| pubmed-article:15039538 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15039538 | lifeskim:mentions | umls-concept:C0003451 | lld:lifeskim |
| pubmed-article:15039538 | lifeskim:mentions | umls-concept:C0000189 | lld:lifeskim |
| pubmed-article:15039538 | lifeskim:mentions | umls-concept:C0021747 | lld:lifeskim |
| pubmed-article:15039538 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15039538 | lifeskim:mentions | umls-concept:C1415900 | lld:lifeskim |
| pubmed-article:15039538 | lifeskim:mentions | umls-concept:C1569072 | lld:lifeskim |
| pubmed-article:15039538 | pubmed:issue | Pt 4 | lld:pubmed |
| pubmed-article:15039538 | pubmed:dateCreated | 2004-3-24 | lld:pubmed |
| pubmed-article:15039538 | pubmed:abstractText | The non-structural protein 5A (NS5A) of hepatitis C virus (HCV) has been implicated in inhibition of antiviral activity of IFN. While previous studies have suggested an interaction between NS5A and the double-stranded RNA-dependent protein kinase (PKR), the possibility still remains that interaction with another molecule(s) is involved in the NS5A-mediated inhibition of IFN. In the present study, we investigated a possible interaction between NS5A and 2',5'-oligoadenylate synthetase (2-5AS), another key molecule in antiviral activity. We observed that NS5A physically interacted with 2-5AS in cultured cells, with an N-terminal portion of NS5A [aa 1-148; NS5A(1-148)] and two separate portions of 2-5AS (aa 52-104 and 184-275) being involved in the interaction. Single point mutations at residue 37 of NS5A affected the degree of the interaction with 2-5AS, with a Phe-to-Leu mutation (F37L) augmenting and a Phe-to-Asn mutation (F37N) diminishing it. Virus rescue assay revealed that the full-length NS5A (NS5A-F) and NS5A(1-148), the latter of which contains neither the IFN sensitivity-determining region (ISDR) nor the PKR-binding domain, significantly counteracted the antiviral activity of IFN. Introduction of a F37N mutation into NS5A(1-148) impaired the otherwise more significant IFN-inhibitory activity of NS5A(1-148). It was also found that the F37N mutation was highly disadvantageous for the replication of an HCV RNA replicon. Taken together, our results suggest the possibility that NS5A interacts with 2-5AS and inhibits the antiviral activity of IFN in an ISDR-independent manner. | lld:pubmed |
| pubmed-article:15039538 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15039538 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15039538 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15039538 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15039538 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15039538 | pubmed:issn | 0022-1317 | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:TaguchiTakash... | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:IshidoSatoshi... | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:HottaHakH | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:Nagano-FujiiM... | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:OhgimotoShinj... | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:AkutsuMasatoM | lld:pubmed |
| pubmed-article:15039538 | pubmed:author | pubmed-author:KadoyaHiroyas... | lld:pubmed |
| pubmed-article:15039538 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15039538 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:15039538 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15039538 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15039538 | pubmed:pagination | 959-69 | lld:pubmed |
| pubmed-article:15039538 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15039538 | pubmed:meshHeading | pubmed-meshheading:15039538... | lld:pubmed |
| pubmed-article:15039538 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15039538 | pubmed:articleTitle | Hepatitis C virus NS5A protein interacts with 2',5'-oligoadenylate synthetase and inhibits antiviral activity of IFN in an IFN sensitivity-determining region-independent manner. | lld:pubmed |
| pubmed-article:15039538 | pubmed:affiliation | Division of Microbiology, Kobe University Graduate School of Medicine, Kobe 650-0017, Japan. | lld:pubmed |
| pubmed-article:15039538 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15039538 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:246730 | entrezgene:pubmed | pubmed-article:15039538 | lld:entrezgene |
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