Abstract:

Objective To investigate the impact of mutations in the V2 domain of HIV-1 envelop glycoprotein （gp） 120 gene on the recognition of neutralizing antibodies （NAbs） specific to the other domains of gp120. Methods HIV-1 pseudoviruses （JR-FL） containing wild type or V2-mutant gp120 monomers were constructed, and the neutralization of CD4-binding site-specific and CD4-induced NAbs to the HIV-1 pseudoviruses was observed. Enzyme linked immunosorbent assay （ELISA） was performed to evaluate the binding affinity of CD4-binding site-specific and CD4-induced NAbs to wild type or V2-mutant gp120. Results Neither CD4-binding site-specific nor CD4-induced NAbs could neutralize the wild type JR-FL pseudoviruses, but both of them could neutralize pseudoviruses containg the gp120 V2 mutant at a low concentration. There was no significant difference in the binding affinity to CD4-binding site-specific NAbs between the wild type and mutant gp120, while the ELISA binding curves of wild type and mutant gp120 against CD4-induced NAbs were separate, and the affinity of CD4-induced NAbs to the mutant gp120 （L175P） was notably higher than that to the wild type gp120. Conclusion The mutations in the V2 domain of HIV-1 gp120 may affect the antiviral activity of NAbs.

Key words: Neutralizing Antibody