title: 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.
authors: 1 Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine , New York, New York.
authors: Evgeny
authors: E
authors: Shmelkov
authors: Arsen
authors: A
authors: Grigoryan
authors: Chavdar
authors: C
authors: Krachmarov
authors: Ruben
authors: R
authors: Abagyan
authors: Timothy
authors: T
authors: Cardozo
mesh_terms: D000595:Amino Acid Sequence; D015483:HIV Antibodies / Q000276:immunology; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000378:metabolism*; D015497:HIV-1 / Q000276:immunology / Q000378:metabolism*; D008969:Molecular Sequence Data
chemical_list: D015483:HIV Antibodies; D015699:HIV Envelope Protein gp120