Rapid conformational epitope mapping of anti-gp120 antibodies with a designed mutant panel displayed on yeast.

ABSTRACT: gp120 is a substrate for protein engineering both for human immunodeficiency virus (HIV) immunogen design and as a bait for isolating anti-HIV antibodies from patient samples. In this work, we describe the display of a stripped core gp120 on the yeast cell surface. Validation against a panel of neutralizing antibodies confirms that yeast-displayed gp120 presents the CD4 binding site in the correct conformation. We map the epitope of the broadly neutralizing anti-gp120 antibody VRC01 using both a random mutagenesis library and a defined mutant panel and find that the resultant epitope maps are consistent with one another and with the crystallographically identified contact residues. Mapping the VRC01-competitive antibodies b12 and b13 reveals energetic differences in their epitopes that are

SUBMITTER: Mata-Fink J 

PROVIDER: S-EPMC3785227 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature