The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication
The ability of vaccinia virus to inhibit processes of cap-dependent translational initiation by inactivating the eukaryotic translation initiation factor 4E (eIF-4E) has been examined. Analyses of the quantities of eIF-4E present in either uninfected mouse L929 cells or vaccinia virus-infected cells...
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Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1992-06, Vol.188 (2), p.934-937 |
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creator | Gierman, Todd M. Frederickson, Robert M. Sonenberg, Nahum Pickup, David J. |
description | The ability of vaccinia virus to inhibit processes of cap-dependent translational initiation by inactivating the eukaryotic translation initiation factor 4E (eIF-4E) has been examined. Analyses of the quantities of eIF-4E present in either uninfected mouse L929 cells or vaccinia virus-infected cells showed that during the first 12 hr of virus replication, when there is a marked decrease in host gene expression in infected cells, there is no change in the total amount of eIF-4E present. Analyses of eIF-4E that was metabolically labeled with [
32P] and then purified by affinity chromatography using m
7GTP-Sepharose 4B, indicated that neither the incorporation of radiolabel into eIF-4E nor the amounts of eIF-4E capable of binding to cap structures changed significantly during virus replication. Immunodetection of phosphorylated and unphosphorylated eIF-4E in cell lysates fractionated by two-dimensional gel electrophoresis showed that the steady-state levels of phosphorylated and unphosphorylated forms of eIF-4E were similar in uninfected and virus-infected cells. These results suggest that vaccinia virus does not gain preferential translation of viral mRNAs over other mRNAs in the cell by reducing either eIF-4E phosphorylation or its ability to bind to the cap structure. |
doi_str_mv | 10.1016/0042-6822(92)90557-6 |
format | Article |
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32P] and then purified by affinity chromatography using m
7GTP-Sepharose 4B, indicated that neither the incorporation of radiolabel into eIF-4E nor the amounts of eIF-4E capable of binding to cap structures changed significantly during virus replication. Immunodetection of phosphorylated and unphosphorylated eIF-4E in cell lysates fractionated by two-dimensional gel electrophoresis showed that the steady-state levels of phosphorylated and unphosphorylated forms of eIF-4E were similar in uninfected and virus-infected cells. These results suggest that vaccinia virus does not gain preferential translation of viral mRNAs over other mRNAs in the cell by reducing either eIF-4E phosphorylation or its ability to bind to the cap structure.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/0042-6822(92)90557-6</identifier><identifier>PMID: 1585661</identifier><identifier>CODEN: VIRLAX</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Electrophoresis, Gel, Two-Dimensional ; Eukaryotic Initiation Factor-4E ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Viral ; In Vitro Techniques ; L Cells (Cell Line) ; Mice ; Microbiology ; Peptide Initiation Factors - metabolism ; Phosphorylation ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; RNA Caps - metabolism ; vaccinia virus ; Vaccinia virus - genetics ; Virology ; Virus Replication</subject><ispartof>Virology (New York, N.Y.), 1992-06, Vol.188 (2), p.934-937</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-8e807669aff92ef6c150386e65f77db4b9fea8d8eeef7bddc2d72db542b62e5e3</citedby><cites>FETCH-LOGICAL-c417t-8e807669aff92ef6c150386e65f77db4b9fea8d8eeef7bddc2d72db542b62e5e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0042682292905576$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5359363$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1585661$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gierman, Todd M.</creatorcontrib><creatorcontrib>Frederickson, Robert M.</creatorcontrib><creatorcontrib>Sonenberg, Nahum</creatorcontrib><creatorcontrib>Pickup, David J.</creatorcontrib><title>The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>The ability of vaccinia virus to inhibit processes of cap-dependent translational initiation by inactivating the eukaryotic translation initiation factor 4E (eIF-4E) has been examined. Analyses of the quantities of eIF-4E present in either uninfected mouse L929 cells or vaccinia virus-infected cells showed that during the first 12 hr of virus replication, when there is a marked decrease in host gene expression in infected cells, there is no change in the total amount of eIF-4E present. Analyses of eIF-4E that was metabolically labeled with [
32P] and then purified by affinity chromatography using m
