Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site.

ABSTRACT: The human immunodeficiency virus type 1 (HIV-1) exterior envelope glycoprotein, gp120, possesses conserved binding sites for interaction with the primary virus receptor, CD4, and also for the co-receptor, generally CCR5. Although gp120 is a major target for virus-specific neutralizing antibodies, the gp120 variable elements and its malleable nature contribute to evasion of effective host-neutralizing antibodies. To understand the conformational character and immunogenicity of the gp120 receptor binding sites as potential vaccine targets, we introduced structure-based modifications to stabilize gp120 core proteins (deleted of the gp120 major variable regions) into the conformation recognized by both receptors. Thermodynamic analysis of the re-engineered core with selected ligands revealed s

SUBMITTER: Dey B 

PROVIDER: S-EPMC2680979 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature