Evidence map›Paper›PMID 42183758›Full record

ArticleVirulence2026

Encephalomyocarditis virus evades IFN-mediated antiviral response by RNF149 targeting JAK1 for ubiquitination and degradation.

Peng Ma, Qi Xie, Yixiao Yang, Yujing Song, Mingquan Liu, Jianting Li, Linjie Li, Zheng Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virulence, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

8 authors.

Peng MaCollege of Basic Medicine, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, China.ORCID 0000-0003-1302-0556
Qi XieCollege of Basic Medicine, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, China.
Yixiao YangSchool of Public Health, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, China.
Yujing SongSchool of Public Health, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, China.
Mingquan LiuCollege of Basic Medicine, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, China.
Jianting LiCollege of Basic Medicine, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, China.
Linjie LiDatong Center for Disease Control and Prevention, Datong, China.
Zheng WangKey Laboratory of Bio-Resources and Eco-Environment, Animal Disease Prevention and Green Development Key Laboratory of Sichuan Province, College of Life Science, Sichuan University, Chengdu, China.ORCID 0009-0004-6313-7810

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Encephalomyocarditis virus (EMCV), an important zoonotic pathogen, causes an acute disease characterized primarily by encephalitis and myocarditis. Interferon (IFN) activates the JAK-STAT signaling pathway to induce the expression of interferon-stimulated genes (ISGs), resulting in antiviral effects. However, the mechanism through which EMCV evades the immune system via the IFN-mediated JAK-STAT signaling pathway remains poorly understood. Here, we identified an E3 ubiquitin ligase, RNF149, that is upregulated in EMCV-infected cells. Overexpression of RNF149 inhibited type I IFN-mediated JAK-STAT signaling pathway activation and its antiviral response, enhancing viral replication. Knockout of RNF149 promoted ISGs expression. Notably, RNF149 interacted with JAK1 and downregulated its protein expression through the E3 ubiquitin ligase. RNF149 promoted the K27- and K33-linked ubiquitination of JAK1, which promoted JAK1 degradation through the proteasome pathway. Taken together, these data describe a negative regulatory mechanism involving RNF149 in interferon antiviral activity and provide insights into the mechanism by which EMCV evades host antiviral immunity. These results provide a new strategy for treating viral infections.

Indexed as

Encephalomyocarditis virusImmune EvasionInterferonsInterferon Type IJanus Kinase 1Ubiquitin-Protein LigasesAnimalsCell LineHEK293 CellsHost-Pathogen InteractionsHumansProteolysisSignal TransductionUbiquitinationVirus ReplicationInterferonsInterferon Type IJAK1 protein, humanJanus Kinase 1Ubiquitin-Protein LigasesEncephalomyocarditis virusinterferonJAK1RNF149ubiquitination

Identifiers

PMID42183758
PMCPMC13203054

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Registered trials

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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.