HIV-1 diverts cortical actin for particle assembly and release

Abstract 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 branchi...

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Main Authors: Rayane Dibsy, Erwan Bremaud, Johnson Mak, Cyril Favard, Delphine Muriaux
Format: Article
Language:English
Published: Nature Portfolio 2023-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-023-41940-0
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author Rayane Dibsy
Erwan Bremaud
Johnson Mak
Cyril Favard
Delphine Muriaux
author_facet Rayane Dibsy
Erwan Bremaud
Johnson Mak
Cyril Favard
Delphine Muriaux
author_sort Rayane Dibsy
collection DOAJ
description Abstract 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.
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spelling doaj.art-6d27d20071c245878660a257a1c62d462023-11-05T12:22:10ZengNature PortfolioNature Communications2041-17232023-10-0114111710.1038/s41467-023-41940-0HIV-1 diverts cortical actin for particle assembly and releaseRayane Dibsy0Erwan Bremaud1Johnson Mak2Cyril Favard3Delphine Muriaux4Institute of Research in Infectious disease of Montpellier (IRIM), University of MontpellierInstitute of Research in Infectious disease of Montpellier (IRIM), University of MontpellierInstitute for Glycomics, Griffith UniversityInstitute of Research in Infectious disease of Montpellier (IRIM), University of MontpellierInstitute of Research in Infectious disease of Montpellier (IRIM), University of MontpellierAbstract 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.https://doi.org/10.1038/s41467-023-41940-0
spellingShingle Rayane Dibsy
Erwan Bremaud
Johnson Mak
Cyril Favard
Delphine Muriaux
HIV-1 diverts cortical actin for particle assembly and release
Nature Communications
title HIV-1 diverts cortical actin for particle assembly and release
title_full HIV-1 diverts cortical actin for particle assembly and release
title_fullStr HIV-1 diverts cortical actin for particle assembly and release
title_full_unstemmed HIV-1 diverts cortical actin for particle assembly and release
title_short HIV-1 diverts cortical actin for particle assembly and release
title_sort hiv 1 diverts cortical actin for particle assembly and release
url https://doi.org/10.1038/s41467-023-41940-0
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