Functional implications of the binding mode of a human conformation-dependent V2 monoclonal antibody against HIV.

ABSTRACT:

Unlabelled

Data from the RV144 HIV vaccine trial indicated that gp120 V2 antibodies were associated with a lower risk of infection; thus, the mapping of V2 epitopes can contribute to the design of an effective HIV vaccine. We solved the crystal structure of human monoclonal antibody (MAb) 2158, which targets a conformational V2 epitope overlapping the α4β7 integrin binding site, and constructed a full-length model of V1V2. Comparison of computational energy stability to experimental enzyme-linked immunosorbent assay (ELISA) results identified a hydrophobic core that stabilizes the V2 region for optimal 2158 binding, as well as residues that directly mediate side chain interactions with MAb 2158. These data define the binding surface recognized by MAb 2158 and offer a structural exp

SUBMITTER: Spurrier B 

PROVIDER: S-EPMC3993739 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature