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Journal of virology2026; 100(6); e0206125; doi: 10.1128/jvi.02061-25

Equine arteritis virus Nsp10 promotes MAVS proteasomal degradation via E3 ligases Smurf1/MARCH5.

Abstract: Equine arteritis virus (EAV) is a positive-sense, single-stranded RNA virus that belongs to the family , which also includes porcine reproductive and respiratory syndrome virus (PRRSV). EAV is the causative agent of equine viral arteritis (EVA), an economically important systemic, reproductive, and respiratory disease of equids. EAV infection triggers host innate immunity, yet the precise strategies employed by the virus to evade immune defenses and achieve productive infection are poorly characterized. In this study, it was observed that EAV infection can induce a cellular IFN response; however, EAV simultaneously significantly suppresses the expression of IFN-β in host cells. Our findings indicate that host cells sense EAV and elicit an IFN response via mitochondrial antiviral-signaling protein (MAVS)-mediated signal, but the virus can dampen this signaling to enhance infection. Further investigation showed that EAV nsp10 protein could interact with MAVS and promote its degradation. By screening, we found that the E3 ubiquitin ligases Smurf1 and MARCH5 are recruited by nsp10 to polyubiquitinate and degrade MAVS. Interestingly, the degradation of MAVS promoted by nsp10 depends on the dimerization of nsp10, which occurs through the interactions of zinc finger motifs. The CARD or PRR domain of MAVS and the 1A domain of nsp10 are responsible for the interaction between MAVS and nsp10. Moreover, we have identified the key amino acid residues that mediate the interactions between nsp10 and its binding partners. Specifically, D249, S287, and the S1/F39/N41 sites are critical for its binding to MAVS, Smurf1, and MARCH5, respectively. This study demonstrated a novel role for the arteriviral RNA helicase nsp10 in targeting MAVS to counteract innate immunity and reveals the mechanism by which EAV antagonizes MAVS.IMPORTANCEDue to the MAVS functions as a "switch" in the immune signal transduction against RNA viruses, MAVS has emerged as the central regulatory target by viruses. Recently, researchers show increasing interest in viral evasion strategies targeting MAVS. The method of antagonism of MAVS by EAV is still unknown. To date, the roles of arteriviral RNA helicases, such as the EAV helicase nsp10, in regulating host cellular responses have received little research attention. In this study, we found that EAV nsp10 could mediate MAVS degradation through the proteasome via the E3 ubiquitin ligases Smurf1 and MARCH5. This is the first time that an arteriviral RNA helicase has been found to have an antagonistic effect on the innate immunity signaling pathway. Overall, our study reveals a novel mechanism by which EAV can evade host innate immunity and provides insight into potential therapeutic strategies for the control of arterivirus infection.
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Publication Date: 2026-05-19 PubMed ID: 42153738PubMed Central: PMC13288486DOI: 10.1128/jvi.02061-25Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

Overview

  • This study investigates how Equine arteritis virus (EAV) evades the host immune response by promoting degradation of the key antiviral signaling protein MAVS through interactions with viral protein nsp10 and host E3 ubiquitin ligases Smurf1 and MARCH5.

Background and Significance

  • EAV is a positive-sense RNA virus that causes equine viral arteritis, affecting horses with systemic, reproductive, and respiratory disease.
  • During viral infection, the host innate immune system mounts an interferon (IFN) response to limit viral replication.
  • MAVS (mitochondrial antiviral-signaling protein) is a critical adaptor protein acting as a signaling hub to trigger IFN production against RNA viruses.
  • Several viruses have evolved mechanisms to antagonize MAVS to evade host immunity, but such strategies for EAV were previously unclear.

