Evidence map›Paper›PMID 42478070›Full record

ArticleTransboundary and emerging diseases2026

Porcine Deltacoronavirus Nsp13 Suppresses the Assembly of the MAVS-TBK1-IRF3 Complex and IRF9 Nuclear Translocation.

Ying Wang, Shijin Lan, Zhenghui Fang, Shixing Yang, Xiaochun Wang, Quan Shen, Yuwei Liu, Ping Wu, Chenglin Zhou, Wen Zhang and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Transboundary and emerging diseases, 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

11 authors.

Ying WangSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.ORCID https://orcid.org/0009-0003-6540-4831
Shijin LanSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.ORCID https://orcid.org/0009-0007-9351-2732
Zhenghui FangSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.
Shixing YangSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.
Xiaochun WangSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.
Quan ShenSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.
Yuwei LiuSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.ORCID https://orcid.org/0000-0002-5495-2926
Ping WuSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.
Chenglin ZhouClinical Laboratory Center, The Affiliated Taizhou People's Hospital of Nanjing Medical University, Taizhou 225300, China, njucm.edu.cn.ORCID https://orcid.org/0000-0003-2661-2067
Wen ZhangSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.ORCID https://orcid.org/0000-0002-9352-6153
Likai JiSchool of Medicine, Jiangsu University, Zhenjiang 212013, China, ujs.edu.cn.ORCID https://orcid.org/0009-0007-0411-7774

Funding

China Postdoctoral Science Foundation 2022M721391National Natural Science Foundation of China 32102682Natural Science Foundation of Higher Education of Jiangsu Province 21KJB230006
6 · The paper itself

Abstract

Porcine deltacoronavirus (PDCoV) is an emerging enteric coronavirus that causes substantial morbidity in swine and may pose a zoonotic risk because of its cross-species transmission potential. Type I interferon (IFN-I) signaling is central to antiviral defense, initiated through the mitochondrial antiviral signaling (MAVS)-TBK1-IFN regulatory factor 3 (IRF3) axis and executed by the downstream JAK-STAT1-STAT2-IRF9 (ISGF3) pathway; however, how PDCoV circumvents both the induction and effector arms of this cascade remains incompletely understood. Here, we identify PDCoV nonstructural protein 13 (Nsp13) as a potent antagonist of IFN-I responses. Ectopic expression of Nsp13 markedly reduces IFN-β production and the expression of IFN-stimulated genes (ISGs, such as ISG56 and CXCL10). Mechanistically, Nsp13 directly binds the C-terminal domain (CTD) of TBK1 and competitively disrupts TBK1 interactions with IRF3 and MAVS. In addition, Nsp13 preferentially binds IRF9 and impairs its nuclear translocation, thereby inhibiting IFN-α-induced signaling. Notably, PDCoV Nsp13 exhibits a host-target binding profile similar to that of SARS-CoV-2 Nsp13, yet it does not alter TBK1 ubiquitination or protein stability. Collectively, these findings reveal a dual-layer immune evasion strategy whereby PDCoV Nsp13 suppresses both IFN induction and downstream signaling, and highlighting Nsp13 as a potential target for antiviral intervention.

Indexed as

Adaptor Proteins, Signal TransducingCoronavirus InfectionsDeltacoronavirusInterferon Regulatory Factor-3Interferon-Stimulated Gene Factor 3, gamma SubunitProtein Serine-Threonine KinasesSwine DiseasesViral Nonstructural ProteinsAnimalsHumansInterferon Type ISignal TransductionSwineAdaptor Proteins, Signal TransducingInterferon Regulatory Factor-3Interferon-Stimulated Gene Factor 3, gamma SubunitInterferon Type IProtein Serine-Threonine KinasesViral Nonstructural ProteinsIFN-IIRF9PDCoV Nsp13TBK1

Identifiers

PMID42478070
PMCPMC13385975

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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.