The ribonuclease l-dependent antiviral roles of human 2′,5′-oligoadenylate synthetase family members against hepatitis C virus
► Expression of the ribonuclease RNase L inhibited HCV replication in Huh7 cells. ► Ectopic expression of the OAS1 p46 and OAS3 p100 activated the RNase L. ► OAS1 p46 was not expressed in Huh7 cells due to an SNP. The latent ribonuclease RNase L and the interferon-inducible 2′,5′-oligoadenylate synt...
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| Veröffentlicht in: | FEBS letters 2013-01, Vol.587 (2), p.156-164 |
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| creator | Kwon, Young-Chan Kang, Ju-Il Hwang, Soon B. Ahn, Byung-Yoon |
| description | ► Expression of the ribonuclease RNase L inhibited HCV replication in Huh7 cells. ► Ectopic expression of the OAS1 p46 and OAS3 p100 activated the RNase L. ► OAS1 p46 was not expressed in Huh7 cells due to an SNP.
The latent ribonuclease RNase L and the interferon-inducible 2′,5′-oligoadenylate synthetase (OAS) have been implicated in the antiviral response against hepatitis C virus (HCV). However, the specific roles of these enzymes against HCV have not been fully elucidated. In this study, a scarce endogenous expression and RNA degrading activity of RNase L in human hepatoma Huh7 cells enabled us to demonstrate the antiviral activity of RNase L against HCV replication through the transient expression of the enzyme. The antiviral potential of specific members of the OAS family was further examined through overexpression and RNA interference approaches. Our data suggested that among the members of the OAS family, OAS1 p46 and OAS3 p100 mediate the RNase l-dependent antiviral activity against HCV. |
| doi_str_mv | 10.1016/j.febslet.2012.11.010 |
| format | Article |
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The latent ribonuclease RNase L and the interferon-inducible 2′,5′-oligoadenylate synthetase (OAS) have been implicated in the antiviral response against hepatitis C virus (HCV). However, the specific roles of these enzymes against HCV have not been fully elucidated. In this study, a scarce endogenous expression and RNA degrading activity of RNase L in human hepatoma Huh7 cells enabled us to demonstrate the antiviral activity of RNase L against HCV replication through the transient expression of the enzyme. The antiviral potential of specific members of the OAS family was further examined through overexpression and RNA interference approaches. Our data suggested that among the members of the OAS family, OAS1 p46 and OAS3 p100 mediate the RNase l-dependent antiviral activity against HCV.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2012.11.010</identifier><identifier>PMID: 23196181</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>2',5'-Oligoadenylate Synthetase - antagonists & inhibitors ; 2',5'-Oligoadenylate Synthetase - genetics ; 2',5'-Oligoadenylate Synthetase - metabolism ; 2′,5′-Oligoadenylate synthetase ; Antiviral Agents - pharmacology ; Antiviral protein ; Carcinoma, Hepatocellular - enzymology ; Carcinoma, Hepatocellular - genetics ; Carcinoma, Hepatocellular - virology ; Cell Line, Tumor ; Endoribonucleases - genetics ; Endoribonucleases - metabolism ; Hepacivirus - drug effects ; Hepacivirus - genetics ; Hepacivirus - pathogenicity ; Hepacivirus - physiology ; Hepatitis C virus ; Host-Pathogen Interactions ; Humans ; Liver Neoplasms - enzymology ; Liver Neoplasms - genetics ; Liver Neoplasms - virology ; RNA Interference ; RNase L ; Viral Nonstructural Proteins - metabolism ; Virus Replication - drug effects ; Virus Replication - physiology</subject><ispartof>FEBS letters, 2013-01, Vol.587 (2), p.156-164</ispartof><rights>2012 Federation of European Biochemical Societies</rights><rights>FEBS Letters 587 (2013) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5761-fb2e72c92815baa44efc3711188ae583a35b2f85b3d7ab384b8b904d692390923</citedby><cites>FETCH-LOGICAL-c5761-fb2e72c92815baa44efc3711188ae583a35b2f85b3d7ab384b8b904d692390923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2012.11.010$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2012.11.010$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,1414,1430,3539,27907,27908,45557,45558,45978,46392,46816</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23196181$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kwon, Young-Chan</creatorcontrib><creatorcontrib>Kang, Ju-Il</creatorcontrib><creatorcontrib>Hwang, Soon B.</creatorcontrib><creatorcontrib>Ahn, Byung-Yoon</creatorcontrib><title>The ribonuclease l-dependent antiviral roles of human 2′,5′-oligoadenylate synthetase family members against hepatitis C virus</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>► Expression of the ribonuclease RNase L inhibited HCV replication in Huh7 cells. ► Ectopic expression of the OAS1 p46 and OAS3 p100 activated the RNase L. ► OAS1 p46 was not expressed in Huh7 cells due to an SNP.
