Evidence map›Paper›PMID 35671758›Full record

ArticleCell reports2022

Parsing the role of NSP1 in SARS-CoV-2 infection.

Tal Fisher, Avi Gluck, Krishna Narayanan, Makoto Kuroda, Aharon Nachshon, Jason C Hsu, Peter J Halfmann, Yfat Yahalom-Ronen, Hadas Tamir, Yaara Finkel and 8 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed, 1 pooled it
6.3field-weighted citation impact, top 2% 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

59 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Extra gene coding capacity of SARS-CoV-2 provides a virus engineering platform for in vitro and in vivo applications.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
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  9. SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Article
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  14. Human coronavirus 3CL protease manipulates host protein STIM1 to facilitate immune evasion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 4 institutions in 3 countries.

Tal FisherDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Avi GluckDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Krishna NarayananDepartment of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, TX 77555-1019, USA.
Makoto KurodaDepartment of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, WI 53711, USA.
Aharon NachshonDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Jason C HsuDepartment of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, TX 77555-1019, USA.
Peter J HalfmannDepartment of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, WI 53711, USA.
Yfat Yahalom-RonenDepartment of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona 74100, Israel.
Hadas TamirDepartment of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona 74100, Israel.
Yaara FinkelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Michal SchwartzDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.
Shay WeissDepartment of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona 74100, Israel.
Chien-Te K TsengDepartment of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, TX 77555-1019, USA; Institute for Human Infections and Immunity, The University of Texas Medical Branch, Galveston, TX 77555-1019, USA.
Tomer IsraelyDepartment of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona 74100, Israel.
Nir ParanDepartment of Infectious Diseases, Israel Institute for Biological Research, Ness Ziona 74100, Israel. Electronic address: nirp@iibr.gov.il.
Yoshihiro KawaokaDepartment of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, WI 53711, USA; Department of Virology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan; The Research Center for Global Viral Diseases, National Center for Global Health and Medicine Research Institute, Tokyo 162-8655, Japan. Electronic address: yoshihiro.kawaoka@wisc.edu.
Shinji MakinoDepartment of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, TX 77555-1019, USA; Institute for Human Infections and Immunity, The University of Texas Medical Branch, Galveston, TX 77555-1019, USA. Electronic address: shmakino@utmb.edu.
Noam Stern-GinossarDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: noam.stern-ginossar@weizmann.ac.il.
Weizmann Institute of Science · ILIsrael Institute for Biological Research · ILThe University of Texas Medical Branch at Galveston · USUniversity of Wisconsin–Madison · US

Funding

Interplay between coronaviruses and nonsense-mediated mRNA decay pathwayR01AI146081 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI MAKINO, SHINJI · 2020 to 2023
$1.2M
NIAID NIH HHS HHSN272201400008CNIAID NIH HHS R01 AI146081
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) leads to shutoff of protein synthesis, and nsp1, a central shutoff factor in coronaviruses, inhibits cellular mRNA translation. However, the diverse molecular mechanisms employed by nsp1 as well as its functional importance are unresolved. By overexpressing various nsp1 mutants and generating a SARS-CoV-2 mutant, we show that nsp1, through inhibition of translation and induction of mRNA degradation, targets translated cellular mRNA and is the main driver of host shutoff during infection. The propagation of nsp1 mutant virus is inhibited exclusively in cells with intact interferon (IFN) pathway as well as in vivo, in hamsters, and this attenuation is associated with stronger induction of type I IFN response. Therefore, although nsp1's shutoff activity is broad, it plays an essential role, specifically in counteracting the IFN response. Overall, our results reveal the multifaceted approach nsp1 uses to shut off cellular protein synthesis and uncover nsp1's explicit role in blocking the IFN response.

Indexed as

COVID-19Viral Nonstructural ProteinsCell LineHumansRNA StabilitySARS-CoV-2Viral Nonstructural ProteinsCoronavirusesCP: MicrobiologyHost shutoffInterferonNsp1RNASARS-CoV-2Translation regulation

Identifiers

PMID35671758
PMCPMC9133101
OpenAlexW4281656701

What OpenQuestion holds

Textmetadata
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.