The host protein CALCOCO2 interacts with bovine viral diarrhoea virus Npro, inhibiting type I interferon production and thereby promoting viral replication
文献类型: 外文期刊
第一作者: Wang, Song
作者: Wang, Song;Wang, Song;Ma, Xiaomei;Guo, Jin;Aizaz, Muhammad;Li, Fangxu;Wang, Jun;Wang, Hongmei;He, Hongbin;Wei, Ran
作者机构:
关键词: BVDV; Npro; CALCOCO2; IRF3; IFN-I; innate immunity
期刊名称:VIRULENCE ( 影响因子:5.2; 五年影响因子:5.9 )
ISSN: 2150-5594
年卷期: 2024 年 15 卷 1 期
页码:
收录情况: SCI
摘要: Bovine viral diarrhoea-mucosal disease caused by bovine viral diarrhoea virus (BVDV) is a major infectious disease that affects the cattle industry. The nonstructural protein Npro of BVDV antagonizes the type I interferon (IFN-I) pathway, thereby escaping the host immune response. The exact mechanism by which Npro uses host proteins to inhibit IFN-I production is unclear. The host protein CALCOCO2 was identified as a binding partner of Npro using a yeast two-hybrid screen. The interaction between Npro and CALCOCO2 was confirmed by yeast co-transformation, co-immunoprecipitation assays, and GST pull-down assays. The stable overexpression of CALCOCO2 markedly promoted BVDV propagation, while the knockdown of CALCOCO2 significantly inhibited BVDV replication in MDBK cells. Interestingly, CALCOCO2 inhibited IFN-I and IFN-stimulated gene production in BVDV-infected cells. Ectopic expression of CALCOCO2 effectively reduced IRF3 protein levels via the proteasome pathway. CALCOCO2 was found to promote Npro-mediated ubiquitination degradation of IRF3 by interacting with IRF3. Our results demonstrate the molecular mechanism by which Npro recruits the CALCOCO2 protein to regulate IRF3 degradation to inhibit IFN-I production.
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