Evidence map›Paper›PMID 29739942›Full record

ArticleNature communications2018

Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition.

Marios G Koliopoulos, Mathilde Lethier, Annemarthe G van der Veen, Kevin Haubrich, Janosch Hennig, Eva Kowalinski, Rebecca V Stevens, Stephen R Martin, Caetano Reis e Sousa, Stephen Cusack and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
7.7field-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

128 citing papers in PubMed, 188 citations in OpenAlex.

  1. Article
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  10. Influenza A virus NS1 protein mimics oncogenic PI3K resulting in isoform specific cellular redistribution and activation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
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  14. Article
  15. Article
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  17. Evolutionary rewiring of the dynamic network underpinning allosteric epistasis in NS1 of the influenza A virus.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Review
  19. Article
  20. A20 as a Potential Therapeutic Target for COVID-19.Immunity, inflammation and disease · 2025
    Review

68 more citing papers are in PubMed but not listed here.

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

11 authors at 2 institutions in 2 countries.

Marios G KoliopoulosMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Mathilde LethierEuropean Molecular Biology Laboratory, 71 Avenue des Martyrs, 38042, Grenoble, Cedex 9, France.
Annemarthe G van der VeenImmunobiology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Kevin HaubrichStructural and Computational Biology Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117, Heidelberg, Germany.
Janosch HennigStructural and Computational Biology Unit, EMBL Heidelberg, Meyerhofstraße 1, 69117, Heidelberg, Germany.
Eva KowalinskiEuropean Molecular Biology Laboratory, 71 Avenue des Martyrs, 38042, Grenoble, Cedex 9, France.
Rebecca V StevensMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Stephen R MartinStructural Biology Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Caetano Reis e SousaImmunobiology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.ORCID 0000-0001-7392-2119
Stephen CusackEuropean Molecular Biology Laboratory, 71 Avenue des Martyrs, 38042, Grenoble, Cedex 9, France.ORCID 0000-0002-9324-0796
Katrin RittingerMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. katrin.rittinger@crick.ac.uk.ORCID 0000-0002-7698-4435
The Francis Crick Institute · GBEuropean Molecular Biology Laboratory · FR

Funding

Wellcome Trust FC001136Wellcome Trust FC001142
6 · The paper itself

Abstract

RIG-I is a viral RNA sensor that induces the production of type I interferon (IFN) in response to infection with a variety of viruses. Modification of RIG-I with K63-linked poly-ubiquitin chains, synthesised by TRIM25, is crucial for activation of the RIG-I/MAVS signalling pathway. TRIM25 activity is targeted by influenza A virus non-structural protein 1 (NS1) to suppress IFN production and prevent an efficient host immune response. Here we present structures of the human TRIM25 coiled-coil-PRYSPRY module and of complexes between the TRIM25 coiled-coil domain and NS1. These structures show that binding of NS1 interferes with the correct positioning of the PRYSPRY domain of TRIM25 required for substrate ubiquitination and provide a mechanistic explanation for how NS1 suppresses RIG-I ubiquitination and hence downstream signalling. In contrast, the formation of unanchored K63-linked poly-ubiquitin chains is unchanged by NS1 binding, indicating that RING dimerisation of TRIM25 is not affected by NS1.

Indexed as

Amino Acid SequenceCells, CulturedDEAD Box Protein 58HEK293 CellsHumansInterferonsProtein BindingProtein DomainsProtein MultimerizationReceptors, ImmunologicRNA, ViralSignal TransductionTranscription FactorsTripartite Motif ProteinsUbiquitinationUbiquitin-Protein LigasesDEAD Box Protein 58INS1 protein, influenza virusInterferonsReceptors, ImmunologicRIGI protein, humanRNA, ViralTranscription FactorsTRIM25 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesViral Nonstructural Proteins

Identifiers

PMID29739942
PMCPMC5940772
OpenAlexW2799425339

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.