Key Findings

  • EAV infection stimulates an initial IFN response but subsequently suppresses IFN-β expression to avoid immune clearance.
  • The viral protein nsp10 interacts directly with MAVS and induces its degradation, thus dampening the MAVS-mediated antiviral signal.
  • This degradation process requires the host’s ubiquitin-proteasome system, specifically involving two E3 ubiquitin ligases, Smurf1 and MARCH5, which are recruited by nsp10.
  • The proteasomal degradation of MAVS depends on nsp10 forming dimers via its zinc finger motifs.
  • MAVS’s CARD or PRR domains interact with the 1A domain of nsp10, facilitating this targeting mechanism.
  • Specific amino acid residues on nsp10 have been identified as critical for these interactions:
    • D249 for MAVS binding
    • S287 for Smurf1 binding
    • S1/F39/N41 for MARCH5 binding

Mechanistic Insights

  • The nsp10 protein, known as an RNA helicase in arteriviruses, contains zinc finger motifs enabling its dimerization—a prerequisite for its function in MAVS degradation.
  • Once nsp10 binds MAVS and recruits Smurf1 and MARCH5, these E3 ligases ubiquitinate MAVS, marking it for degradation via the proteasome.
  • This targeted degradation inhibits the MAVS-mediated antiviral signaling cascade, reducing IFN-β production and thus impairing host antiviral defenses.

Importance and Implications

  • This is the first study demonstrating an arterivirus RNA helicase (nsp10) as a viral factor antagonizing innate immunity by targeting MAVS.
  • The findings advance understanding of viral immune evasion, particularly how EAV modulates host innate immune signaling to promote infection.
  • Identifying precise molecular interactions and critical residues provides potential targets for antiviral drug development aimed at restoring MAVS function.
  • The study suggests that inhibiting nsp10 dimerization or blocking its interaction with Smurf1/MARCH5 could be therapeutic strategies to control EAV infection.

Conclusion

  • The research reveals a novel viral immune evasion mechanism where EAV’s nsp10 targets the key immune signaling protein MAVS for degradation via host E3 ubiquitin ligases Smurf1 and MARCH5.
  • This degradation of MAVS suppresses the innate immune response and facilitates EAV infection, highlighting a critical virus-host interaction that may be exploited for therapeutic development.

Cite This Article

APA
Zhou B, Chen K, Liang H, Qi T, Guo X, Wen Y-J, Du C, Wang X. (2026). Equine arteritis virus Nsp10 promotes MAVS proteasomal degradation via E3 ligases Smurf1/MARCH5. J Virol, 100(6), e0206125. https://doi.org/10.1128/jvi.02061-25

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 100
Issue: 6
Pages: e0206125
PII: e02061-25

Researcher Affiliations

Zhou, Bingqian
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Chen, Kewei
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
  • Key Laboratory for Clinical Diagnosis and Treatment of Animal Diseases of Ministry of Agriculture, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, China.
Liang, Haibing
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Qi, Ting
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Guo, Xing
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Wen, Yong-Jun
  • Key Laboratory for Clinical Diagnosis and Treatment of Animal Diseases of Ministry of Agriculture, College of Veterinary Medicine, Inner Mongolia Agricultural University, Hohhot, China.
Du, Cheng
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Wang, Xiaojun
  • State Key Laboratory of Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
  • Institute of Western Agriculture, Chinese Academy of Agricultural Sciences, Changji, China.
  • China-Kazakhstan Joint Laboratory for Herbivorous Animal Disease Research, Heilongjiang Province, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.

MeSH Terms

  • Animals
  • Equartevirus / metabolism
  • Equartevirus / genetics
  • Adaptor Proteins, Signal Transducing / metabolism
  • Adaptor Proteins, Signal Transducing / genetics
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitin-Protein Ligases / genetics
  • Viral Nonstructural Proteins / metabolism
  • Viral Nonstructural Proteins / genetics
  • Proteasome Endopeptidase Complex / metabolism
  • Horses
  • Humans
  • Immunity, Innate
  • Signal Transduction
  • Proteolysis
  • HEK293 Cells
  • Host-Pathogen Interactions
  • Interferon-beta / metabolism
  • Arterivirus Infections / virology
  • Arterivirus Infections / metabolism
  • Ubiquitination
  • Cell Line
  • Protein Binding

Grant Funding

  • 2025ZD01900100 / Prevention and Control of Emerging and Major Infectious Diseases-National Science and Technology Major Project
  • IWA2023 / Tianchi Talent Introduction Plan
  • ZZYD2023010 / Xinjiang Talent Development Fund

Conflict of Interest Statement

The authors declare no conflict of interest.

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