Swine acute diarrhea syndrome coronavirus nucleocapsid protein antagonizes the IFN response through inhibiting TRIM25 oligomerization and functional activation of RIG-I/TRIM25
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Published:2024-04-08
Issue:1
Volume:55
Page:
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ISSN:1297-9716
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Container-title:Veterinary Research
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language:en
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Short-container-title:Vet Res
Author:
Zhang Jiyu, Shi Hongyan, Zhang Liaoyuan, Feng Tingshuai, Chen Jianfei, Zhang Xin, Ji Zhaoyang, Jing Zhaoyang, Zhu Xiaoyuan, Liu Dakai, Yang Xiaoman, Zeng Miaomiao, Shi DaORCID, Feng Li
Abstract
AbstractSwine 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.
Funder
the Regional Innovation and Development Joint Fund of National Natural Science Foundation of China the National Key R&D Program of China the Central Public-interest Scientific Institution Basal Research Found
Publisher
Springer Science and Business Media LLC
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