HIV-1 diverts cortical actin for particle assembly and release

Rayane Dibsy, Erwan Bremaud, Johnson Mak, Cyril Favard and Delphine Muriaux ()
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Rayane Dibsy: University of Montpellier
Erwan Bremaud: University of Montpellier
Johnson Mak: Griffith University
Cyril Favard: University of Montpellier
Delphine Muriaux: University of Montpellier

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-41940-0

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