Evidence map›Paper›PMID 34369011›Full record

ArticleProteins2022

A distinct ssDNA/RNA binding interface in the Nsp9 protein from SARS-CoV-2.

Serene El-Kamand, Mar-Dean Du Plessis, Natasha Breen, Lexie Johnson, Samuel Beard, Ann H Kwan, Derek J Richard, Liza Cubeddu, Roland Gamsjaeger

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 13% 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, 28 citations in OpenAlex.

  1. Article
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  7. Article
  8. Review
  9. Article
  10. SARS-CoV-2 and the DNA damage response.The Journal of general virology · 2023
    Review
  11. Article
  12. Article
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  15. 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

9 authors at 3 institutions in 1 country.

Serene El-KamandSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Mar-Dean Du PlessisSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Natasha BreenSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Lexie JohnsonSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Samuel BeardSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, Queensland, Australia.
Ann H KwanSchool of Life and Environmental Sciences and Sydney Nano Institute, University of Sydney, New South Wales, Australia.
Derek J RichardSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, Queensland, Australia.
Liza CubedduSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.
Roland GamsjaegerSchool of Science, Western Sydney University, Penrith, New South Wales, Australia.ORCID https://orcid.org/0000-0003-1095-2569
Western Sydney University · AUThe University of Sydney · AUTranslational Research Institute · AU

Funding

Western Sydney University
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel, highly infectious RNA virus that belongs to the coronavirus family. Replication of the viral genome is a fundamental step in the virus life cycle and SARS-CoV-2 non-structural protein 9 (Nsp9) is shown to be essential for virus replication through its ability to bind RNA in the closely related SARS-CoV-1 strain. Two recent studies revealing the three-dimensional structure of Nsp9 from SARS-CoV-2 have demonstrated a high degree of similarity between Nsp9 proteins within the coronavirus family. However, the binding affinity to RNA is very low which, until now, has prevented the determination of the structural details of this interaction. In this study, we have utilized nuclear magnetic resonance spectroscopy (NMR) in combination with surface biolayer interferometry (BLI) to reveal a distinct binding interface for both ssDNA and RNA that is different to the one proposed in the recently solved SARS-CoV-2 replication and transcription complex (RTC) structure. Based on these data, we have proposed a structural model of a Nsp9-RNA complex, shedding light on the molecular details of these important interactions.

Indexed as

Binding SitesDNA, Single-StrandedInterferometryMagnetic Resonance SpectroscopyModels, MolecularProtein ConformationProtein MultimerizationRNARNA-Binding ProteinsSolutionsViral Nonstructural ProteinsDNA, Single-StrandedORF1ab polyprotein, SARS-CoV-2RNARNA-Binding ProteinsSolutionsViral Nonstructural ProteinscoronavirusCOVID-19Nsp9RNASARS-CoV-2

Identifiers

PMID34369011
PMCPMC8441931
OpenAlexW3190773265

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.