دورية أكاديمية

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

التفاصيل البيبلوغرافية
العنوان: Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly
المؤلفون: Murigneux, Emilie, Softic, Laurent, Aubé, Corentin, Grandi, Carmen, Judith, Delphine, Bruce, Johanna, Le Gall, Morgane, Guillonneau, François, Schmitt, Alain, Parissi, Vincent, Berlioz-Torrent, Clarisse, Meertens, Laurent, Hansen, Maike, Gallois-Montbrun, Sarah
المساهمون: Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Radboud University Nijmegen, Centre de Recherche en Cancérologie et Immunologie Intégrée Nantes-Angers (CRCI2NA ), Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Nantes Université - UFR de Médecine et des Techniques Médicales (Nantes Univ - UFR MEDECINE), Nantes Université - pôle Santé, Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ)-Nantes Université - pôle Santé, Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ), Microbiologie Fondamentale et Pathogénicité (MFP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Viral DNA Integration and Chromatin Dynamics Network (DyNAVir), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS)-Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Génomes, biologie cellulaire et thérapeutiques (GenCellDis (U944 / UMR7212)), Collège de France (CdF (institution))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Institut de Recherche Saint-Louis - Hématologie Immunologie Oncologie (Département de recherche de l’UFR de médecine, ex- Institut Universitaire Hématologie-IUH) (IRSL), Université Paris Cité (UPCité), Hopital Saint-Louis AP-HP (AP-HP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), This work was supported by the Agence Nationale de la Recherche (ANR RA-Covid-19, ANR-20-COV1-000) to S.G.M. and L.M., the Agence Nationale de la Recherche sur le SIDA et les hépatites virales-Maladies Infectieuses Emergentes (ANRS-MIE) to S.G.M., the Christine Mohrmann Fellowship and the Netherlands Organization for Scientific Research (NWO) ENW-XS award (OCENW.XS21.2.050) to M.M.K.H. and by the DIM Thérapie Génique Paris Ile-de-France Région, IBiSA, and the Labex GR-Ex to Proteom’IC core facility. M.M.K.H. also acknowledges support from the French Ministry of Foreign Affairs, the French Embassy in the Netherlands and the French Ministry of Higher Education and Research through the Descartes Huygens Prize. We thank Virginie Salnot and Thomas Guilbert for their technical support and Monsef Benkirane, Ali Amara, Stéphane Emiliani, Mélissa Ait Said, Katy Janvier, Gordon Langsley, Phillipe Roingeard, Emilie-Fleur Gautier and Ismael Boussaid for helpful discussions., ANR-20-COV1-0001,APCOD,Les cellules présentatrices d'antigènes dans la maladie de COVID-19 à résolution monocellulaire(2020)
المصدر: ISSN: 2041-1723.
بيانات النشر: HAL CCSD
Nature Publishing Group
سنة النشر: 2024
مصطلحات موضوعية: [SDV]Life Sciences [q-bio]
الوصف: International audience ; 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.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/38245532; hal-04591662; https://u-paris.hal.science/hal-04591662Test; https://u-paris.hal.science/hal-04591662/documentTest; https://u-paris.hal.science/hal-04591662/file/s41467-024-44958-0.pdfTest; PUBMED: 38245532; PUBMEDCENTRAL: PMC10799903
DOI: 10.1038/s41467-024-44958-0
الإتاحة: https://doi.org/10.1038/s41467-024-44958-0Test
https://u-paris.hal.science/hal-04591662Test
https://u-paris.hal.science/hal-04591662/documentTest
https://u-paris.hal.science/hal-04591662/file/s41467-024-44958-0.pdfTest
حقوق: http://creativecommons.org/licenses/byTest/ ; info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.CC15482F
قاعدة البيانات: BASE