Impact of mutations in the V2 domain of HIV-1 envelop glycoprotein 120 on the recognition of neutralizing antibodies targeting the CD4-binding site / 中华皮肤科杂志
Chinese Journal of Dermatology
;
(12): 731-734, 2012.
Article
Dans Chinois
| WPRIM
| ID: wpr-420904
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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
langue:
Chinois
Texte intégral:
Chinese Journal of Dermatology
Année:
2012
Type:
Article
Documents relatifs à ce sujet
MEDLINE
...
LILACS
LIS