The N-terminus of Bunyamwera orthobunyavirus NSs protein is essential for interferon antagonism

被引：44
|
作者：
van Knippenberg, Ingeborg [1 ]
Carlton-Smith, Charlie [1 ]
Elliott, Richard M. [1 ]
机构：
[1] Univ St Andrews, Biomed Sci Res Ctr, St Andrews KY16 9ST, Fife, Scotland
来源：
JOURNAL OF GENERAL VIROLOGY | 2010年 / 91卷
基金：
英国惠康基金; 英国生物技术与生命科学研究理事会;
关键词：
PHOSPHORYLATION; TRANSLATION; DEGRADATION; COUNTERACTS; INDUCTION; MECHANISM; PRODUCT;
D O I：
10.1099/vir.0.021774-0
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Bunyamwera virus NSs protein is involved in the inhibition of cellular transcription and the interferon (IFN) response, and it interacts with the Med8 component of Mediator. A spontaneous mutant of a recombinant NSs-deleted Bunyamwera virus (rBUNdeINSs2) was identified and characterized. This mutant virus, termed mBUNNSs22, expresses a 21 aa N-terminally truncated form of NSs. Like rBUNdeINSs2, mBUNNSs22 is attenuated in IFN-deficient cells, and to a greater extent in IFN-competent cells. Both rBUNdeINSs2 and mBUNNSs22 are potent IFN inducers and their growth can be rescued by depleting cellular IRF3. Strikingly, despite encoding an NSs protein that contains the Med8 interaction domain, mBUNNSs22 fails to block RNA polymerase II activity during infection. Overall, our data suggest that both the interaction of NSs with Med8 and a novel unidentified function of the NSs N-terminus, seem necessary for Bunyamwera virus to counteract host antiviral responses.
引用
收藏
页码：2002 / 2006
页数：5
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