Journal
MICROBIOLOGY SPECTRUM
Volume 9, Issue 1, Pages -Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/Spectrum.00169-21
Keywords
N terminus; Nsp1; SARS-CoV-2; crystal structure; protein translation; ribosome
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Funding
- National Natural Science Foundation of China [81971936, 82041004]
- Fundamental Research Funds for the Central Universities, Hubei Province's Outstanding Medical Academic Leader program
- Foundation for Innovative Research Groups of the National Natural Science Foundation of Hubei [2020CFA015]
- Foundation for Innovative Research Groups of Hubei Health Commission [WJ2021C002]
- Huazhong University of Science and Technology (HUST) COVID-19 Rapid Response Call [2020kfyXGYJ036]
- Wuhan Municipal Health Commission Emergency Fund [EX20E04]
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The N terminus of Nsp1 stabilizes the binding of the Nsp1 C terminus to ribosomes and acts as a nonspecific barrier to block the mRNA channel, thus abrogating host mRNA translation.
Nonstructural protein 1 (Nsp1) of severe acute respiratory syndrome coronaviruses (SARS-CoVs) is an important pathogenic factor that inhibits host protein translation by means of its C terminus. However, its N-terminal function remains elusive. Here, we determined the crystal structure of the N terminus (amino acids [aa] 11 to 125) of SARSCoV-2 Nsp1 at a 1.25-angstrom resolution. Further functional assays showed that the N terminus of SARS-CoVs Nsp1 alone loses the ability to colocalize with ribosomes and inhibit protein translation. The C terminus of Nsp1 can colocalize with ribosomes, but its protein translation inhibition ability is significantly weakened. Interestingly, fusing the C terminus of Nsp1 with enhanced green fluorescent protein (EGFP) or other proteins in place of its N terminus restored the protein translation inhibitory ability to a level equivalent to that of full-length Nsp1. Thus, our results suggest that the N terminus of Nsp1 is able to stabilize the binding of the Nsp1 C terminus to ribosomes and act as a nonspecific barrier to block the mRNA channel, thus abrogating host mRNA translation.
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