4th International AIDS Conference Stockholm, Sweden. — June 12-16, 1988

Int Conf AIDS. 1988 Jun 12-16;4:1,.106 (abstract no. PL1)

Robin A Weiss
Chester Beatty Labs, Inst of Cancer Research, London, UK

The envelope glycoproteins of HIV are important as targets for neutralizing antibodies and for the recognition of cell surface receptors. Serological studies of infected subjects and analysis of monoclonal antibodies to gp120 and gp4l indicate that both common and variable neutralization antigens exist in the HIV envelope. Some of these antigenic sites are becoming precisely defined and may be important in designing effective vaccines.

The receptor for all strains of HIV-1, HIV-2 and SIV studied is the CD4 cell surface antigen. CD4 acts as the HIV receptor on cells in culture of T-cell, B-cell, monocytic, epithelial and neural origin. HIV gp120 and CD4 bind to each other with high affinity and the HIV recognition site on CD4 is close to that for the monoclonal antibody leu3a. The conservation of receptor recognition between diverse strains of HIV and SIV, and on different cell types can be exploited to develop reagents that block HIV-receptor interactions and hence infection. Examples are the generation of anti-CD4 anti-idiotypic antibodies that weakly neutralize HIV, and recombinant soluble CD4 that strongly blocks HIV infection.

Our current understanding of the HIV envelope and receptor will be reviewed in relation to pathogenesis, treatment and protection.

880612
PL1

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