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HIV-1 clade C escapes broadly neutralizing autologous antibodies with N332 glycan specificity by distinct mechanisms.

Abstract：

:The glycan supersite centered on N332 in the V3 base of the HIV-1 envelope (Env) is a target for broadly neutralizing antibodies (bnAbs) such as PGT121 and PGT128. In this study, we examined the basis of resistance of HIV-1 clade C Envs obtained from broadly cross neutralizing (BCN) plasma of an Indian donor with N332 specificity. Pseudotyped viruses expressing autologous envs were found to be resistant to autologous BCN plasma as well as to PGT121 and PGT128 mAbs despite the majority of Envs containing an intact N332 residue. While resistance of one of the Envs to neutralization by autologous plasma antibodies with shorter V1 loop length was found to be correlated with a N332S mutation, resistance to neutralization of rest of the Envs was found to be associated with longer V1 loop length and acquisition of protective N-glycans. In summary, we show evidence of escape of circulating HIV-1 clade C in an individual from autologous BCN antibodies by three distinct mechanisms.

journal_name

Retrovirology

journal_title

Retrovirology

authors

Deshpande S,Patil S,Kumar R,Hermanus T,Murugavel KG,Srikrishnan AK,Solomon S,Morris L,Bhattacharya J

doi

10.1186/s12977-016-0297-2

subject

Has Abstract

pub_date

2016-08-30 00:00:00

pages

60

issue

1

issn

1742-4690

pii

10.1186/s12977-016-0297-2

journal_volume

13

pub_type

杂志文章

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