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

Author

Listed:
  • 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
    Institut de Cancérologie de l’Ouest (ICO), CRCi2NA-Inserm UMR 1307, CNRS UMR 6075, Nantes Université)

  • 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)

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.

Suggested Citation

  • Emilie Murigneux & Laurent Softic & Corentin Aubé & Carmen Grandi & Delphine Judith & Johanna Bruce & Morgane Le Gall & François Guillonneau & Alain Schmitt & Vincent Parissi & Clarisse Berlioz-Torren, 2024. "Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-44958-0
    DOI: 10.1038/s41467-024-44958-0
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    1. Siwen Long & Mykhailo Guzyk & Laura Perez Vidakovics & Xiao Han & Renhua Sun & Megan Wang & Marc D. Panas & Egon Urgard & Jonathan M. Coquet & Andres Merits & Adnane Achour & Gerald M. McInerney, 2024. "SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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