Impact of mutations in the V2 domain of HIV-1 envelop glycoprotein 120 on the recognition of neutralizing antibodies targeting the CD4-binding site
10.3760/cma.j.issn.0412-4030.2012.10.015
- VernacularTitle:HIV-1 V2区突变对CD4结合位点中和抗体识别的影响
- Author:
Musang LIU
;
Matsushita SHUZO
;
Shibata JUNJI
;
Weida LIU
- Publication Type:Journal Article
- Keywords:
HIV-1;
Mutation;
Neutralizing antibody
- From:
Chinese Journal of Dermatology
2012;45(10):731-734
- CountryChina
- Language:Chinese
-
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.MethodsHIV-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.
