect it from the deleterious effects of stress. HSP can be induced in cells following infection by a variety of viruses in vitro. We have studied the parameters of HSP synthesis in HIV infected cells. We identified 3 constitutive HSP 72 forms. HS response of HIV-infected and non-infected cells is identical in increasing the synthesis of HSPs which are produced at 37 C, while the differences are connected with biosynthesis of strictly inducible HSP72 forms. HIV infection changes the spectrum of proteins normally synthesized at 37 C. The synthesis of many proteins markedly slows down, but the synthesis of p78, p74, p40, p32 proteins of host cell origin with an unknown function increases. P78 was found to be identical to BIP, immunoglobulin heavy chain binding protein, previously isolated from lymphoid cells. Probably binding with BIP increases the efficiency of env assembly in oligomeric structures. We suggest, BIP will be find in a complex with env monomers until oligomers were formed. Defective env proteins unable to form oligomers, remain in a BIP complex and are not secreted. We detected 4 heat shock regulatory site (HSRS) in HIV-genome: 2 HSRS-in promoters, 1 HSRS-in pol gene, 1 HSRS-in tat region. All of HSRS were shown to contain the region of non-random homology with different mobile genetical elements. Evolutionary significance of HSRS in HIV genome based on the transcriptional activation of HSRS by heat-shock and some other factors, has been discussed.
Publication Types:
Keywords:
- AIDS Vaccines
- Acquired Immunodeficiency Syndrome
- HIV Infections
- HIV Seropositivity
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- In Vitro
- Molecular Chaperones
- Stress
- molecular chaperone GRP78
Other ID:
UI: 102203092
From Meeting Abstracts