Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2004-10-13
pubmed:abstractText
The NS1 proteins of influenza A and B viruses (A/NS1 and B/NS1 proteins) have only approximately 20% amino acid sequence identity. Nevertheless, these proteins show several functional similarities, such as their ability to bind to the same RNA targets and to inhibit the activation of protein kinase R in vitro. A critical function of the A/NS1 protein is the inhibition of synthesis of alpha/beta interferon (IFN-alpha/beta) during viral infection. Recently, it was also found that the B/NS1 protein inhibits IFN-alpha/beta synthesis in virus-infected cells. We have now found that the expression of the B/NS1 protein complements the growth of an influenza A virus with A/NS1 deleted. Expression of the full-length B/NS1 protein (281 amino acids), as well as either its N-terminal RNA-binding domain (amino acids 1 to 93) or C-terminal domain (amino acids 94 to 281), in the absence of any other influenza B virus proteins resulted in the inhibition of IRF-3 nuclear translocation and IFN-beta promoter activation. A mutational analysis of the truncated B/NS1(1-93) protein showed that RNA-binding activity correlated with IFN-beta promoter inhibition. In addition, a recombinant influenza B virus with NS1 deleted induces higher levels of IRF-3 activation, as determined by its nuclear translocation, and of IFN-alpha/beta synthesis than wild-type influenza B virus. Our results support the hypothesis that the NS1 protein of influenza B virus plays an important role in antagonizing the IRF-3- and IFN-induced antiviral host responses to virus infection.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-10024172, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-10205180, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-10725408, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-10920397, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-10933707, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-11027311, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-11090154, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-11157743, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-11421366, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12114540, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12368362, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12438621, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12502864, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12504570, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12517228, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12692549, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12702806, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-12915566, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-14645582, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-14747551, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-14967035, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-1660837, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-3811235, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-7958859, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-8139028, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-8207822, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-8313914, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-8806538, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9360601, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9360602, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9463386, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9541017, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9566918, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9651582, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9660935, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9865487, http://linkedlifedata.com/resource/pubmed/commentcorrection/15479798-9878611
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11574-82
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The N- and C-terminal domains of the NS1 protein of influenza B virus can independently inhibit IRF-3 and beta interferon promoter activation.
pubmed:affiliation
Department of Microbiology, Box 1124, Mount Sinai School of Medicine, 1 Gustave L. Levy Pl., New York, NY 10029, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't