Proteomics

Dataset Information

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SARS-CoV-2 N protein interacts with cellular G3BP


ABSTRACT: Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) antagonizes stress granule formation, in part, via interaction between SARS-CoV-2 nucleocapsid (N) protein and Ras-GTPase-activating SH3-domain-binding protein 1 (G3BP1). In this study, we assessed interaction between the N protein of SARS-CoV-2 S clade and G3BP1 in Calu-3 cells

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Severe Acute Respiratory Syndrome

SUBMITTER: Dongbum Kim  

LAB HEAD: Hyung-Joo Kwon

PROVIDER: PXD035715 | Pride | 2022-10-15

REPOSITORIES: Pride

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Publications

Differential effect of SARS-CoV-2 infection on stress granule formation in Vero and Calu-3 cells.

Kim Dongbum D   Maharjan Sony S   Kang Mijeong M   Kim Jinsoo J   Park Sangkyu S   Kim Minyoung M   Baek Kyeongbin K   Kim Suyeon S   Suh Jun Gyo JG   Lee Younghee Y   Kwon Hyung-Joo HJ  

Frontiers in microbiology 20220823


Stress granule formation is induced by numerous environmental stressors, including sodium arsenite treatment and viral infection. Accordingly, stress granules can inhibit viral propagation and function as part of the antiviral host response to numerous viral infections. Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) antagonizes stress granule formation, in part, via interaction between SARS-CoV-2 nucleocapsid (N) protein and Ras-GTPase-activating SH3-domain-binding protein 1 (G3BP1  ...[more]

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