Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly

Emilie Murigneux, Laurent Softic, Corentin Aubé, Carmen Grandi, Delphine Judith, Johanna Bruce, Morgane Le Gall, François Guillonneau, Alain Schmitt, Vincent Parissi, Clarisse Berlioz-Torrent, Laurent Meertens, Maike M. K. Hansen and Sarah Gallois-Montbrun ()
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Emilie Murigneux: Université Paris Cité, CNRS, Inserm, Institut Cochin
Laurent Softic: Université Paris Cité, CNRS, Inserm, Institut Cochin
Corentin Aubé: Université Paris Cité, CNRS, Inserm, Institut Cochin
Carmen Grandi: Radboud University
Delphine Judith: Université Paris Cité, CNRS, Inserm, Institut Cochin
Johanna Bruce: Proteom’IC facility, Université Paris Cité, CNRS, Inserm, Institut Cochin
Morgane Le Gall: Proteom’IC facility, Université Paris Cité, CNRS, Inserm, Institut Cochin
François Guillonneau: Proteom’IC facility, Université Paris Cité, CNRS, Inserm, Institut Cochin
Alain Schmitt: Université Paris Cité, CNRS, Inserm, Institut Cochin
Vincent Parissi: Microbiologie Fondamentale et Pathogénicité Laboratory (MFP), UMR 5234, « Mobility of pathogenic genomes and chromatin dynamics » team (MobilVIR), CNRS-University of Bordeaux, DyNAVIR network
Clarisse Berlioz-Torrent: Université Paris Cité, CNRS, Inserm, Institut Cochin
Laurent Meertens: Université Paris Cité, Inserm U944, CNRS 7212, Institut de Recherche Saint-Louis, Hôpital Saint-Louis
Maike M. K. Hansen: Radboud University
Sarah Gallois-Montbrun: Université Paris Cité, CNRS, Inserm, Institut Cochin

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract Considerable progress has been made in understanding the molecular host-virus battlefield during SARS-CoV-2 infection. Nevertheless, the assembly and egress of newly formed virions are less understood. To identify host proteins involved in viral morphogenesis, we characterize the proteome of SARS-CoV-2 virions produced from A549-ACE2 and Calu-3 cells, isolated via ultracentrifugation on sucrose cushion or by ACE-2 affinity capture. Bioinformatic analysis unveils 92 SARS-CoV-2 virion-associated host factors, providing a valuable resource to better understand the molecular environment of virion production. We reveal that G3BP1 and G3BP2 (G3BP1/2), two major stress granule nucleators, are embedded within virions and unexpectedly favor virion production. Furthermore, we show that G3BP1/2 participate in the formation of cytoplasmic membrane vesicles, that are likely virion assembly sites, consistent with a proviral role of G3BP1/2 in SARS-CoV-2 dissemination. Altogether, these findings provide new insights into host factors required for SARS-CoV-2 assembly with potential implications for future therapeutic targeting.

Date: 2024
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DOI: 10.1038/s41467-024-44958-0

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