扎伊尔埃博拉病毒VP35的C末端碱性氨基酸基序对于I型干扰素拮抗作用至关重要，并且与另一种干扰素拮抗剂甲型流感病毒NS1蛋白的RNA结合结构域具有高度同源性。
A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential for type I interferon antagonism and displays high identity with the RNA-binding domain of another interferon antagonist, the NS1 protein of influenza A virus.
作者信息
Hartman Amy L, Towner Jonathan S, Nichol Stuart T
机构信息
Special Pathogens Branch, Division of Viral and Rickettsial Diseases, National Center for Infectious Diseases, Centers for Disease Control and Prevention, 1600 Clifton Road MS G-14 Atlanta, GA 30329, USA.
出版信息
Virology. 2004 Oct 25;328(2):177-84. doi: 10.1016/j.virol.2004.07.006.
The ebolavirus VP35 protein antagonizes the cellular type I interferon response by blocking phosphorylation of IRF-3, a transcription factor that turns on the expression of a large number of antiviral genes. To identify the domain of VP35 responsible for interferon antagonism, we generated mutations within the VP35 gene and found that a C-terminal basic amino acid motif is required for inhibition of ISG56 reporter gene expression as well as IFN-beta production. Remarkably, this basic amino acid motif displayed high sequence identity with part of the N-terminal RNA-binding domain of another interferon-antagonist, the NS1 protein of influenza A virus.
埃博拉病毒VP35蛋白通过阻断转录因子IRF-3的磷酸化来拮抗细胞I型干扰素反应，IRF-3可开启大量抗病毒基因的表达。为了确定VP35中负责干扰素拮抗作用的结构域，我们在VP35基因内产生了突变，发现C端碱性氨基酸基序是抑制ISG56报告基因表达以及IFN-β产生所必需的。值得注意的是，这个碱性氨基酸基序与另一种干扰素拮抗剂甲型流感病毒NS1蛋白的N端RNA结合结构域的一部分具有高度的序列同一性。
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