Cargando…

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...

Descripción completa

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
_version_ 1785069561996902400
author 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
author_facet 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
author_sort Yang, Zemin
collection PubMed
description 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.
format Online
Article
Text
id pubmed-10327126
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Cold Spring Harbor Laboratory
record_format MEDLINE/PubMed
spelling pubmed-103271262023-07-08 Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication 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 bioRxiv Article 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. Cold Spring Harbor Laboratory 2023-06-30 /pmc/articles/PMC10327126/ /pubmed/37425880 http://dx.doi.org/10.1101/2023.06.29.546885 Text en https://creativecommons.org/licenses/by-nd/4.0/This work is licensed under a Creative Commons Attribution-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, and only so long as attribution is given to the creator. The license allows for commercial use.
spellingShingle Article
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
Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
title Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
title_full Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
title_fullStr Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
title_full_unstemmed Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
title_short Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replication
title_sort interaction between host g3bp and viral nucleocapsid protein regulates sars-cov-2 replication
topic Article
url 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
work_keys_str_mv AT yangzemin interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT johnsonbryana interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT meliopoulosvictoriaa interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT juxiaohui interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT zhangpeipei interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT hughesmichaelp interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT wujinjun interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT koreskikaitlinp interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT changticheng interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT wugang interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT hixonjeff interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT duffnerjay interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT wongkathy interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT lemieuxrene interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT lokugamagekumarig interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT alvardorojelioe interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT crocquetvaldespatriciaa interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT walkerdavidh interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT plantekenneths interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT plantejessicaa interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT weaverscottc interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT kimhongjoo interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT meyersrachel interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT schultzcherrystacey interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT dingqiang interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT menacheryvineetd interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication
AT taylorjpaul interactionbetweenhostg3bpandviralnucleocapsidproteinregulatessarscov2replication