The kinase activity of pseudorabies virus US3 is required for modulation of the actin cytoskeleton
Abstract Different viruses exploit the host cytoskeleton to facilitate replication and spread. The conserved US3 protein of the alphaherpesvirus pseudorabies virus induces actin stress fiber disassembly and formation of actin-containing cell projections, which are associated with enhanced intercellu...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2009-03, Vol.385 (1), p.155-160 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Van den Broeke, Céline Deruelle, Matthias Nauwynck, Hans J Coller, Kelly E Smith, Gregory A Van Doorsselaere, Jan Favoreel, Herman W |
| description | Abstract Different viruses exploit the host cytoskeleton to facilitate replication and spread. The conserved US3 protein of the alphaherpesvirus pseudorabies virus induces actin stress fiber disassembly and formation of actin-containing cell projections, which are associated with enhanced intercellular virus spread. Proteins of members of other virus families, notably vaccinia virus F11L protein and human immunodeficiency virus Nef protein, induce actin rearrangements that are very similar to those induced by US3. Interestingly, unlike F11L and Nef, the US3 protein displays serine/threonine kinase activity. Here, we report that the kinase activity of pseudorabies virus US3 is absolutely required for its actin modulating activity. These data show that different viruses have developed independent mechanisms to induce very similar actin rearrangements. |
| doi_str_mv | 10.1016/j.virol.2008.11.050 |
| format | Article |
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The conserved US3 protein of the alphaherpesvirus pseudorabies virus induces actin stress fiber disassembly and formation of actin-containing cell projections, which are associated with enhanced intercellular virus spread. Proteins of members of other virus families, notably vaccinia virus F11L protein and human immunodeficiency virus Nef protein, induce actin rearrangements that are very similar to those induced by US3. Interestingly, unlike F11L and Nef, the US3 protein displays serine/threonine kinase activity. Here, we report that the kinase activity of pseudorabies virus US3 is absolutely required for its actin modulating activity. These data show that different viruses have developed independent mechanisms to induce very similar actin rearrangements.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2008.11.050</identifier><identifier>PMID: 19136132</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actin ; Actins - metabolism ; Alphaherpesvirus ; Animals ; Cell Line ; Cell projections ; Cytoskeleton - enzymology ; Cytoskeleton - metabolism ; Herpesvirus ; Herpesvirus 1, Suid - enzymology ; Herpesvirus 1, Suid - genetics ; Human immunodeficiency virus ; Infectious Disease ; Kinase activity ; Mice ; Protein-Serine-Threonine Kinases - metabolism ; Pseudorabies - pathology ; Pseudorabies virus ; Stress fibers ; US3 ; Vaccinia virus ; Viral Proteins - metabolism</subject><ispartof>Virology (New York, N.Y.), 2009-03, Vol.385 (1), p.155-160</ispartof><rights>Elsevier Inc.</rights><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-a6657b2cae7ae21528161a56b6d394e728048c23e6cffed2da72ee8ccef055b33</citedby><cites>FETCH-LOGICAL-c443t-a6657b2cae7ae21528161a56b6d394e728048c23e6cffed2da72ee8ccef055b33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0042682208007885$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19136132$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van den Broeke, Céline</creatorcontrib><creatorcontrib>Deruelle, Matthias</creatorcontrib><creatorcontrib>Nauwynck, Hans J</creatorcontrib><creatorcontrib>Coller, Kelly E</creatorcontrib><creatorcontrib>Smith, Gregory A</creatorcontrib><creatorcontrib>Van Doorsselaere, Jan</creatorcontrib><creatorcontrib>Favoreel, Herman W</creatorcontrib><title>The kinase activity of pseudorabies virus US3 is required for modulation of the actin cytoskeleton</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract Different viruses exploit the host cytoskeleton to facilitate replication and spread. The conserved US3 protein of the alphaherpesvirus pseudorabies virus induces actin stress fiber disassembly and formation of actin-containing cell projections, which are associated with enhanced intercellular virus spread. Proteins of members of other virus families, notably vaccinia virus F11L protein and human immunodeficiency virus Nef protein, induce actin rearrangements that are very similar to those induced by US3. Interestingly, unlike F11L and Nef, the US3 protein displays serine/threonine kinase activity. Here, we report that the kinase activity of pseudorabies virus US3 is absolutely required for its actin modulating activity. These data show that different viruses have developed independent mechanisms to induce very similar actin rearrangements.