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  • Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry.

Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry.

Cell reports (2022-02-03)
Belinda L Spillings, Christopher J Day, Albert Garcia-Minambres, Anupriya Aggarwal, Nicholas D Condon, Thomas Haselhorst, Damian F J Purcell, Stuart G Turville, Jennifer L Stow, Michael P Jennings, Johnson Mak
ABSTRACT

Here, we present ultrastructural analyses showing that incoming HIV are captured near the lymphocyte surface in a virion-glycan-dependent manner. Biophysical analyses show that removal of either virion- or cell-associated N-glycans impairs virus-cell binding, and a similar glycan-dependent relationship is observed between purified HIV envelope (Env) and primary T cells. Trimming of N-glycans from either HIV or Env does not inhibit protein-protein interactions. Glycan arrays reveal HIV preferentially binds to N-acetylglucosamine and mannose. Interfering with these glycan-based interactions reduces HIV infectivity. These glycan interactions are distinct from previously reported glycan-lectin and non-specific electrostatic charge-based interactions. Specific glycan-glycan-mediated attachment occurs prior to virus entry and enhances efficiency of infection. Binding and fluorescent imaging data support glycan-glycan interactions as being responsible, at least in part, for initiating contact between HIV and the host cell, prior to viral Env-cellular CD4 engagement.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
GlycoProfile 2-AB Labeling Kit
Sigma-Aldrich
Anti-Rat IgG (whole molecule)–Biotin antibody produced in goat, affinity isolated antibody, buffered aqueous solution