Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P-2/Cholesterol nanoclusters

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Yandrapalli, Naresh
Lubart, Quentin
Tanwar, Hanumant S
Picart, Catherine
Mak, Johnson
Muriaux, Delphine
Favard, Cyril
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2016
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Abstract

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.

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Scientific Reports

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6

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1

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© The Author(s) 2016. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Biochemistry and cell biology

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Multidisciplinary Sciences

Science & Technology - Other Topics

HUMAN-IMMUNODEFICIENCY-VIRUS

PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE CLUSTERS

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Yandrapalli, N; Lubart, Q; Tanwar, HS; Picart, C; Mak, J; Muriaux, D; Favard, C, Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P-2/Cholesterol nanoclusters, Scientific Reports, 2016, 6 (1)

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