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Sequence-conserved and antibody-accessible sites in the V1V2 domain of HIV-1 gp120 envelope protein.


ABSTRACT: The immune-correlates analysis of the RV144 trial suggested that epitopes targeted by protective antibodies (Abs) reside in the V1V2 domain of gp120. We mapped V1V2 positional sequence variation onto the conserved V1V2 structural fold and showed that while most of the solvent-accessible V1V2 amino acids vary between strains, there are two accessible molecular surface regions that are conserved and also naturally antigenic. These sites may contain epitopes targeted by broadly cross-reactive anti-V1V2 antibodies.

SUBMITTER: Shmelkov E 

PROVIDER: S-EPMC4151074 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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Sequence-conserved and antibody-accessible sites in the V1V2 domain of HIV-1 gp120 envelope protein.

Shmelkov Evgeny E   Grigoryan Arsen A   Krachmarov Chavdar C   Abagyan Ruben R   Cardozo Timothy T  

AIDS research and human retroviruses 20140814 9


The immune-correlates analysis of the RV144 trial suggested that epitopes targeted by protective antibodies (Abs) reside in the V1V2 domain of gp120. We mapped V1V2 positional sequence variation onto the conserved V1V2 structural fold and showed that while most of the solvent-accessible V1V2 amino acids vary between strains, there are two accessible molecular surface regions that are conserved and also naturally antigenic. These sites may contain epitopes targeted by broadly cross-reactive anti-  ...[more]

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