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

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ElliottGeneralVirology91-N-terminus.pdf (258.7Kb)
Date
04/2010
Author
Van Knippenberg, Ingeborg Christine
Carlton-Smith, Charles
Elliott, Richard Michael
Funder
The Wellcome Trust
Medical Research Council
Grant ID
079810/Z/06/Z
G0800161
Keywords
QR Microbiology
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Abstract
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 (rBUNdelNSs2) was identified and characterized. This mutant virus, termed mBUNNSs22, expresses a 21 aa N-terminally truncated form of NSs. Like rBUNdelNSs2, mBUNNSs22 is attenuated in IFN-deficient cells, and to a greater extent in IFN-competent cells. Both rBUNdelNSs2 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.
Citation
Van Knippenberg , I C , Carlton-Smith , C & Elliott , R M 2010 , ' The N-terminus of Bunyamwera orthobunyavirus NSs protein is essential for interferon antagonism ' , Journal of General Virology , vol. 91 , no. 8 , pp. 2002-2006 . https://doi.org/10.1099/vir.0.021774-0
Publication
Journal of General Virology
Status
Peer reviewed
DOI
https://doi.org/10.1099/vir.0.021774-0
ISSN
0022-1317
Type
Journal article
Rights
This article is published by the Society for General Microbiology under the Open Option which allows reuse for non commercial purposes.
Description
This work is supported by UK MRC and BBRC
Collections
  • Biology Research
  • Biomedical Sciences Research Complex (BSRC) Research
  • University of St Andrews Research
URL
http://www.scopus.com/inward/record.url?scp=77955297217&partnerID=8YFLogxK
URI
http://hdl.handle.net/10023/1148

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