期刊
AQUACULTURE
卷 538, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.aquaculture.2021.736583
关键词
Spring viremia of carp virus (SVCV); N protein; Ubiquitination degradation; Viperin_sv1
资金
- National Natural Science Foundation of China [31972834]
- National Key Research and Development Program of China [2018YFD0900505]
Viperin_sv1, a novel splice variant with stronger antiviral effect than viperin, is degraded by SVCV infection through the ubiquitin-proteasome pathway. The degradation can be prevented by mutating viperin_sv1 at Lys201, suggesting a new defense mechanism of SVCV to interfere with the host immune response.
Viperin is known as interferon-stimulating genes (ISGs) and plays broad-spectrum antiviral effects during viral infection. Viperin_sv1, a novel viperin splice variant, has recently been identified from SVCV-infected FHM cells with a stronger antiviral effect than viperin by activating IFN signaling pathway. Meanwhile, SVCV infection can suppress the protein level of viperin_sv1 to escape the host immune but the related mechanism remains to be unclear. In this study, the degradation of viperin_sv1 protein was confirmed to be significantly activated by SVCV infection and recovered by MG132 but not NH4Cl or 3-MA. SVCV infection also enhanced the ubiquitination of viperin_sv1, which proved that the viperin_sv1 was degraded through the ubiquitin-proteasome pathway (UPP). Overexpression of SVCV-N protein was able to lead to the degradation of viperin-sv1 while mutating the viperin_sv1 at Lys201 blocked the degradation during SVCV infection or SVCV-N protein overexpression. Besides, the western blot and qRT-PCR tests showed the viperin_sv1-K201R-mediated IFN production is more stable and plays a stronger inhibitory effect on SVCV replication than viperin_sv1. Taken together, this study demonstrates a new defense mechanism of SVCV to dampen the host IFN response by interfering and degrading viperin_sv1.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据