Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/154058
Title: Structural basis and function of the N terminus of SARS-CoV-2 nonstructural protein 1
Authors: Zhao, Kaitao
Ke, Zunhui
Hu, Hongbing
Liu, Yahui
Li, Aixin
Hua, Rong
Guo, Fangteng
Xiao, Junfeng
Zhang, Yu
Duan, Ling
Yan, Xin-Fu
Gao, Yong-Gui
Liu, Bing
Xia, Yuchen
Li, Yan
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

Files in This Item:
File Description SizeFormat 
Spectrum.00169-21.pdf3.03 MBAdobe PDFView/Open

Page view(s)

43
Updated on Jul 5, 2022

Download(s)

13
Updated on Jul 5, 2022

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.