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10.1016/j.isci.2021.103562

http://scihub22266oqcxt.onion/10.1016/j.isci.2021.103562
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34901782!8642831!34901782
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suck abstract from ncbi

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  • SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress granules to impair host stress response #MMPMID34901782
  • Nabeel-Shah S; Lee H; Ahmed N; Burke GL; Farhangmehr S; Ashraf K; Pu S; Braunschweig U; Zhong G; Wei H; Tang H; Yang J; Marcon E; Blencowe BJ; Zhang Z; Greenblatt JF
  • iScience 2022[Jan]; 25 (1): 103562 PMID34901782show ga
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein is essential for viral replication, making it a promising target for antiviral drug and vaccine development. SARS-CoV-2 infected patients exhibit an uncoordinated immune response; however, the underlying mechanistic details of this imbalance remain obscure. Here, starting from a functional proteomics workflow, we cataloged the protein-protein interactions of SARS-CoV-2 proteins, including an evolutionarily conserved specific interaction of N with the stress granule resident proteins G3BP1 and G3BP2. N localizes to stress granules and sequesters G3BPs away from their typical interaction partners, thus attenuating stress granule formation. We found that N binds directly to host mRNAs in cells, with a preference for 3' UTRs, and modulates target mRNA stability. We show that the N protein rewires the G3BP1 mRNA-binding profile and suppresses the physiological stress response of host cells, which may explain the imbalanced immune response observed in SARS-CoV-2 infected patients.
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  • suck abstract from ncbi

    103562 1.25 2022