Evidence map›Paper›PMID 34132580›Full record

ArticleMicrobiology spectrum2021

Structural Basis and Function of the N Terminus of SARS-CoV-2 Nonstructural Protein 1.

Kaitao Zhao, Zunhui Ke, Hongbing Hu, Yahui Liu, Aixin Li, Rong Hua, Fangteng Guo, Junfeng Xiao, Yu Zhang, Ling Duan and 5 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure-function mapping and mechanistic insights on the SARS CoV2 Nsp1.Protein science : a publication of the Protein Society · 2024
    Article
  4. SARS-CoV2 Nsp1 is a metal-dependent DNA and RNA endonuclease.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022
    Review
  13. Review
  14. Review
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 4 countries.

Kaitao Zhao *State Key Laboratory of Virology and Hubei Province Key Laboratory of Allergy and Immunology, Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan, China.ORCID 0000-0002-0261-1599
Zunhui Ke *Department of Blood Transfusion, Wuhan Children's Hospital, Tongji Medical College, Huazhong University of Science & Technology, Wuhan, China.
Hongbing Hu *Department of Blood Transfusion, Wuhan Children's Hospital, Tongji Medical College, Huazhong University of Science & Technology, Wuhan, China.
Yahui LiuDepartment of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Aixin LiState Key Laboratory of Virology and Hubei Province Key Laboratory of Allergy and Immunology, Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan, China.
Rong HuaState Key Laboratory of Virology and Hubei Province Key Laboratory of Allergy and Immunology, Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan, China.
Fangteng GuoState Key Laboratory of Virology and Hubei Province Key Laboratory of Allergy and Immunology, Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan, China.
Junfeng XiaoDepartment of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Yu ZhangFaculty of Science (Medical Science), The University of Sydney, Sydney, New South Wales, Australia.
Ling DuanDepartment of Blood Transfusion, Wuhan Children's Hospital, Tongji Medical College, Huazhong University of Science & Technology, Wuhan, China.
Xin-Fu YanSchool of Biological Sciences, Nanyang Technological University, Singapore.
Yong-Gui GaoSchool of Biological Sciences, Nanyang Technological University, Singapore.
Bing LiuBioBank, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.
Yuchen XiaState Key Laboratory of Virology and Hubei Province Key Laboratory of Allergy and Immunology, Institute of Medical Virology, School of Basic Medical Sciences, Wuhan University, Wuhan, China.ORCID 0000-0001-8460-3893
Yan LiDepartment of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Wuhan University · CNHuazhong University of Science and Technology · CNWuhan Children's Hospital · CNNanyang Technological University · SGFirst Affiliated Hospital of Xi'an Jiaotong University · CNThe University of Sydney · AU

Funding

National Natural Science Foundation of China (NSFC) 81971936
6 · The paper itself

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.

Indexed as

COVID-19Crystallography, X-RayHEK293 CellsHumansProtein BiosynthesisProtein ConformationProtein DomainsRNA, MessengerSARS-CoV-2Sequence Analysis, ProteinViral Nonstructural ProteinsORF1ab polyprotein, SARS-CoV-2RNA, MessengerViral Nonstructural Proteinscrystal structureNsp1N terminusprotein translationribosomeSARS-CoV-2

Identifiers

PMID34132580
PMCPMC8552758
OpenAlexW3168017236

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.