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  • Kumar, Pravin, et al. (author)
  • Clinically observed deletions in SARS-CoV-2 Nsp1 affect its stability and ability to inhibit translation
  • 2022
  • In: FEBS Letters. - : John Wiley & Sons. - 0014-5793 .- 1873-3468. ; 596:9, s. 1203-1213
  • Journal article (peer-reviewed)abstract
    • Nonstructural protein 1 (Nsp1) of SARS-CoV-2 inhibits host cell translation through an interaction between its C-terminal domain and the 40S ribosome. The N-terminal domain (NTD) of Nsp1 is a target of recurring deletions, some of which are associated with altered COVID-19 disease progression. Here, we characterize the efficiency of translational inhibition by clinically observed Nsp1 deletion variants. We show that a frequent deletion of residues 79–89 severely reduces the ability of Nsp1 to inhibit translation while not abrogating Nsp1 binding to the 40S. Notably, while the SARS-CoV-2 5′ untranslated region enhances translation of mRNA, it does not protect from Nsp1-mediated inhibition. Finally, thermal stability measurements and structure predictions reveal a correlation between stability of the NTD and the efficiency of translation inhibition.
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journal article (1)
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peer-reviewed (1)
Author/Editor
Terenin, Ilya (1)
Hauryliuk, Vasili, 1 ... (1)
Kurata, Tatsuaki (1)
Schexnaydre, Erin (1)
Carlson, Lars-Anders (1)
Kumar, Pravin (1)
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Umeå University (1)
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Natural sciences (1)
Medical and Health Sciences (1)
Year
2022 (1)

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