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|Title:||Structural basis and function of the N terminus of SARS-CoV-2 nonstructural protein 1||Authors:||Zhao, Kaitao
|Keywords:||Science::Biological sciences||Issue Date:||2021||Source:||Zhao, K., Ke, Z., Hu, H., Liu, Y., Li, A., Hua, R., Guo, F., Xiao, J., Zhang, Y., Duan, L., Yan, X., Gao, Y., Liu, B., Xia, Y. & Li, Y. (2021). Structural basis and function of the N terminus of SARS-CoV-2 nonstructural protein 1. Microbiology Spectrum, 9(1), e00169-21-. https://dx.doi.org/10.1128/Spectrum.00169-21||Journal:||Microbiology Spectrum||Abstract:||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 SARS-CoV-2 Nsp1 at a 1.25-Å 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.||URI:||https://hdl.handle.net/10356/154058||ISSN:||2165-0497||DOI:||10.1128/Spectrum.00169-21||Rights:||© 2021 Zhao et al. This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
Updated on Jul 5, 2022
Updated on Jul 5, 2022
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