Evidence map›Paper›PMID 29107643›Full record

ArticleCell host & microbe2017

Nuclear TRIM25 Specifically Targets Influenza Virus Ribonucleoproteins to Block the Onset of RNA Chain Elongation.

Nicholas R Meyerson, Ligang Zhou, Yusong R Guo, Chen Zhao, Yizhi J Tao, Robert M Krug, Sara L Sawyer

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

Article in Cell host & microbe, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
5.5field-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

77 citing papers in PubMed, 125 citations in OpenAlex.

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  11. Article
  12. Antiviral Effects of Avian Interferon-Stimulated Genes.Animals : an open access journal from MDPI · 2024
    Review
  13. Article
  14. Review
  15. Review
  16. Article
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17 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

7 authors at 2 institutions in 1 country.

Nicholas R MeyersonBioFrontiers Institute, Department of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO 80303, USA.
Ligang ZhouDepartment of Molecular Biosciences, LaMontagne Center for Infectious Disease, University of Texas at Austin, Austin, TX 78712, USA.
Yusong R GuoDepartment of BioSciences, Rice University, Houston, TX 77005, USA.
Chen ZhaoDepartment of Molecular Biosciences, LaMontagne Center for Infectious Disease, University of Texas at Austin, Austin, TX 78712, USA.
Yizhi J TaoDepartment of BioSciences, Rice University, Houston, TX 77005, USA.
Robert M KrugDepartment of Molecular Biosciences, LaMontagne Center for Infectious Disease, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: rkrug@austin.utexas.edu.
Sara L SawyerBioFrontiers Institute, Department of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, CO 80303, USA. Electronic address: ssawyer@colorado.edu.
Rice University · USUniversity of Colorado Boulder · US

Funding

REPLICATION OF INFLUENZA VIRUSR01AI011772 · NIAID · UNIVERSITY OF TEXAS AUSTIN · PI KRUG, ROBERT M · 1985 to 2017
$10.7M
Rapid evolution of genes critical for genome integrityR01GM093086 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI SAWYER, SARA · 2010 to 2016
$1.9M
NIAID NIH HHS R01 AI011772NIGMS NIH HHS R01 GM093086
6 · The paper itself

Abstract

TRIM25 is an E3 ubiquitin ligase that activates RIG-I to promote the antiviral interferon response. The NS1 protein from all strains of influenza A virus binds TRIM25, although not all virus strains block the interferon response, suggesting alternative mechanisms for TRIM25 action. Here we present a nuclear role for TRIM25 in specifically restricting influenza A virus replication. TRIM25 inhibits viral RNA synthesis through a direct mechanism that is independent of its ubiquitin ligase activity and the interferon pathway. This activity can be inhibited by the viral NS1 protein. TRIM25 inhibition of viral RNA synthesis results from its binding to viral ribonucleoproteins (vRNPs), the structures containing individual viral RNA segments, the viral polymerase, and multiple viral nucleoproteins. TRIM25 binding does not inhibit initiation of capped-RNA-primed viral mRNA synthesis by the viral polymerase. Rather, the onset of RNA chain elongation is inhibited because TRIM25 prohibits the movement of RNA into the polymerase complex.

Indexed as

A549 CellsAntiviral AgentsAntiviral Restriction FactorsCarrier ProteinsCell LineDEAD Box Protein 58HEK293 CellsHost-Pathogen InteractionsHumansInfluenza A virusInfluenza A Virus, H3N2 SubtypeInfluenza, HumanInterferonsModels, MolecularProtein BindingReceptors, ImmunologicAntiviral AgentsAntiviral Restriction FactorsCarrier ProteinsDEAD Box Protein 58INS1 protein, influenza virusInterferonsReceptors, ImmunologicRibonucleoproteinsRIGI protein, humanRNA, MessengerRNA, ViralSUMO-1 ProteinTranscription FactorsTRIM25 protein, humanTRIM5 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesViral Nonstructural ProteinsInfluenza virusnuclear TRIM25viral ribonucleoproteinsviral RNA synthesis

Identifiers

PMID29107643
PMCPMC6309188
OpenAlexW2767043304

What OpenQuestion holds

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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.