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10.1038/s41421-021-00275-0

http://scihub22266oqcxt.onion/10.1038/s41421-021-00275-0
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34035218!8147577!34035218
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suck abstract from ncbi


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pmid34035218      Cell+Discov 2021 ; 7 (1): 38
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  • SARS-CoV-2 nucleocapsid protein impairs stress granule formation to promote viral replication #MMPMID34035218
  • Zheng ZQ; Wang SY; Xu ZS; Fu YZ; Wang YY
  • Cell Discov 2021[May]; 7 (1): 38 PMID34035218show ga
  • The newly emerging coronavirus SARS-CoV-2 causes severe lung disease and substantial mortality. How the virus evades host defense for efficient replication is not fully understood. In this report, we found that the SARS-CoV-2 nucleocapsid protein (NP) impaired stress granule (SG) formation induced by viral RNA. SARS-CoV-2 NP associated with the protein kinase PKR after dsRNA stimulation. SARS-CoV-2 NP did not affect dsRNA-induced PKR oligomerization, but impaired dsRNA-induced PKR phosphorylation (a hallmark of its activation) as well as SG formation. SARS-CoV-2 NP also targeted the SG-nucleating protein G3BP1 and impaired G3BP1-mediated SG formation. Deficiency of PKR or G3BP1 impaired dsRNA-triggered SG formation and increased SARS-CoV-2 replication. The NP of SARS-CoV also targeted both PKR and G3BP1 to impair dsRNA-induced SG formation, whereas the NP of MERS-CoV targeted PKR, but not G3BP1 for the impairment. Our findings suggest that SARS-CoV-2 NP promotes viral replication by impairing formation of antiviral SGs, and reveal a conserved mechanism on evasion of host antiviral responses by highly pathogenic human betacoronaviruses.
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