Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly - Université Paris Cité
Journal Articles Nature Communications Year : 2024

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

Emilie Murigneux
  • Function : Author
Laurent Softic
  • Function : Author
Corentin Aubé
  • Function : Author
Carmen Grandi
Delphine Judith
  • Function : Author
Johanna Bruce
Morgane Le Gall
Alain Schmitt
Maike Hansen

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.
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hal-04591662 , version 1 (29-05-2024)

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Emilie Murigneux, Laurent Softic, Corentin Aubé, Carmen Grandi, Delphine Judith, et al.. Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly. Nature Communications, 2024, 15 (1), pp.640. ⟨10.1038/s41467-024-44958-0⟩. ⟨hal-04591662⟩
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