Related Experiment Video
Updated: Apr 26, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
Sequence-conserved and antibody-accessible sites in the V1V2 domain of HIV-1 gp120 envelope protein
Evgeny Shmelkov1, Arsen Grigoryan, Chavdar Krachmarov
11 Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine , New York, New York.
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.
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