Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation
Abstract The measles virus (MV) P gene encodes three proteins: P, an essential polymerase cofactor, and C and V, which have multiple functions including immune evasion. We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear transloca...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2007-03, Vol.360 (1), p.72-83 |
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| creator | Devaux, Patricia von Messling, Veronika Songsungthong, Warangkhana Springfeld, Christoph Cattaneo, Roberto |
| description | Abstract The measles virus (MV) P gene encodes three proteins: P, an essential polymerase cofactor, and C and V, which have multiple functions including immune evasion. We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear translocation of the signal transducer and activator of transcription factors (STAT) after interferon type I treatment. In particular, MV P inhibits STAT1 phosphorylation. This is shown not only by transient expression but also by reverse genetic analyses based on a new functional infectious cDNA derived from a MV vaccine vial (Moraten strain). Our study also identifies a conserved sequence around P protein tyrosine 110 as a candidate interaction site with a cellular protein. |
| doi_str_mv | 10.1016/j.virol.2006.09.049 |
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We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear translocation of the signal transducer and activator of transcription factors (STAT) after interferon type I treatment. In particular, MV P inhibits STAT1 phosphorylation. This is shown not only by transient expression but also by reverse genetic analyses based on a new functional infectious cDNA derived from a MV vaccine vial (Moraten strain). 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We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear translocation of the signal transducer and activator of transcription factors (STAT) after interferon type I treatment. In particular, MV P inhibits STAT1 phosphorylation. This is shown not only by transient expression but also by reverse genetic analyses based on a new functional infectious cDNA derived from a MV vaccine vial (Moraten strain). Our study also identifies a conserved sequence around P protein tyrosine 110 as a candidate interaction site with a cellular protein.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cell Nucleus - metabolism</subject><subject>Cercopithecus aethiops</subject><subject>GENES</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>IMMUNITY</subject><subject>Immunity, Innate</subject><subject>Infectious Disease</subject><subject>Innate immunity</subject><subject>INTERFERON</subject><subject>Interferon signaling</subject><subject>Interferon Type I - pharmacology</subject><subject>Measles - immunology</subject><subject>Measles - virology</subject><subject>MEASLES VIRUS</subject><subject>Measles virus - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Phosphoprotein</subject><subject>PHOSPHOPROTEINS</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>PHOSPHORYLATION</subject><subject>Phosphorylation - drug effects</subject><subject>POLYMERASES</subject><subject>Sequence Alignment</subject><subject>Signal Transduction</subject><subject>STAT1 Transcription Factor - metabolism</subject><subject>TRANSCRIPTION FACTORS</subject><subject>TRANSLOCATION</subject><subject>TYROSINE</subject><subject>Tyrosine - physiology</subject><subject>VACCINES</subject><subject>Vero Cells</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkktr3DAUhUVpaaZpf0GhCArZ2b16WBovWgihLwh0kemqCyFL14wmHmsi2YH595U7UwrdZCGE4LtHnHMuIW8Z1AyY-rCrH0OKQ80BVA1tDbJ9RlYMWlWBkOw5WQFIXqk15xfkVc47KG-t4SW5YJox3ii2Ir82xxRzGJEyBjSMdNoi3aPNA2Za9OdMD9uYyzmkOGEBQqYJH-aQ0NMp0m6I7p7eba437C-ZjoOdQhxfkxe9HTK-Od-X5OeXz5ubb9Xtj6_fb65vKyc1myoNynLsHAjrJCrJpJNCadFwbb3unEXX9wJQNh4aaRvZe-ZlB6r1ci19Ly7J-5NuzFMw2YUJ3dbFcUQ3GQ5t8QysUFcnqhh5mDFPZh-yw2GwI8Y5Gw1cwBr0kyBrlRLQQgHFCXQlwpywN4cU9jYdDQOzVGR25k9FZqnIQGtKRWXq3Vl-7vbo_82cOynAxxOAJbPHgGmxhKNDXzIvjnwMT3zw6b95N4QxODvc4xHzLs5pLHUYZjI3YO6WLVmWBBSAZlyK3wz5t9M</recordid><startdate>20070330</startdate><enddate>20070330</enddate><creator>Devaux, Patricia</creator><creator>von