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Updated: May 18, 2026

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle (GUV) Membranes
Published on: July 28, 2016
Virus assembly and plasma membrane domains: which came first?
A Kerviel1, A Thomas, L Chaloin
1Centre d'études d'agents Pathogènes et Biotechnologies pour la Santé, CNRS - UMR 5236, 1919 route de Mende, Montpellier F-34 293, France.
Abstract:
Viral assembly is a key step in the virus life cycle. In this review, we focus mainly on the ability of retroviruses, especially HIV-1, to assemble at the plasma membrane of their host cells. The assembly process of RNA enveloped viruses necessitates a fine orchestration between the different viral components and specific interactions between viral proteins and lipids of the host cell membrane. Searching for a comparison with another RNA enveloped virus, we refer to influenza virus to show how it could share (or not) some common features with HIV-1 assembly since both viruses are believed to assemble mainly in raft microdomains. We also discuss the role of RNA and the cellular actin cytoskeleton in enhancing these viral assembly processes. Finally, based on the literature and on new results we have obtained by molecular docking, we propose another mechanism for HIV-1 assembly in membrane domains. This mechanism involves the trapping of acidic lipids by the viral Gag protein by means of ionic protein-lipid interactions, inducing thereby formation of acidic lipid-enriched microdomains (ALEM).
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