Human immunodeficiency virus 1 envelope glycoprotein gp120 V3-glycan patch (V3-glycan patch)

The HIV-1 envelope glycoprotein gp120 V3-glycan patch is a highly conserved 'supersite of vulnerability' located on the outer domain of the HIV-1 envelope (Env) trimer (asm.org, nih.gov). It is defined by a dense cluster of high-mannose, under-processed N-linked glycans, centered around the asparagine at position 332 (N332), and the underlying GDIR peptide motif at the base of the V3 loop (nih.gov, elifesciences.org). This site is a primary target for potent broadly neutralizing antibodies (bNAbs) such as PGT121 and 10-1074, which are capable of neutralizing a vast array of HIV-1 strains by blocking viral attachment and entry into host CD4+ T cells (asm.org, nih.gov). Although the glycan shield generally functions to protect the virus from the host immune system, the V3-glycan patch represents a critical target for both passive antibody therapy and vaccine immunogen design (frontiersin.org, researchgate.net). Therapeutic challenges include the virus's ability to evade neutralization through glycan shifting or mutations that alter the N332 glycosylation site (asm.org, nih.gov).

Other names

N332 glycan supersiteV3/N332 glycan epitopeHigh-mannose patchV3-glycan supersite of vulnerabilityIntrinsic mannose patchIMP

Broadly neutralizing antibodies (bNAbs) bind to the V3-glycan patch on the HIV-1 envelope trimer, sterically hindering the interaction between gp120 and host cell receptors (CD4 and CCR5/CXCR4), thereby preventing viral entry and infection (asm.org, nih.gov).