Evidence map›Paper›PMID 37415298›Full record

ArticleRNA biology2023

SARS-CoV-2 Nsp1 mediated mRNA degradation requires mRNA interaction with the ribosome.

Soraya I Shehata, Roy Parker

Open access · goldAbstract read
In one paragraph

Article in RNA biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. 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
  3. Article
  4. Article
  5. Article
  6. Review
  7. Structure-function mapping and mechanistic insights on the SARS CoV2 Nsp1.Protein science : a publication of the Protein Society · 2024
    Article
  8. 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
  9. Inhibition of mRNA nuclear export promotes SARS-CoV-2 pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Review
  12. Review
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Soraya I ShehataDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO, USA; Medical Scientist Training Program, University of Colorado Anschutz Medical Campus, Aurora, CO, USA.ORCID 0000-0002-2909-064X
Roy ParkerDepartment of Biochemistry, University of Colorado Boulder, Boulder, CO, USA; Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, CO, USA.ORCID 0000-0002-8412-4152
Howard Hughes Medical Institute · USUniversity of Colorado Boulder · US

Funding

Stress Granules in Yeast and MammalsR01GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 1991 to 2021
$3.3M
Understanding and Manipulating the Degradation of the C9orf72 Repeat Expansion RNAF30AG076323 · NIA · UNIVERSITY OF COLORADO · PI SHEHATA, SORAYA I · 2022 to 2024
$121k
NIA NIH HHS F30 AG076323NIGMS NIH HHS R01 GM045443
6 · The paper itself

Abstract

Nsp1 is a SARS-CoV-2 host shutoff factor that both represses cellular translation and promotes host RNA decay. However, it is unclear how these two activities are connected and interact with normal translation processes. Here, we performed mutational analyses of Nsp1, and these revealed that both the N and C terminal domains of Nsp1 are important for translational repression. Furthermore, we demonstrate that specific residues in the N terminal domain are required for cellular RNA degradation but not bulk translation shutoff of host mRNAs, thereby separating RNA degradation from translation repression. We also present evidence that Nsp1 mediated RNA degradation requires engagement of the ribosome with mRNA. First, we observe that cytosolic lncRNAs, which are not translated, escape Nsp1 mediated degradation. Second, inhibition of translation elongation with emetine does not prevent Nsp1 mediated degradation, while blocking translation initiation before 48S ribosome loading reduces mRNA degradation. Taken together, we suggest that Nsp1 represses translation and promotes mRNA degradation only after ribosome engagement with the mRNA. This raises the possibility that Nsp1 may trigger RNA degradation through pathways that recognize stalled ribosomes.

Indexed as

COVID-19SARS-CoV-2HumansProtein BiosynthesisRibosomesRNA, MessengerRNA StabilityViral Nonstructural ProteinsRNA, MessengerViral Nonstructural Proteinshost shutoffNsp1RNA decaySARS-CoV-2stress granuletranslation

Identifiers

PMID37415298
PMCPMC10332192
OpenAlexW4383482065

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.