Evidence map›Paper›PMID 35893676›Full record

ArticleViruses2022

TRIM7 Restricts Coxsackievirus and Norovirus Infection by Detecting the C-Terminal Glutamine Generated by 3C Protease Processing.

Jakub Luptak, Donna L Mallery, Aminu S Jahun, Anna Albecka, Dean Clift, Osaid Ather, Greg Slodkowicz, Ian Goodfellow, Leo C James

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  10. Article
  11. Interplay between TRIM7 and antiviral immunity.Frontiers in cellular and infection microbiology · 2023
    Review
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.

Jakub LuptakMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.ORCID 0000-0002-9527-8755
Donna L MalleryMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Aminu S JahunDivision of Virology, Department of Pathology, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.ORCID 0000-0002-4585-1701
Anna AlbeckaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Dean CliftMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Osaid AtherMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Greg SlodkowiczThe Francis Crick Institute, London NW1 1AT, UK.
Ian GoodfellowDivision of Virology, Department of Pathology, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
Leo C JamesMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
MRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GBThe Francis Crick Institute · GB

Funding

Medical Research Council MC_U105181010Medical Research Council MR/S023380/1Medical Research Council U105181010Wellcome TrustWellcome Trust 200594/Z/16/ZWellcome Trust 207498/Z/17/ZWellcome Trust 214344/A/18/Z
6 · The paper itself

Abstract

TRIM7 catalyzes the ubiquitination of multiple substrates with unrelated biological functions. This cross-reactivity is at odds with the specificity usually displayed by enzymes, including ubiquitin ligases. Here we show that TRIM7's extreme substrate promiscuity is due to a highly unusual binding mechanism, in which the PRYSPRY domain captures any ligand with a C-terminal helix that terminates in a hydrophobic residue followed by a glutamine. Many of the non-structural proteins found in RNA viruses contain C-terminal glutamines as a result of polyprotein cleavage by 3C protease. This viral processing strategy generates novel substrates for TRIM7 and explains its ability to inhibit Coxsackie virus and norovirus replication. In addition to viral proteins, cellular proteins such as glycogenin have evolved C-termini that make them a TRIM7 substrate. The 'helix-ΦQ' degron motif recognized by TRIM7 is reminiscent of the N-end degron system and is found in ~1% of cellular proteins. These features, together with TRIM7's restricted tissue expression and lack of immune regulation, suggest that viral restriction may not be its physiological function.

Indexed as

Caliciviridae InfectionsGlutamineTripartite Motif ProteinsUbiquitin-Protein Ligases3C Viral ProteasesEnterovirusHumansNorovirusViral Proteins3C Viral ProteasesGlutamineTRIM7 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesViral Proteins3Cpro3C proteasecoxsackievirusdegradationISGMproNorovirusrestrictionSARS-CoV-2TRIM7

Identifiers

PMID35893676
PMCPMC9394474
OpenAlexW4287219586

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.