HIV-1 diverts cortical actin for particle assembly and release.

Autor: Dibsy R; Institute of Research in Infectious disease of Montpellier (IRIM), University of Montpellier, UMR9004 CNRS, Montpellier, France., Bremaud E; Institute of Research in Infectious disease of Montpellier (IRIM), University of Montpellier, UMR9004 CNRS, Montpellier, France., Mak J; Institute for Glycomics, Griffith University, Brisbane, Australia., Favard C; Institute of Research in Infectious disease of Montpellier (IRIM), University of Montpellier, UMR9004 CNRS, Montpellier, France., Muriaux D; Institute of Research in Infectious disease of Montpellier (IRIM), University of Montpellier, UMR9004 CNRS, Montpellier, France. delphine.muriaux@irim.cnrs.fr.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2023 Oct 31; Vol. 14 (1), pp. 6945. Date of Electronic Publication: 2023 Oct 31.
DOI: 10.1038/s41467-023-41940-0
Abstrakt: Enveloped viruses assemble and bud from the host cell membranes. Any role of cortical actin in these processes have often been a source of debate. Here, we assessed if cortical actin was involved in HIV-1 assembly in infected CD4 T lymphocytes. Our results show that preventing actin branching not only increases HIV-1 particle release but also the number of individual HIV-1 Gag assembly clusters at the T cell plasma membrane. Indeed, in infected T lymphocytes and in in vitro quantitative model systems, we show that HIV-1 Gag protein prefers areas deficient in F-actin for assembling. Finally, we found that the host factor Arpin, an inhibitor of Arp2/3 branched actin, is recruited at the membrane of infected T cells and it can associate with the viral Gag protein. Altogether, our data show that, for virus assembly and particle release, HIV-1 prefers low density of cortical actin and may favor local actin debranching by subverting Arpin.
(© 2023. The Author(s).)
Databáze: MEDLINE
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