pubmed-article:18588927 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C0014047 | lld:lifeskim |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C0021747 | lld:lifeskim |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C0084378 | lld:lifeskim |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C1425699 | lld:lifeskim |
pubmed-article:18588927 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
pubmed-article:18588927 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:18588927 | pubmed:dateCreated | 2008-8-29 | lld:pubmed |
pubmed-article:18588927 | pubmed:abstractText | The interferon (IFN) antagonists of Japanese encephalitis virus (JEV) proteins contribute to the JE pathogenesis. Most flavivirus non-structural (NS) proteins correlate with virus-induced inflammation and immune escape. NS4A proteins of West Nile virus and dengue type 2 virus have been demonstrated to inhibit IFN signaling. In this study, JEV NS4A without the C-terminal 2K domain has been demonstrated to partially block activation of an IFN-stimulated response element (ISRE)-based cis-reporter by IFN-alpha/beta. In addition, JEV NS4A significantly inhibited the phosphorylation levels of STAT1 and STAT2, but not TYK2 in the IFN-treated cells. Moreover, the N-terminus of a RNA helicase DDX42 protein identified using a phage display human brain cDNA library have been demonstrated to specifically bind to JEV NS4A in vitro using a co-immunoprecipitation assay. The interaction between JEV NS4A and RNA helicase DDX42 showed partial co-localization in human medulloblastoma TE-671 cells by confocal microscopy. Importantly, the expression of N-terminal DDX42 is able to overcome JEV-induced antagonism of IFN responses. Therefore, these results show that JEV NS4A without the C-terminal 2K domain is associated with modulation of the IFN response and the interaction of JEV NS4A with RNA helicase DDX42 could be important for JE pathogenesis. | lld:pubmed |
pubmed-article:18588927 | pubmed:language | eng | lld:pubmed |
pubmed-article:18588927 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18588927 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18588927 | pubmed:month | Oct | lld:pubmed |
pubmed-article:18588927 | pubmed:issn | 0168-1702 | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:T'uS CSC | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:LinWei-YongWY | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:KaoMing-Ching... | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:LaiChih-HoCH | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:LinCheng-WenC... | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:YangTsuey-Chi... | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:LinYing-JuYJ | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:LiShih-WeinSW | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:ChengChieh-We... | lld:pubmed |
pubmed-article:18588927 | pubmed:author | pubmed-author:ChengMei-Hsiu... | lld:pubmed |
pubmed-article:18588927 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18588927 | pubmed:volume | 137 | lld:pubmed |
pubmed-article:18588927 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18588927 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18588927 | pubmed:pagination | 49-55 | lld:pubmed |
pubmed-article:18588927 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:18588927 | pubmed:meshHeading | pubmed-meshheading:18588927... | lld:pubmed |
pubmed-article:18588927 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18588927 | pubmed:articleTitle | Interferon antagonist function of Japanese encephalitis virus NS4A and its interaction with DEAD-box RNA helicase DDX42. | lld:pubmed |
pubmed-article:18588927 | pubmed:affiliation | Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan. cwlin@mail.cmu.edu.tw | lld:pubmed |
pubmed-article:18588927 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18588927 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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