Source:http://linkedlifedata.com/resource/pubmed/id/17548221
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2007-6-22
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pubmed:abstractText |
The paramyxovirus P gene encodes accessory proteins antagonistic to interferon (IFN). Viral proteins responsible for the IFN antagonism, however, are distinct among paramyxoviruses. Here we determine bovine parainfluenza virus type 3 (bPIV3) IFN antagonists that suppress IFN-beta production, and investigate the underlying molecular mechanism. Of bPIV3 P gene products, C and V proteins were found to suppress double-stranded RNA-stimulated IFN-beta production. The V protein of bPIV3 and Sendai virus in the same genus Respirovirus significantly inhibits double-stranded RNA-stimulated IFN-beta production and the IFN-beta promoter activation enhanced by overexpression of MDA5 but not RIG-I, and yet does not suppress IFN-beta production induced by TRIF, TBK1, and IKKi. The V protein of both viruses specifically binds to MDA5 but not RIG-I. These results suggest that the V protein targets MDA5 for blockage of the IFN-beta gene activation signal. On the other hand, both bPIV3 and Sendai virus C proteins modestly inhibited IFN-beta production irrespective of a species of the signaling molecules used as an inducer. Interestingly, reporter gene expression driven by various promoters was also suppressed by the C proteins irrespective of the promoter species. These results demonstrate that the target of the respirovirus C protein is undoubtedly different from that of the V protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DDX58 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/IFIH1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-beta,
http://linkedlifedata.com/resource/pubmed/chemical/V protein, Sendai virus,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nonstructural C protein, Sendai...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1286-4579
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
954-62
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17548221-Animals,
pubmed-meshheading:17548221-Cattle,
pubmed-meshheading:17548221-Cell Line,
pubmed-meshheading:17548221-DEAD-box RNA Helicases,
pubmed-meshheading:17548221-Gene Expression Regulation,
pubmed-meshheading:17548221-HeLa Cells,
pubmed-meshheading:17548221-Humans,
pubmed-meshheading:17548221-Interferon-beta,
pubmed-meshheading:17548221-Parainfluenza Virus 3, Bovine,
pubmed-meshheading:17548221-Signal Transduction,
pubmed-meshheading:17548221-Transcriptional Activation,
pubmed-meshheading:17548221-Viral Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Bovine parainfluenza virus type 3 accessory proteins that suppress beta interferon production.
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pubmed:affiliation |
Microbiology Section, Department of Pathological Sciences, Faculty of Medical Sciences, University of Fukui, 23-3 Shimoaizuki, Matsuoka, Yoshida-gun, Fukui 910-1193, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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