Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR)
Bovine viral diarrhea virus (BVDV) is a positive-sense RNA virus known to produce double-stranded RNA (dsRNA) during its replication in the cytoplasm. Extended dsRNA duplexes can be hyperedited by adenosine deaminase acting on RNA (ADAR), which catalyzes adenosine (A)-to-inosine (I) editing. A-to-I...
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| Veröffentlicht in: | Archives of virology 2014-07, Vol.159 (7), p.1735-1741 |
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| creator | Mohamed, Yassir Mahgoub Bangphoomi, Norasuthi Yamane, Daisuke Suda, Yuto Kato, Kentaro Horimoto, Taisuke Akashi, Hiroomi |
| description | Bovine viral diarrhea virus (BVDV) is a positive-sense RNA virus known to produce double-stranded RNA (dsRNA) during its replication in the cytoplasm. Extended dsRNA duplexes can be hyperedited by adenosine deaminase acting on RNA (ADAR), which catalyzes adenosine (A)-to-inosine (I) editing. A-to-I editing has been reported for various viruses. A number of cellular antiviral defense strategies are stimulated by dsRNA, and this may involve hyperediting of dsRNA by ADARs, followed by targeted cleavage by cytoplasmic endonucleases. Here, we identify ADAR as a binding partner of BVDV NS4A in vitro and in vivo and show that the N-terminal domain of NS4A is the ADAR-binding domain. We also show that ADAR has an inhibitory effect on BVDV replication when overexpressed in BVDV-infected bovine cells. Our findings suggest a role of NS4A in the interaction of BVDV with ADAR that favors virus replication. |
| doi_str_mv | 10.1007/s00705-014-1997-3 |
| format | Article |
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Extended dsRNA duplexes can be hyperedited by adenosine deaminase acting on RNA (ADAR), which catalyzes adenosine (A)-to-inosine (I) editing. A-to-I editing has been reported for various viruses. A number of cellular antiviral defense strategies are stimulated by dsRNA, and this may involve hyperediting of dsRNA by ADARs, followed by targeted cleavage by cytoplasmic endonucleases. Here, we identify ADAR as a binding partner of BVDV NS4A in vitro and in vivo and show that the N-terminal domain of NS4A is the ADAR-binding domain. We also show that ADAR has an inhibitory effect on BVDV replication when overexpressed in BVDV-infected bovine cells. Our findings suggest a role of NS4A in the interaction of BVDV with ADAR that favors virus replication.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-014-1997-3</identifier><identifier>PMID: 24500065</identifier><language>eng</language><publisher>Vienna: Springer-Verlag</publisher><subject>Adenosine ; adenosine deaminase ; Adenosine Deaminase - genetics ; Adenosine Deaminase - metabolism ; Animals ; Biomedical and Life Sciences ; Biomedicine ; Bovine viral diarrhea virus ; Cattle ; Cell culture ; Cell Line ; Cloning ; cytoplasm ; Diarrhea ; Diarrhea Viruses, Bovine Viral - genetics ; Diarrhea Viruses, Bovine Viral - metabolism ; double-stranded RNA ; Editing ; Gene Expression Regulation, Viral ; Genomes ; Infectious Diseases ; Medical Microbiology ; Monoclonal antibodies ; Original Article ; Protein Binding ; Protein Structure, Tertiary ; RNA, Double-Stranded - metabolism ; RNA, Viral - metabolism ; RNA-Binding Proteins ; Two-Hybrid System Techniques ; Viral Nonstructural Proteins - genetics ; Viral Nonstructural Proteins - metabolism ; Virology ; virus replication ; Virus Replication - physiology ; Viruses</subject><ispartof>Archives of virology, 2014-07, Vol.159 (7), p.1735-1741</ispartof><rights>Springer-Verlag Wien 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c565t-8237fddc5d71c1f6f4d5db879b4a71f11e95297d15250d89d51439269e4ef7353</citedby><cites>FETCH-LOGICAL-c565t-8237fddc5d71c1f6f4d5db879b4a71f11e95297d15250d89d51439269e4ef7353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00705-014-1997-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00705-014-1997-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24500065$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mohamed, Yassir Mahgoub</creatorcontrib><creatorcontrib>Bangphoomi, Norasuthi</creatorcontrib><creatorcontrib>Yamane, Daisuke</creatorcontrib><creatorcontrib>Suda, Yuto</creatorcontrib><creatorcontrib>Kato, Kentaro</creatorcontrib><creatorcontrib>Horimoto, Taisuke</creatorcontrib><creatorcontrib>Akashi, Hiroomi</creatorcontrib><title>Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR)</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><addtitle>Arch Virol</addtitle><description>Bovine viral diarrhea virus (BVDV) is a positive-sense RNA virus known to produce double-stranded RNA (dsRNA) during its replication in the cytoplasm. 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Our findings suggest a role of NS4A in the interaction of BVDV with ADAR that favors virus replication.</description><subject>Adenosine</subject><subject>adenosine deaminase</subject><subject>Adenosine Deaminase - genetics</subject><subject>Adenosine Deaminase - metabolism</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bovine viral diarrhea virus</subject><subject>Cattle</subject><subject>Cell culture</subject><subject>Cell Line</subject><subject>Cloning</subject><subject>cytoplasm</subject><subject>Diarrhea</subject><subject>Diarrhea Viruses, Bovine Viral - genetics</subject><subject>Diarrhea Viruses, Bovine Viral - metabolism</subject><subject>double-stranded RNA</subject><subject>Editing</subject><subject>Gene Expression Regulation, Viral</subject><subject>Genomes</subject><subject>Infectious Diseases</subject><subject>Medical Microbiology</subject><subject>Monoclonal antibodies</subject><subject>Original Article</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>RNA, Double-Stranded - metabolism</subject><subject>RNA, Viral - metabolism</subject><subject>RNA-Binding Proteins</subject><subject>Two-Hybrid System Techniques</subject><subject>Viral Nonstructural Proteins - genetics</subject><subject>Viral Nonstructural Proteins - metabolism</subject><subject>Virology</subject><subject>virus replication</subject><subject>Virus Replication - physiology</subject><subject>Viruses</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkU9v1DAQxS0EotvCB-AClriUQ8DjP3F8jAqFShWgQs-WN55sXe06rZ0U9dLPXkcpFeKAuHhkz-89e_wIeQXsPTCmP-SyMFUxkBUYoyvxhKxACl412jRPyYoJJqumZs0e2c_5krFyINRzsselKptarcjd94vbHDq3pSGOmFw3hiHSNY6_EEsdbkJEehNSAXxwKV2gm7dTpnGIeUxTN05z8yoNI4ZIZUtd9NR5jEOetR7dLkSXkc7ecUOL_dnXlh62H9uzdy_Is95tM758qAfk_PjTz6Mv1em3zydH7WnVqVqNVcOF7r3vlNfQQV_30iu_LlOupdPQA6BR3GgPiivmG-NV-QbDa4MSey2UOCCHi2955_WEebS7kDvcbl3EYcoWlJJGygaa_0AlCK2U4QV9-xd6OUwplkFmiikONYhCwUJ1acg5YW-vUti5dGuB2TlHu-RoS452ztHOmtcPztN6h_5R8Tu4AvAFyKUVN5j-uPofrm8WUe8G6zYpZHv-gxeAMRBKGxD3AkmwLw</recordid><startdate>20140701</startdate><enddate>20140701</enddate><creator>Mohamed, Yassir Mahgoub</creator><creator>Bangphoomi, Norasuthi</creator><creator>Yamane, Daisuke</creator><creator>Suda, Yuto</creator><creator>Kato, Kentaro</creator><creator>Horimoto, Taisuke</creator><creator>Akashi, Hiroomi</creator><general>Springer-Verlag</general><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>FBQ</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>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20140701</creationdate><title>Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR)</title><author>Mohamed, Yassir Mahgoub ; Bangphoomi, Norasuthi ; Yamane, Daisuke ; Suda, Yuto ; Kato, Kentaro ; Horimoto, Taisuke ; Akashi, Hiroomi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c565t-8237fddc5d71c1f6f4d5db879b4a71f11e95297d15250d89d51439269e4ef7353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Adenosine</topic><topic>adenosine deaminase</topic><topic>Adenosine Deaminase - genetics</topic><topic>Adenosine Deaminase - metabolism</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bovine viral diarrhea virus</topic><topic>Cattle</topic><topic>Cell culture</topic><topic>Cell Line</topic><topic>Cloning</topic><topic>cytoplasm</topic><topic>Diarrhea</topic><topic>Diarrhea Viruses, Bovine Viral - genetics</topic><topic>Diarrhea Viruses, Bovine Viral - metabolism</topic><topic>double-stranded RNA</topic><topic>Editing</topic><topic>Gene Expression Regulation, Viral</topic><topic>Genomes</topic><topic>Infectious Diseases</topic><topic>Medical Microbiology</topic><topic>Monoclonal antibodies</topic><topic>Original Article</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>RNA, Double-Stranded - metabolism</topic><topic>RNA, Viral - metabolism</topic><topic>RNA-Binding Proteins</topic><topic>Two-Hybrid System Techniques</topic><topic>Viral Nonstructural Proteins - genetics</topic><topic>Viral Nonstructural Proteins - 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Extended dsRNA duplexes can be hyperedited by adenosine deaminase acting on RNA (ADAR), which catalyzes adenosine (A)-to-inosine (I) editing. A-to-I editing has been reported for various viruses. A number of cellular antiviral defense strategies are stimulated by dsRNA, and this may involve hyperediting of dsRNA by ADARs, followed by targeted cleavage by cytoplasmic endonucleases. Here, we identify ADAR as a binding partner of BVDV NS4A in vitro and in vivo and show that the N-terminal domain of NS4A is the ADAR-binding domain. We also show that ADAR has an inhibitory effect on BVDV replication when overexpressed in BVDV-infected bovine cells. Our findings suggest a role of NS4A in the interaction of BVDV with ADAR that favors virus replication.</abstract><cop>Vienna</cop><pub>Springer-Verlag</pub><pmid>24500065</pmid><doi>10.1007/s00705-014-1997-3</doi><tpages>7</tpages></addata></record> |
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| subjects | Adenosine adenosine deaminase Adenosine Deaminase - genetics Adenosine Deaminase - metabolism Animals Biomedical and Life Sciences Biomedicine Bovine viral diarrhea virus Cattle Cell culture Cell Line Cloning cytoplasm Diarrhea Diarrhea Viruses, Bovine Viral - genetics Diarrhea Viruses, Bovine Viral - metabolism double-stranded RNA Editing Gene Expression Regulation, Viral Genomes Infectious Diseases Medical Microbiology Monoclonal antibodies Original Article Protein Binding Protein Structure, Tertiary RNA, Double-Stranded - metabolism RNA, Viral - metabolism RNA-Binding Proteins Two-Hybrid System Techniques Viral Nonstructural Proteins - genetics Viral Nonstructural Proteins - metabolism Virology virus replication Virus Replication - physiology Viruses |
| title | Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR) |
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