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Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P₂/Cholesterol nanoclusters

Version 2 2024-06-12, 15:01
Version 1 2017-01-04, 12:56
journal contribution
posted on 2024-06-12, 15:01 authored by N Yandrapalli, Q Lubart, HS Tanwar, C Picart, J Mak, D Muriaux, C Favard
The self-assembly of HIV-1 Gag polyprotein at the inner leaflet of the cell host plasma membrane is the key orchestrator of virus assembly. The binding between Gag and the plasma membrane is mediated by specific interaction of the Gag matrix domain and the PI(4,5)P2 lipid (PIP2). It is unknown whether this interaction could lead to local reorganization of the plasma membrane lipids. In this study, using model membranes, we examined the ability of Gag to segregate specific lipids upon self-assembly. We show for the first time that Gag self-assembly is responsible for the formation of PIP2 lipid nanoclusters, enriched in cholesterol but not in sphingomyelin. We also show that Gag mainly partition into liquid-disordered domains of these lipid membranes. Our work strongly suggests that, instead of targeting pre-existing plasma membrane lipid domains, Gag is more prone to generate PIP2/Cholesterol lipid nanodomains at the inner leaflet of the plasma membrane during early events of virus assembly.

History

Journal

Scientific reports

Volume

6

Article number

39332

Pagination

1-13

Location

London, Eng.

eISSN

2045-2322

Language

eng

Publication classification

C Journal article, C1 Refereed article in a scholarly journal

Copyright notice

2016, The Authors

Publisher

Nature Publishing Group