ArticleJournal of virology2017
Porcine Deltacoronavirus nsp5 Antagonizes Type I Interferon Signaling by Cleaving STAT2.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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Who cites it
110 citing papers in PubMed, 172 citations in OpenAlex.
- PRRSV suppresses FTO-dependentmBio · 2026Article
- Engineering a dimeric porcine deltacoronavirus S-RBD subunit vaccine for enhanced immunogenicity and neutralizing antibody responses.BMC veterinary research · 2026Article
- Coronavirus Nsp5‑mediated dual‑site cleavage of GSDMA modifies its antiviral and proinflammatory functions.PLoS pathogens · 2026Article
- Article
- Porcine Deltacoronavirus Nsp13 Suppresses the Assembly of the MAVS-TBK1-IRF3 Complex and IRF9 Nuclear Translocation.Transboundary and emerging diseases · 2026Article
- UHRF1 restricts HCoV-229E infection through epigenetic silencing of the viral receptor APN.Nature communications · 2025Article
- The coronavirus 3CL protease: Unveiling its complex host interactions and central role in viral pathogenesis.Virologica Sinica · 2025Review
- Cleavage of the selective autophagy receptor NBR1 by the PDCoV main protease NSP5 impairs autophagic degradation of the viral envelope protein.Autophagy · 2025Article
- SADS-CoV nsp5 Inhibits Interferon Production by Targeting Kinase IKKε.Microorganisms · 2025Article
- Review
- HCoV-229E Mpro Suppresses RLR-Mediated Innate Immune Signalling Through Cleavage of NEMO and Through Other Mechanisms.International journal of molecular sciences · 2025Article
- Emerging RNA-centric technologies to probe RNA-protein interactions: importance in decoding the life cycle of positive sense single strand RNA viruses and antiviral discovery.Frontiers in cellular and infection microbiology · 2025Review
- Chebulinic acid suppresses porcine epidemic diarrhea virus infection by inhibiting viral entry and viral main protease.Frontiers in cellular and infection microbiology · 2025Article
- The S2 Pocket Governs the Genus-Specific Substrate Selectivity of Coronavirus 3C-Like Protease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Impaired interferon response in senecavirus A infection and identification of 3CJournal of virology · 2024Article
- Porcine deltacoronavirus nucleocapsid protein antagonizes JAK-STAT signaling pathway by targeting STAT1 through KPNA2 degradation.Journal of virology · 2024Article
- Porcine deltacoronavirus nonstructural protein 2 inhibits type I and III IFN production by targeting STING for degradation.Veterinary research · 2024Article
- Article
- SARS-CoV-2 NSP5 antagonizes MHC II expression by subverting histone deacetylase 2.Journal of cell science · 2024Article
- Deep profiling of potential substrate atlas of porcine epidemic diarrhea virus 3C-like protease.Journal of virology · 2024Article
50 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine deltacoronavirus (PDCoV) is an emerging swine enteropathogenic coronavirus. The first outbreak of PDCoV was announced from the United States in 2014, followed by reports in Asia. The nonstructural protein nsp5 is a 3C-like protease of coronavirus, and our previous study showed that PDCoV nsp5 inhibits type I interferon (IFN) production. In this study, we found that PDCoV nsp5 significantly inhibited IFN-stimulated response element (ISRE) promoter activity and transcription of IFN-stimulated genes (ISGs), suggesting that PDCoV nsp5 also suppresses IFN signaling. Detailed analysis showed that nsp5 cleaved signal transducer and activator of transcription 2 (STAT2) but not Janus kinase 1 (JAK1), tyrosine kinase 2 (TYK2), STAT1, and interferon regulatory factor 9 (IRF9), key molecules of the JAK-STAT pathway. STAT2 cleavage was dependent on the protease activity of nsp5. Interestingly, nsp5 cleaved STAT2 at two sites, glutamine 685 (Q685) and Q758, and similar cleavage was observed in PDCoV-infected cells. As expected, cleaved STAT2 impaired the ability to induce ISGs, demonstrating that STAT2 cleavage is an important mechanism utilized by PDCoV nsp5 to antagonize IFN signaling. We also discussed the substrate selection and binding mode of PDCoV nsp5 by homologous modeling of PDCoV nsp5 with the two cleaved peptide substrates. The results of our study demonstrate that PDCoV nsp5 antagonizes type I IFN signaling by cleaving STAT2 and provides structural insights for comprehending the cleavage mechanism of PDCoV nsp5, revealing a potential new function for PDCoV nsp5 in type I IFN signaling.
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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.