Smurf2 alters BPV1 trafficking and decreases infection
Papillomavirus capsid proteins L1 and L2 mediate virion attachment, internalization and trafficking. In our studies of the capsid proteins, we identified an interaction of L2 with the E3 ligase Smad ubiquitin regulatory factor 2 (Smurf2). Smurf2 expression alters BPV1 virion trafficking and L2 prote...
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description | Papillomavirus capsid proteins L1 and L2 mediate virion attachment, internalization and trafficking. In our studies of the capsid proteins, we identified an interaction of L2 with the E3 ligase Smad ubiquitin regulatory factor 2 (Smurf2). Smurf2 expression alters BPV1 virion trafficking and L2 protein levels. Using BPV1 pseudovirions (PSVs) containing a GFP or DSRed transgene encapsidated by L1 and L2 proteins, our data showed that although only BPV1 L2 interacts with Smurf2, both L1 and L2 levels decrease in a Smurf2- and ubiquitin-dependent manner. The decrease in L2 protein levels corresponded to a decrease in infection (i.e., loss of GFP or DSRed expression). We propose that Smurf2 regulates L2 protein cellular localization and therefore alters L2 protein levels. This change in trafficking and protein level decreases nuclear delivery and transcription of encapsidated pseudoviral transgenes and thus decreases BPV1 infection levels. |
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In our studies of the capsid proteins, we identified an interaction of L2 with the E3 ligase Smad ubiquitin regulatory factor 2 (Smurf2). Smurf2 expression alters BPV1 virion trafficking and L2 protein levels. Using BPV1 pseudovirions (PSVs) containing a GFP or DSRed transgene encapsidated by L1 and L2 proteins, our data showed that although only BPV1 L2 interacts with Smurf2, both L1 and L2 levels decrease in a Smurf2- and ubiquitin-dependent manner. The decrease in L2 protein levels corresponded to a decrease in infection (i.e., loss of GFP or DSRed expression). We propose that Smurf2 regulates L2 protein cellular localization and therefore alters L2 protein levels. This change in trafficking and protein level decreases nuclear delivery and transcription of encapsidated pseudoviral transgenes and thus decreases BPV1 infection levels.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-011-0924-0</identifier><identifier>PMID: 21318310</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Animals ; Antibodies ; Biological and medical sciences ; Biomedical and Life Sciences ; Biomedicine ; Bovine papillomavirus 1 - immunology ; Bovine papillomavirus 1 - pathogenicity ; Capsid Proteins - metabolism ; Cell Line ; Cercopithecus aethiops ; Fundamental and applied biological sciences. 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In our studies of the capsid proteins, we identified an interaction of L2 with the E3 ligase Smad ubiquitin regulatory factor 2 (Smurf2). Smurf2 expression alters BPV1 virion trafficking and L2 protein levels. Using BPV1 pseudovirions (PSVs) containing a GFP or DSRed transgene encapsidated by L1 and L2 proteins, our data showed that although only BPV1 L2 interacts with Smurf2, both L1 and L2 levels decrease in a Smurf2- and ubiquitin-dependent manner. The decrease in L2 protein levels corresponded to a decrease in infection (i.e., loss of GFP or DSRed expression). We propose that Smurf2 regulates L2 protein cellular localization and therefore alters L2 protein levels. This change in trafficking and protein level decreases nuclear delivery and transcription of encapsidated pseudoviral transgenes and thus decreases BPV1 infection levels.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bovine papillomavirus 1 - immunology</subject><subject>Bovine papillomavirus 1 - pathogenicity</subject><subject>Capsid Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cercopithecus aethiops</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heparan sulfate</subject><subject>Humans</subject><subject>Infections</subject><subject>Infectious Diseases</subject><subject>Laboratories</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Original Article</subject><subject>Papillomavirus</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Ubiquitin-Protein Ligases - immunology</subject><subject>Virology</subject><subject>Virus Replication</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kU1LxDAQhoMo7rr6A7xIEUQv1ZmkadOjLn6BoKB4LWl2ItVuuybtwX9vSlcFQS8JJM88mXnD2D7CKQJkZz4sIGNAjCHnSQwbbIqJ4LHKcrXJpiAgiVUKasJ2vH8FCAdCbrMJR4FKIExZ-rjsneWRrjtyPrp4eMaoc9rayrxVzUukm0W0IONIe_JR1VgyXdU2u2zL6trT3nqfsaery6f5TXx3f307P7-LTSJEF2uQUmosS0WZtFhyo2wGNkckKVQuYSGUSkojQWclCVXmocKG5hLiSErM2PGoXbn2vSffFcvKG6pr3VDb-0KlIoyLCQTy5F8SgSvgIk0H9PAX-tr2rgljDD7gPAcZIBwh41rvHdli5aqldh_BVAzhF2P4RQi_GMIvBvHBWtyXS1p8V3ylHYCjNaC90bV1ujGV_-ESTNMsfOCM8ZHz4ap5IffT4d-vfwKU1ZhR</recordid><startdate>20110501</startdate><enddate>20110501</enddate><creator>Dabydeen, Sarah A.</creator><creator>Meneses, Patricio I.</creator><general>Springer Vienna</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</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>20110501</creationdate><title>Smurf2 alters BPV1 trafficking and decreases infection</title><author>Dabydeen, Sarah A. ; Meneses, Patricio I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-a0555a1bb8e75f1b2c8f70f911e538950d3884bc50a7be38b9a05f1314e21e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bovine papillomavirus 1 - immunology</topic><topic>Bovine papillomavirus 1 - pathogenicity</topic><topic>Capsid Proteins - metabolism</topic><topic>Cell Line</topic><topic>Cercopithecus aethiops</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heparan sulfate</topic><topic>Humans</topic><topic>Infections</topic><topic>Infectious Diseases</topic><topic>Laboratories</topic><topic>Medical Microbiology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Original Article</topic><topic>Papillomavirus</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Ubiquitin-Protein Ligases - immunology</topic><topic>Virology</topic><topic>Virus Replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dabydeen, Sarah A.</creatorcontrib><creatorcontrib>Meneses, Patricio I.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Biological Science Journals</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dabydeen, Sarah A.</au><au>Meneses, Patricio I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Smurf2 alters BPV1 trafficking and decreases infection</atitle><jtitle>Archives of virology</jtitle><stitle>Arch Virol</stitle><addtitle>Arch Virol</addtitle><date>2011-05-01</date><risdate>2011</risdate><volume>156</volume><issue>5</issue><spage>827</spage><epage>838</epage><pages>827-838</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>Papillomavirus capsid proteins L1 and L2 mediate virion attachment, internalization and trafficking. In our studies of the capsid proteins, we identified an interaction of L2 with the E3 ligase Smad ubiquitin regulatory factor 2 (Smurf2). Smurf2 expression alters BPV1 virion trafficking and L2 protein levels. Using BPV1 pseudovirions (PSVs) containing a GFP or DSRed transgene encapsidated by L1 and L2 proteins, our data showed that although only BPV1 L2 interacts with Smurf2, both L1 and L2 levels decrease in a Smurf2- and ubiquitin-dependent manner. The decrease in L2 protein levels corresponded to a decrease in infection (i.e., loss of GFP or DSRed expression). We propose that Smurf2 regulates L2 protein cellular localization and therefore alters L2 protein levels. This change in trafficking and protein level decreases nuclear delivery and transcription of encapsidated pseudoviral transgenes and thus decreases BPV1 infection levels.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>21318310</pmid><doi>10.1007/s00705-011-0924-0</doi><tpages>12</tpages></addata></record> |
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subjects | Animals Antibodies Biological and medical sciences Biomedical and Life Sciences Biomedicine Bovine papillomavirus 1 - immunology Bovine papillomavirus 1 - pathogenicity Capsid Proteins - metabolism Cell Line Cercopithecus aethiops Fundamental and applied biological sciences. Psychology Heparan sulfate Humans Infections Infectious Diseases Laboratories Medical Microbiology Microbiology Miscellaneous Original Article Papillomavirus Plasmids Proteins Ubiquitin-Protein Ligases - immunology Virology Virus Replication |
title | Smurf2 alters BPV1 trafficking and decreases infection |
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