The latent ribonuclease RNase L and the interferon-inducible 2′,5′-oligoadenylate synthetase (OAS) have been implicated in the antiviral response against hepatitis C virus (HCV). However, the specific roles of these enzymes against HCV have not been fully elucidated. In this study, a scarce endogenous expression and RNA degrading activity of RNase L in human hepatoma Huh7 cells enabled us to demonstrate the antiviral activity of RNase L against HCV replication through the transient expression of the enzyme. The antiviral potential of specific members of the OAS family was further examined through overexpression and RNA interference approaches. Our data suggested that among the members of the OAS family, OAS1 p46 and OAS3 p100 mediate the RNase l-dependent antiviral activity against HCV.</description><subject>2',5'-Oligoadenylate Synthetase - antagonists & inhibitors</subject><subject>2',5'-Oligoadenylate Synthetase - genetics</subject><subject>2',5'-Oligoadenylate Synthetase - metabolism</subject><subject>2′,5′-Oligoadenylate synthetase</subject><subject>Antiviral Agents - pharmacology</subject><subject>Antiviral protein</subject><subject>Carcinoma, Hepatocellular - enzymology</subject><subject>Carcinoma, Hepatocellular - genetics</subject><subject>Carcinoma, Hepatocellular - virology</subject><subject>Cell Line, Tumor</subject><subject>Endoribonucleases - genetics</subject><subject>Endoribonucleases - metabolism</subject><subject>Hepacivirus - drug effects</subject><subject>Hepacivirus - genetics</subject><subject>Hepacivirus - pathogenicity</subject><subject>Hepacivirus - physiology</subject><subject>Hepatitis C virus</subject><subject>Host-Pathogen Interactions</subject><subject>Humans</subject><subject>Liver Neoplasms - enzymology</subject><subject>Liver Neoplasms - genetics</subject><subject>Liver Neoplasms - virology</subject><subject>RNA Interference</subject><subject>RNase L</subject><subject>Viral Nonstructural Proteins - metabolism</subject><subject>Virus Replication - drug effects</subject><subject>Virus Replication - physiology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhiMEokvhEUA-ciDBY8eJc0J01VKkShwoZ8tOJl2vnGSxnaLcEI_UR-qT4GgXrnAZ29I_31jfZNlroAVQqN7vix5NcBgLRoEVAAUF-iTbgKx5zstKPs02lEKZi7rhZ9mLEPY0vSU0z7MzxqGp0n2T_brdIfHWTOPcOtQBics7PODY4RiJHqO9t1474ieHgUw92c2DHgl7_PnwTqSST87eTTqlF6cjkrCMcYdxBfV6sG4hAw4GfSD6TtsxRLLDg4422kC2JLHn8DJ71msX8NXpPM--XV3ebq_zmy-fPm8_3uStqCvIe8OwZm3DJAijdVli3_IaAKTUKCTXXBjWS2F4V2vDZWmkaWjZVQ3jDU3lPHt75B789H3GENVgQ4vO6RGnOShgUiS1TSlSVByjrZ9C8Nirg7eD9osCqlb9aq9O-tWqXwGopD_1vTmNmM2A3d-uP75T4PoY-GEdLv9HVVeXF-zrust1lcAolVWzoj4cUZic3Vv0KrQWxxY767GNqpvsP377G_rqsd8</recordid><startdate>20130116</startdate><enddate>20130116</enddate><creator>Kwon, Young-Chan</creator><creator>Kang, Ju-Il</creator><creator>Hwang, Soon B.</creator><creator>Ahn, Byung-Yoon</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>20130116</creationdate><title>The ribonuclease l-dependent antiviral roles of human 2′,5′-oligoadenylate synthetase family members against hepatitis C virus</title><author>Kwon, Young-Chan ; Kang, Ju-Il ; Hwang, Soon B. ; Ahn, Byung-Yoon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5761-fb2e72c92815baa44efc3711188ae583a35b2f85b3d7ab384b8b904d692390923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>2',5'-Oligoadenylate Synthetase - antagonists & inhibitors</topic><topic>2',5'-Oligoadenylate Synthetase - genetics</topic><topic>2',5'-Oligoadenylate Synthetase - metabolism</topic><topic>2′,5′-Oligoadenylate synthetase</topic><topic>Antiviral Agents - pharmacology</topic><topic>Antiviral protein</topic><topic>Carcinoma, Hepatocellular - enzymology</topic><topic>Carcinoma, Hepatocellular - genetics</topic><topic>Carcinoma, Hepatocellular - virology</topic><topic>Cell Line, Tumor</topic><topic>Endoribonucleases - genetics</topic><topic>Endoribonucleases - metabolism</topic><topic>Hepacivirus - drug effects</topic><topic>Hepacivirus - genetics</topic><topic>Hepacivirus - pathogenicity</topic><topic>Hepacivirus - physiology</topic><topic>Hepatitis C virus</topic><topic>Host-Pathogen Interactions</topic><topic>Humans</topic><topic>Liver Neoplasms - enzymology</topic><topic>Liver Neoplasms - genetics</topic><topic>Liver Neoplasms - virology</topic><topic>RNA Interference</topic><topic>RNase L</topic><topic>Viral Nonstructural Proteins - metabolism</topic><topic>Virus Replication - drug effects</topic><topic>Virus Replication - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kwon, Young-Chan</creatorcontrib><creatorcontrib>Kang, Ju-Il</creatorcontrib><creatorcontrib>Hwang, Soon B.</creatorcontrib><creatorcontrib>Ahn, Byung-Yoon</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kwon, Young-Chan</au><au>Kang, Ju-Il</au><au>Hwang, Soon B.</au><au>Ahn, Byung-Yoon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ribonuclease l-dependent antiviral roles of human 2′,5′-oligoadenylate synthetase family members against hepatitis C virus</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2013-01-16</date><risdate>2013</risdate><volume>587</volume><issue>2</issue><spage>156</spage><epage>164</epage><pages>156-164</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>► Expression of the ribonuclease RNase L inhibited HCV replication in Huh7 cells. ► Ectopic expression of the OAS1 p46 and OAS3 p100 activated the RNase L. ► OAS1 p46 was not expressed in Huh7 cells due to an SNP.
The latent ribonuclease RNase L and the interferon-inducible 2′,5′-oligoadenylate synthetase (OAS) have been implicated in the antiviral response against hepatitis C virus (HCV). However, the specific roles of these enzymes against HCV have not been fully elucidated. In this study, a scarce endogenous expression and RNA degrading activity of RNase L in human hepatoma Huh7 cells enabled us to demonstrate the antiviral activity of RNase L against HCV replication through the transient expression of the enzyme. The antiviral potential of specific members of the OAS family was further examined through overexpression and RNA interference approaches. Our data suggested that among the members of the OAS family, OAS1 p46 and OAS3 p100 mediate the RNase l-dependent antiviral activity against HCV.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>23196181</pmid><doi>10.1016/j.febslet.2012.11.010</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; ScienceDirect Journals (5 years ago - present); Alma/SFX Local Collection |
| subjects | 2',5'-Oligoadenylate Synthetase - antagonists & inhibitors 2',5'-Oligoadenylate Synthetase - genetics 2',5'-Oligoadenylate Synthetase - metabolism 2′,5′-Oligoadenylate synthetase Antiviral Agents - pharmacology Antiviral protein Carcinoma, Hepatocellular - enzymology Carcinoma, Hepatocellular - genetics Carcinoma, Hepatocellular - virology Cell Line, Tumor Endoribonucleases - genetics Endoribonucleases - metabolism Hepacivirus - drug effects Hepacivirus - genetics Hepacivirus - pathogenicity Hepacivirus - physiology Hepatitis C virus Host-Pathogen Interactions Humans Liver Neoplasms - enzymology Liver Neoplasms - genetics Liver Neoplasms - virology RNA Interference RNase L Viral Nonstructural Proteins - metabolism Virus Replication - drug effects Virus Replication - physiology |
| title | The ribonuclease l-dependent antiviral roles of human 2′,5′-oligoadenylate synthetase family members against hepatitis C virus |
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