Center for Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Protein Cell. 2010 Oct;1(10):956-64. doi: 10.1007/s13238-010-0117-8. Epub 2010 Nov 9.
The zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses by eliminating viral mRNAs in the cytoplasm. In previous studies, we demonstrated that ZAP directly binds to the viral mRNAs and recruits the RNA exosome to degrade the target RNA. In this article, we provide evidence that a DEXH box RNA helicase, DHX30, is required for optimal antiviral activity of ZAP. Pull-down and co-immunoprecipitation assays demonstrated that DHX30 and ZAP interacted with each other via their N terminal domains. Downregulation of DHX30 with shRNAs reduced ZAP's antiviral activity. These data implicate that DHX30 is a cellular factor involved in the antiviral function of ZAP.
锌指抗病毒蛋白（ZAP）是一种宿主因子，通过在细胞质中消除病毒 mRNA 来特异性抑制某些病毒的复制。在之前的研究中，我们证明 ZAP 直接与病毒 mRNA 结合，并募集 RNA 外切体来降解靶 RNA。在本文中，我们提供了证据表明 DEXH 盒 RNA 解旋酶 DHX30 是 ZAP 发挥最佳抗病毒活性所必需的。下拉和共免疫沉淀实验表明，DHX30 和 ZAP 通过其 N 端结构域相互作用。用 shRNAs 下调 DHX30 会降低 ZAP 的抗病毒活性。这些数据表明 DHX30 是一种参与 ZAP 抗病毒功能的细胞因子。
