Evidence map›Paper›PMID 34799561›Full record

ArticleNature communications2021

Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities.

Thomas Kruse, Caroline Benz, Dimitriya H Garvanska, Richard Lindqvist, Filip Mihalic, Fabian Coscia, Raviteja Inturi, Ahmed Sayadi, Leandro Simonetti, Emma Nilsson and 12 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.1field-weighted citation impact, top 3% 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

42 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. SARS-CoV-2 S assembly into virions facilitated by host ERM proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  8. Review
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  11. Article
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  13. Article
  14. Article
  15. SARS-CoV-2 biology and host interactions.Nature reviews. Microbiology · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

22 authors at 5 institutions in 4 countries.

Thomas Kruse *The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Caroline Benz *Department of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23, Uppsala, Sweden.ORCID http://orcid.org/0000-0002-5166-3598
Dimitriya H Garvanska *The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Richard Lindqvist *Department of Clinical Microbiology, Umeå University, 90185, Umeå, Sweden.
Filip MihalicDepartment of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, Husargatan 3, 751 23, Uppsala, Sweden.
Fabian CosciaThe Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Raviteja InturiDepartment of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, Husargatan 3, 751 23, Uppsala, Sweden.ORCID http://orcid.org/0000-0003-1344-3962
Ahmed SayadiDepartment of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23, Uppsala, Sweden.
Leandro SimonettiDepartment of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23, Uppsala, Sweden.ORCID http://orcid.org/0000-0003-1283-9770
Emma NilssonDepartment of Clinical Microbiology, Umeå University, 90185, Umeå, Sweden.
Muhammad AliDepartment of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23, Uppsala, Sweden.ORCID http://orcid.org/0000-0002-8858-6776
Johanna KlicheDepartment of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23, Uppsala, Sweden.
Ainhoa Moliner MorroDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
Andreas MundThe Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, 2200, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-7843-5341
Eva AnderssonDepartment of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, Husargatan 3, 751 23, Uppsala, Sweden.
Gerald McInerneyDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-2257-7241
Matthias MannThe Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Per JemthDepartment of Medical Biochemistry and Microbiology, Uppsala University, BMC, Box 582, Husargatan 3, 751 23, Uppsala, Sweden.ORCID http://orcid.org/0000-0003-1516-7228
Norman E DaveyDivision of Cancer Biology, The Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, UK.
Anna K ÖverbyDepartment of Clinical Microbiology, Umeå University, 90185, Umeå, Sweden. anna.overby@umu.se.ORCID http://orcid.org/0000-0001-6553-0940
Jakob NilssonThe Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health and Medical Sciences, Blegdamsvej 3B, 2200, Copenhagen, Denmark. jakob.nilsson@cpr.ku.dk.ORCID http://orcid.org/0000-0003-4100-1125
Ylva IvarssonDepartment of Chemistry - BMC, Uppsala University, Box 576, Husargatan 3, 751 23, Uppsala, Sweden. ylva.ivarsson@kemi.uu.se.ORCID http://orcid.org/0000-0002-7081-3846
Uppsala University · SEUniversity of Copenhagen · DKUmeå University · SEKarolinska Institutet · SEInstitute of Cancer Research · GB

Funding

Cancer Research UK 28159
6 · The paper itself

Abstract

Viral proteins make extensive use of short peptide interaction motifs to hijack cellular host factors. However, most current large-scale methods do not identify this important class of protein-protein interactions. Uncovering peptide mediated interactions provides both a molecular understanding of viral interactions with their host and the foundation for developing novel antiviral reagents. Here we describe a viral peptide discovery approach covering 23 coronavirus strains that provides high resolution information on direct virus-host interactions. We identify 269 peptide-based interactions for 18 coronaviruses including a specific interaction between the human G3BP1/2 proteins and an ΦxFG peptide motif in the SARS-CoV-2 nucleocapsid (N) protein. This interaction supports viral replication and through its ΦxFG motif N rewires the G3BP1/2 interactome to disrupt stress granules. A peptide-based inhibitor disrupting the G3BP1/2-N interaction dampened SARS-CoV-2 infection showing that our results can be directly translated into novel specific antiviral reagents.

Indexed as

Adaptor Proteins, Signal TransducingDNA HelicasesHumansIntegration Host FactorsPoly-ADP-Ribose Binding ProteinsRNA-Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsSARS-CoV-2Virus ReplicationAdaptor Proteins, Signal TransducingDNA HelicasesG3BP1 protein, humanG3BP2 protein, humanIntegration Host FactorsPoly-ADP-Ribose Binding ProteinsRNA-Binding ProteinsRNA HelicasesRNA Recognition Motif Proteins

Identifiers

PMID34799561
PMCPMC8605023
OpenAlexW3212975895

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.