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

The HIV-1 gp120 high-mannose N-glycan patch near the V3 base is a critical antigenic region on the surface of the HIV-1 envelope glycoprotein (Env) (Kong et al., 2013, PubMed: 24030493). This site is frequently termed the "V3-glycan supersite" because it serves as a primary target for several potent broadly neutralizing antibodies (bNAbs) such as PGT121 and 10-1074 (Walker et al., 2011, PubMed: 21903924). The patch is defined by a dense cluster of host-derived N-linked glycans, particularly at positions N332, N301, and N334, which surround the base of the third variable (V3) loop (Sok et al., 2014, PubMed: 24743101). Biologically, these glycans contribute to the "glycan shield," a mechanism the virus uses to evade the host immune system by masking conserved protein surfaces (Wei et al., 2003, PubMed: 12646913). During the infection process, the V3 loop is essential for binding to host co-receptors like CCR5 or CXCR4, facilitating viral entry into CD4+ T cells. Therapeutic interventions targeting this patch involve the use of bNAbs to neutralize the virus and prevent infection or reduce viral load in infected individuals (Sanders & Moore, 2017, PubMed: 28813411). This target is currently a cornerstone of HIV-1 vaccine research, specifically in the development of immunogens designed to prime the immune system to produce V3-glycan-specific antibodies.

Other names

V3-glycan supersiteN332-glycan supersitegp120 high-mannose patchV3-base glycan cluster

Neutralization of viral particles by binding to the glycan-protein interface, preventing co-receptor engagement and viral-cell membrane fusion.