Messling, Veronika</creator><creator>Songsungthong, Warangkhana</creator><creator>Springfeld, Christoph</creator><creator>Cattaneo, Roberto</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><scope>OTOTI</scope></search><sort><creationdate>20070330</creationdate><title>Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation</title><author>Devaux, Patricia ; von Messling, Veronika ; Songsungthong, Warangkhana ; Springfeld, Christoph ; Cattaneo, Roberto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-706a2ebc03ac4e6414c43673527ad7bcaecff30e45d054a54fd1d4b069d484df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cell Nucleus - metabolism</topic><topic>Cercopithecus aethiops</topic><topic>GENES</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>IMMUNITY</topic><topic>Immunity, Innate</topic><topic>Infectious Disease</topic><topic>Innate immunity</topic><topic>INTERFERON</topic><topic>Interferon signaling</topic><topic>Interferon Type I - pharmacology</topic><topic>Measles - immunology</topic><topic>Measles - virology</topic><topic>MEASLES VIRUS</topic><topic>Measles virus - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Phosphoprotein</topic><topic>PHOSPHOPROTEINS</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>PHOSPHORYLATION</topic><topic>Phosphorylation - drug effects</topic><topic>POLYMERASES</topic><topic>Sequence Alignment</topic><topic>Signal Transduction</topic><topic>STAT1 Transcription Factor - metabolism</topic><topic>TRANSCRIPTION FACTORS</topic><topic>TRANSLOCATION</topic><topic>TYROSINE</topic><topic>Tyrosine - physiology</topic><topic>VACCINES</topic><topic>Vero Cells</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Devaux, Patricia</creatorcontrib><creatorcontrib>von Messling, Veronika</creatorcontrib><creatorcontrib>Songsungthong, Warangkhana</creatorcontrib><creatorcontrib>Springfeld, Christoph</creatorcontrib><creatorcontrib>Cattaneo, Roberto</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><collection>OSTI.GOV</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Devaux, Patricia</au><au>von Messling, Veronika</au><au>Songsungthong, Warangkhana</au><au>Springfeld, Christoph</au><au>Cattaneo, Roberto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2007-03-30</date><risdate>2007</risdate><volume>360</volume><issue>1</issue><spage>72</spage><epage>83</epage><pages>72-83</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract The measles virus (MV) P gene encodes three proteins: P, an essential polymerase cofactor, and C and V, which have multiple functions including immune evasion. We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear translocation of the signal transducer and activator of transcription factors (STAT) after interferon type I treatment. In particular, MV P inhibits STAT1 phosphorylation. This is shown not only by transient expression but also by reverse genetic analyses based on a new functional infectious cDNA derived from a MV vaccine vial (Moraten strain). Our study also identifies a conserved sequence around P protein tyrosine 110 as a candidate interaction site with a cellular protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17112561</pmid><doi>10.1016/j.virol.2006.09.049</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Virology (New York, N.Y.), 2007-03, Vol.360 (1), p.72-83 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via ScienceDirect (Elsevier) |
| subjects | 60 APPLIED LIFE SCIENCES Animals Base Sequence Cell Nucleus - metabolism Cercopithecus aethiops GENES HeLa Cells Humans IMMUNITY Immunity, Innate Infectious Disease Innate immunity INTERFERON Interferon signaling Interferon Type I - pharmacology Measles - immunology Measles - virology MEASLES VIRUS Measles virus - metabolism Molecular Sequence Data Phosphoprotein PHOSPHOPROTEINS Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism PHOSPHORYLATION Phosphorylation - drug effects POLYMERASES Sequence Alignment Signal Transduction STAT1 Transcription Factor - metabolism TRANSCRIPTION FACTORS TRANSLOCATION TYROSINE Tyrosine - physiology VACCINES Vero Cells Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism |
| title | Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation |
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