tetano
Editor, Senior Moderator
Nat Commun
. 2024 Jan 20;15(1):640.
doi: 10.1038/s41467-024-44958-0. Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly
Emilie Murigneux[SUP] #[/SUP][SUP] 1 [/SUP], Laurent Softic[SUP] #[/SUP][SUP] 1 [/SUP], Corentin Aubé[SUP] #[/SUP][SUP] 1 [/SUP], Carmen Grandi[SUP] 2 [/SUP], Delphine Judith[SUP] 1 [/SUP], Johanna Bruce[SUP] 3 [/SUP], Morgane Le Gall[SUP] 3 [/SUP], François Guillonneau[SUP] 3 4 [/SUP], Alain Schmitt[SUP] 1 [/SUP], Vincent Parissi[SUP] 5 [/SUP], Clarisse Berlioz-Torrent[SUP] 1 [/SUP], Laurent Meertens[SUP] 6 [/SUP], Maike M K Hansen[SUP] 2 [/SUP], Sarah Gallois-Montbrun[SUP] 7 [/SUP]
Affiliations
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.
. 2024 Jan 20;15(1):640.
doi: 10.1038/s41467-024-44958-0. Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly
Emilie Murigneux[SUP] #[/SUP][SUP] 1 [/SUP], Laurent Softic[SUP] #[/SUP][SUP] 1 [/SUP], Corentin Aubé[SUP] #[/SUP][SUP] 1 [/SUP], Carmen Grandi[SUP] 2 [/SUP], Delphine Judith[SUP] 1 [/SUP], Johanna Bruce[SUP] 3 [/SUP], Morgane Le Gall[SUP] 3 [/SUP], François Guillonneau[SUP] 3 4 [/SUP], Alain Schmitt[SUP] 1 [/SUP], Vincent Parissi[SUP] 5 [/SUP], Clarisse Berlioz-Torrent[SUP] 1 [/SUP], Laurent Meertens[SUP] 6 [/SUP], Maike M K Hansen[SUP] 2 [/SUP], Sarah Gallois-Montbrun[SUP] 7 [/SUP]
Affiliations
- PMID: 38245532
- PMCID: PMC10799903
- DOI: 10.1038/s41467-024-44958-0
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.