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Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication

G3BP1/2 are paralogous proteins that promote stress granule formation in response to cellular stresses, including viral infection. G3BP1/2 are prominent interactors of the nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, the functional consequences o...

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Detalles Bibliográficos
Autores principales: Yang, Zemin, Johnson, Bryan A., Meliopoulos, Victoria A., Ju, Xiaohui, Zhang, Peipei, Hughes, Michael P., Wu, Jinjun, Koreski, Kaitlin P., Chang, Ti-Cheng, Wu, Gang, Hixon, Jeff, Duffner, Jay, Wong, Kathy, Lemieux, Rene, Lokugamage, Kumari G., Alvardo, Rojelio E., Crocquet-Valdes, Patricia A., Walker, David H., Plante, Kenneth S., Plante, Jessica A., Weaver, Scott C., Kim, Hong Joo, Meyers, Rachel, Schultz-Cherry, Stacey, Ding, Qiang, Menachery, Vineet D., Taylor, J. Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10327126/
https://www.ncbi.nlm.nih.gov/pubmed/37425880
http://dx.doi.org/10.1101/2023.06.29.546885
Descripción
Sumario:G3BP1/2 are paralogous proteins that promote stress granule formation in response to cellular stresses, including viral infection. G3BP1/2 are prominent interactors of the nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, the functional consequences of the G3BP1-N interaction in the context of viral infection remain unclear. Here we used structural and biochemical analyses to define the residues required for G3BP1-N interaction, followed by structure-guided mutagenesis of G3BP1 and N to selectively and reciprocally disrupt their interaction. We found that mutation of F17 within the N protein led to selective loss of interaction with G3BP1 and consequent failure of the N protein to disrupt stress granule assembly. Introduction of SARS-CoV-2 bearing an F17A mutation resulted in a significant decrease in viral replication and pathogenesis in vivo, indicating that the G3BP1-N interaction promotes infection by suppressing the ability of G3BP1 to form stress granules.