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Swine acute diarrhea syndrome coronavirus nucleocapsid protein antagonizes the IFN response through inhibiting TRIM25 oligomerization and functional activation of RIG-I/TRIM25

文献类型： 外文期刊

作者： Zhang J.;Shi H.;Zhang L.;Feng T.;Chen J.;Zhang X.;Ji Z.;Jing Z.;Zhu X.;Liu D.;Yang X.;Zeng M.;Shi D.;Feng L.

作者机构：

关键词： interferon;nucleocapsid;RIG-I;Swine acute diarrhea syndrome coronavirus;TRIM25

期刊名称： Veterinary research

ISSN： 1297-9716

年卷期： 2024 年 55 卷 1 期

页码：

收录情况： SCIE（2024版）

摘要： Swine acute diarrhea syndrome coronavirus (SADS-CoV), an emerging Alpha-coronavirus, brings huge economic loss in swine industry. Interferons (IFNs) participate in a frontline antiviral defense mechanism triggering the activation of numerous downstream antiviral genes. Here, we demonstrated that TRIM25 overexpression significantly inhibited SADS-CoV replication, whereas TRIM25 deficiency markedly increased viral yield. We found that SADS-CoV N protein suppressed interferon-beta (IFN-β) production induced by Sendai virus (SeV) or poly(I:C). Moreover, we determined that SADS-CoV N protein interacted with RIG-I N-terminal two caspase activation and recruitment domains (2CARDs) and TRIM25 coiled-coil dimerization (CCD) domain. The interaction of SADS-CoV N protein with RIG-I and TRIM25 caused TRIM25 multimerization inhibition, the RIG-I-TRIM25 interaction disruption, and consequent the IRF3 and TBK1 phosphorylation impediment. Overexpression of SADS-CoV N protein facilitated the replication of VSV-GFP by suppressing IFN-β production. Our results demonstrate that SADS-CoV N suppresses the host IFN response, thus highlighting the significant involvement of TRIM25 in regulating antiviral immune defenses. © 2024. The Author(s).

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