Identification of a broad and potent V3 glycan site bNAb targeting an N332_gp120 glycan-independent epitope.

ABSTRACT: Broadly neutralizing antibodies (bNAbs) against HIV-1 can suppress viremia in vivo and inform vaccine development. Here, we characterized 007, a V3 glycan site bNAb exhibiting high levels of antiviral activity against multiclade pseudovirus panels^1-3 (GeoMean IC₅₀ = 0.012 μg/mL, breadth = 69%, 217 virus strains) by targeting a N332_gp120 glycan-independent V3 epitope, a site of Env vulnerability to which only weakly neutralizing antibodies had previously been identified. Functional analyses demonstrated distinct binding and neutralization profiles compared to classical V3 glycan site bNAbs. A 007 Fab-Env cryo-EM structure revealed contacts with the V3 ³²⁴GD/NIR³²⁷ motif and interactions with N156_gp120 and N301_gp12

SUBMITTER: Gieselmann L 

PROVIDER: S-EPMC12439949 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature