| Title: |
Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry |
| Authors: |
Spillings, BL; Day, CJ; Garcia-Minambres, A; Aggarwal, A; Condon, ND; Haselhorst, T; Purcell, DFJ; Turville, SG; Stow, JL; Jennings, MP; Mak, J |
| Publisher Information: |
CELL PRESS |
| Publication Year: |
2022 |
| Collection: |
The University of Melbourne: Digital Repository |
| Description: |
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. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| ISSN: |
2211-1247 |
| Relation: |
https://hdl.handle.net/11343/302532 |
| Availability: |
https://hdl.handle.net/11343/302532 |
| Rights: |
https://creativecommons.org/licenses/by-nc-nd/4.0 ; CC BY-NC-ND |
| Accession Number: |
edsbas.CCDDEC63 |
| Database: |
BASE |