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

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 TRI...

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Published in:Veterinary research (Paris) 2024-04, Vol.55 (1), p.44-44, Article 44
Main Authors: 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, Da, Feng, Li
Format: Article
Language:English
Subjects:
Alphacoronavirus - metabolism
Animals
Biological response modifiers
Coronaviruses
DEAD Box Protein 58 - metabolism
Diarrhea
Hogs
Interferon
Interferons - genetics
Kinases
Life Sciences
Middle East respiratory syndrome
nucleocapsid
Nucleocapsid Proteins
Oligomers
Plasmids
Pork industry
RIG-I
Scientific equipment and supplies industry
Swine
Swine acute diarrhea syndrome coronavirus
TRIM25
Viruses
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Summary: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.
ISSN:1297-9716
0928-4249
1297-9716
DOI:10.1186/s13567-024-01303-z