</description><subject>Actin</subject><subject>Actins - metabolism</subject><subject>Alphaherpesvirus</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cell projections</subject><subject>Cytoskeleton - enzymology</subject><subject>Cytoskeleton - metabolism</subject><subject>Herpesvirus</subject><subject>Herpesvirus 1, Suid - enzymology</subject><subject>Herpesvirus 1, Suid - genetics</subject><subject>Human immunodeficiency virus</subject><subject>Infectious Disease</subject><subject>Kinase activity</subject><subject>Mice</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Pseudorabies - pathology</subject><subject>Pseudorabies virus</subject><subject>Stress fibers</subject><subject>US3</subject><subject>Vaccinia virus</subject><subject>Viral Proteins - metabolism</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFr3DAQhUVpSbZpf0Gh6NSb3ZFkS9pDCyU0aSHQQ5KzkKUx0a7X2kj2wv77ytmFQi85DQPfewPvDSGfGNQMmPy6qQ8hxaHmALpmrIYW3pAVg7WsQDTsLVkBNLySmvNL8j7nDZRdKbggl2zNhGSCr0j38IR0G0abkVo3hUOYjjT2dJ9x9jHZLmCm5c6c6eO9oCHThM9zSOhpHxPdRT8PdgpxXETT08lkpO44xbzFAac4fiDvejtk_HieV-Tx5ufD9a_q7s_t7-sfd5VrGjFVVspWddxZVBY5a7lmktlWdtKLdYOKa2i04wKl63v03FvFEbVz2EPbdkJckS8n332KzzPmyexCdjgMdsQ4ZyPlutVSvA5yEIpLoQooTqBLMeeEvdmnsLPpaBiYpQOzMS8dmKUDw5gpHRTV57P93O3Q_9OcQy_AtxOAJY1DwGSyCzg69CVXNxkfwysHvv-nd0MYg7PDFo-YN3FOYwnaMJO5AXO_vMHyBaABlNat-AszFa8W</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Van den Broeke, Céline</creator><creator>Deruelle, Matthias</creator><creator>Nauwynck, Hans J</creator><creator>Coller, Kelly E</creator><creator>Smith, Gregory A</creator><creator>Van Doorsselaere, Jan</creator><creator>Favoreel, Herman W</creator><general>Elsevier Inc</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20090301</creationdate><title>The kinase activity of pseudorabies virus US3 is required for modulation of the actin cytoskeleton</title><author>Van den Broeke, Céline ; Deruelle, Matthias ; Nauwynck, Hans J ; Coller, Kelly E ; Smith, Gregory A ; Van Doorsselaere, Jan ; Favoreel, Herman W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-a6657b2cae7ae21528161a56b6d394e728048c23e6cffed2da72ee8ccef055b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Actin</topic><topic>Actins - metabolism</topic><topic>Alphaherpesvirus</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Cell projections</topic><topic>Cytoskeleton - enzymology</topic><topic>Cytoskeleton - metabolism</topic><topic>Herpesvirus</topic><topic>Herpesvirus 1, Suid - enzymology</topic><topic>Herpesvirus 1, Suid - genetics</topic><topic>Human immunodeficiency virus</topic><topic>Infectious Disease</topic><topic>Kinase activity</topic><topic>Mice</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Pseudorabies - pathology</topic><topic>Pseudorabies virus</topic><topic>Stress fibers</topic><topic>US3</topic><topic>Vaccinia virus</topic><topic>Viral Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van den Broeke, Céline</creatorcontrib><creatorcontrib>Deruelle, Matthias</creatorcontrib><creatorcontrib>Nauwynck, Hans J</creatorcontrib><creatorcontrib>Coller, Kelly E</creatorcontrib><creatorcontrib>Smith, Gregory A</creatorcontrib><creatorcontrib>Van Doorsselaere, Jan</creatorcontrib><creatorcontrib>Favoreel, Herman W</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>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van den Broeke, Céline</au><au>Deruelle, Matthias</au><au>Nauwynck, Hans J</au><au>Coller, Kelly E</au><au>Smith, Gregory A</au><au>Van Doorsselaere, Jan</au><au>Favoreel, Herman W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The kinase activity of pseudorabies virus US3 is required for modulation of the actin cytoskeleton</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>385</volume><issue>1</issue><spage>155</spage><epage>160</epage><pages>155-160</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract Different viruses exploit the host cytoskeleton to facilitate replication and spread. The conserved US3 protein of the alphaherpesvirus pseudorabies virus induces actin stress fiber disassembly and formation of actin-containing cell projections, which are associated with enhanced intercellular virus spread. Proteins of members of other virus families, notably vaccinia virus F11L protein and human immunodeficiency virus Nef protein, induce actin rearrangements that are very similar to those induced by US3. Interestingly, unlike F11L and Nef, the US3 protein displays serine/threonine kinase activity. Here, we report that the kinase activity of pseudorabies virus US3 is absolutely required for its actin modulating activity. These data show that different viruses have developed independent mechanisms to induce very similar actin rearrangements.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19136132</pmid><doi>10.1016/j.virol.2008.11.050</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Actin Actins - metabolism Alphaherpesvirus Animals Cell Line Cell projections Cytoskeleton - enzymology Cytoskeleton - metabolism Herpesvirus Herpesvirus 1, Suid - enzymology Herpesvirus 1, Suid - genetics Human immunodeficiency virus Infectious Disease Kinase activity Mice Protein-Serine-Threonine Kinases - metabolism Pseudorabies - pathology Pseudorabies virus Stress fibers US3 Vaccinia virus Viral Proteins - metabolism |
| title | The kinase activity of pseudorabies virus US3 is required for modulation of the actin cytoskeleton |
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