Factors limiting the immunogenicity of HIV-1 gp120 envelope glycoproteins

Structure of trimeric HIV-1 envelope glycoproteins.

Release of gp120 Restraints Leads to an Entry-Competent Intermediate State of the HIV-1 Envelope Glycoproteins

Primary human immunodeficiency virus (HIV-1) envelope glycoprotein (Env) trimers [(gp120/gp41)3] typically exist in a metastable closed conformation (state 1). Binding the CD4 receptor triggers Env to undergo extensive conformational changes to mediate virus entry. We identified specific gp120 residues that restrain Env in state 1. Alteration of these restraining residues destabilized state 1, ...

Finding trimeric HIV-1 envelope glycoproteins in random noise.

In two recent papers, Mao et al. (1, 2) present the trimeric structure of the HIV-1 gp160 trimer at 11and 6-Å resolutions, respectively. The authors repeatedly emphasize their “reference-free,” “gold standard” methodology, but in neither of their papers do they state how the particles were selected from the electron micrographs. They do state (figure S3 in ref. 1): “Each row shows a sequence of...

Peptide mimic of the HIV envelope gp120-gp41 interface.

The human immunodeficiency virus envelope glycoprotein (Env) is composed of surface (gp120) and transmembrane (gp41) subunits, which are noncovalently associated on the viral surface. Human immunodeficiency virus Env mediates viral entry after undergoing a complex series of conformational changes induced by interaction with cellular CD4 and a chemokine coreceptor. These changes propagate from g...

Structure of the Core of the HIV-1 gp120 Exterior Envelope Glycoprotein

The x-ray crystal structure of the gp120 core derived from the HXBc2 strain of HIV-1, in a ternary complex with two-domain CD4 and a neutralizing antibody, has been solved [1]. The gp120 core contains deletions of the V1, V2 and V3 variable loops and of the Nand C-termini, compared with full-length gp120. The implications of this structure for understanding the interaction of the HIV-1 envelope...