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

被引:111
作者
Hartman, AL [1 ]
Towner, JS [1 ]
Nichol, ST [1 ]
机构
[1] Ctr Dis Control & Prevent, Special Pathogens Branch, Div Viral & Rickettsial Dis, Natl Ctr Infect Dis, Atlanta, GA 30329 USA
关键词
filovirus; ebolavirus; hemorrhagic fever; interferon; VP35; NS1; influenza;
D O I
10.1016/j.virol.2004.07.006
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:177 / 184
页数:8
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