Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/154058
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dc.contributor.authorZhao, Kaitaoen_US
dc.contributor.authorKe, Zunhuien_US
dc.contributor.authorHu, Hongbingen_US
dc.contributor.authorLiu, Yahuien_US
dc.contributor.authorLi, Aixinen_US
dc.contributor.authorHua, Rongen_US
dc.contributor.authorGuo, Fangtengen_US
dc.contributor.authorXiao, Junfengen_US
dc.contributor.authorZhang, Yuen_US
dc.contributor.authorDuan, Lingen_US
dc.contributor.authorYan, Xin-Fuen_US
dc.contributor.authorGao, Yong-Guien_US
dc.contributor.authorLiu, Bingen_US
dc.contributor.authorXia, Yuchenen_US
dc.contributor.authorLi, Yanen_US
dc.date.accessioned2022-02-15T02:38:16Z-
dc.date.available2022-02-15T02:38:16Z-
dc.date.issued2021-
dc.identifier.citationZhao, 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.00169-21en_US
dc.identifier.issn2165-0497en_US
dc.identifier.urihttps://hdl.handle.net/10356/154058-
dc.description.abstractNonstructural 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.en_US
dc.language.isoenen_US
dc.relation.ispartofMicrobiology Spectrumen_US
dc.rights© 2021 Zhao et al. This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.en_US
dc.subjectScience::Biological sciencesen_US
dc.titleStructural basis and function of the N terminus of SARS-CoV-2 nonstructural protein 1en_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doi10.1128/Spectrum.00169-21-
dc.description.versionPublished versionen_US
dc.identifier.pmid34132580-
dc.identifier.scopus2-s2.0-85115904965-
dc.identifier.issue1en_US
dc.identifier.volume9en_US
dc.identifier.spagee00169-21en_US
dc.subject.keywordsN Terminusen_US
dc.subject.keywordsSARS-CoV-2en_US
dc.description.acknowledgementThis work was supported by the National Natural Science Foundation of China (project no. 81971936 and 82041004), the 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 (project no. 2020CFA015), Foundation for Innovative Research Groups of Hubei Health Commission (project no. WJ2021C002), Huazhong University of Science and Technology (HUST) COVID-19 Rapid Response Call (2020kfyXGYJ036), and Wuhan Municipal Health Commission Emergency Fund for COVID-19 (EX20E04).en_US
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