Academic Journal
Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry
| Τίτλος: | Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry |
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| Συγγραφείς: | Spillings, BL, Day, CJ, Garcia-Minambres, A, Aggarwal, A, Condon, ND, Haselhorst, T, Purcell, DFJ, Turville, SG, Stow, JL, Jennings, MP, Mak, J |
| Στοιχεία εκδότη: | CELL PRESS |
| Έτος έκδοσης: | 2022 |
| Συλλογή: | The University of Melbourne: Digital Repository |
| Περιγραφή: | 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. |
| Τύπος εγγράφου: | article in journal/newspaper |
| Γλώσσα: | English |
| ISSN: | 2211-1247 |
| Relation: | https://hdl.handle.net/11343/302532 |
| Διαθεσιμότητα: | https://hdl.handle.net/11343/302532 |
| Rights: | https://creativecommons.org/licenses/by-nc-nd/4.0 ; CC BY-NC-ND |
| Αριθμός Καταχώρησης: | edsbas.CCDDEC63 |
| Βάση Δεδομένων: | BASE |
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