7GTP-Sepharose 4B, indicated that neither the incorporation of radiolabel into eIF-4E nor the amounts of eIF-4E capable of binding to cap structures changed significantly during virus replication. Immunodetection of phosphorylated and unphosphorylated eIF-4E in cell lysates fractionated by two-dimensional gel electrophoresis showed that the steady-state levels of phosphorylated and unphosphorylated forms of eIF-4E were similar in uninfected and virus-infected cells. These results suggest that vaccinia virus does not gain preferential translation of viral mRNAs over other mRNAs in the cell by reducing either eIF-4E phosphorylation or its ability to bind to the cap structure.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Eukaryotic Initiation Factor-4E</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Viral</subject><subject>In Vitro Techniques</subject><subject>L Cells (Cell Line)</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Peptide Initiation Factors - metabolism</subject><subject>Phosphorylation</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>RNA Caps - metabolism</subject><subject>vaccinia virus</subject><subject>Vaccinia virus - genetics</subject><subject>Virology</subject><subject>Virus Replication</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2KFDEUhYMoYzv6BgpZiOiiNElVkspGkGH8gQE34zqkkhu9Wl1pk1SDb2_KbsadQiAJ9zuHyzmEPOXsNWdcvWFsEJ0ahXhpxCvDpNSdukd2nBnVsX7g98nuDnlIHpXynbW_1uyCXHA5SqX4jqTbb0Bh_eHyr1TR05rdUmZXMS0UF6x4ekbna8p0uKZY6JIq3aeAESHQsGZcvtLabHxacwGaIj0675va0SPmtdAMhxn9H6fH5EF0c4En5_uSfHl_fXv1sbv5_OHT1bubzg9c126EkWmljIvRCIjKc8n6UYGSUeswDZOJ4MYwAkDUUwheBC3CJAcxKQES-kvy4uR7yOnnCqXaPRYP8-wWSGuxWphBST3-F-TKbIvoBg4n0OdUSoZoDxn3LTfLmd0KsVvadkvbmna2Qqxqsmdn_3XaQ_grOjXQ5s_Pc1e8m2PL32O5w2QvTa_6hr09YdBCOyJkWzzC4iFgBl9tSPjvPX4D8BKpPw</recordid><startdate>19920601</startdate><enddate>19920601</enddate><creator>Gierman, Todd M.</creator><creator>Frederickson, Robert M.</creator><creator>Sonenberg, Nahum</creator><creator>Pickup, David J.</creator><general>Elsevier Inc</general><general>Elsevier</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19920601</creationdate><title>The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication</title><author>Gierman, Todd M. ; Frederickson, Robert M. ; Sonenberg, Nahum ; Pickup, David J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-8e807669aff92ef6c150386e65f77db4b9fea8d8eeef7bddc2d72db542b62e5e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Eukaryotic Initiation Factor-4E</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Viral</topic><topic>In Vitro Techniques</topic><topic>L Cells (Cell Line)</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Peptide Initiation Factors - metabolism</topic><topic>Phosphorylation</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>RNA Caps - metabolism</topic><topic>vaccinia virus</topic><topic>Vaccinia virus - genetics</topic><topic>Virology</topic><topic>Virus Replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gierman, Todd M.</creatorcontrib><creatorcontrib>Frederickson, Robert M.</creatorcontrib><creatorcontrib>Sonenberg, Nahum</creatorcontrib><creatorcontrib>Pickup, David J.</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>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>Gierman, Todd M.</au><au>Frederickson, Robert M.</au><au>Sonenberg, Nahum</au><au>Pickup, David J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1992-06-01</date><risdate>1992</risdate><volume>188</volume><issue>2</issue><spage>934</spage><epage>937</epage><pages>934-937</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><coden>VIRLAX</coden><abstract>The ability of vaccinia virus to inhibit processes of cap-dependent translational initiation by inactivating the eukaryotic translation initiation factor 4E (eIF-4E) has been examined. Analyses of the quantities of eIF-4E present in either uninfected mouse L929 cells or vaccinia virus-infected cells showed that during the first 12 hr of virus replication, when there is a marked decrease in host gene expression in infected cells, there is no change in the total amount of eIF-4E present. Analyses of eIF-4E that was metabolically labeled with [
32P] and then purified by affinity chromatography using m
7GTP-Sepharose 4B, indicated that neither the incorporation of radiolabel into eIF-4E nor the amounts of eIF-4E capable of binding to cap structures changed significantly during virus replication. Immunodetection of phosphorylated and unphosphorylated eIF-4E in cell lysates fractionated by two-dimensional gel electrophoresis showed that the steady-state levels of phosphorylated and unphosphorylated forms of eIF-4E were similar in uninfected and virus-infected cells. These results suggest that vaccinia virus does not gain preferential translation of viral mRNAs over other mRNAs in the cell by reducing either eIF-4E phosphorylation or its ability to bind to the cap structure.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1585661</pmid><doi>10.1016/0042-6822(92)90557-6</doi><tpages>4</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
subjects | Animals Biological and medical sciences Electrophoresis, Gel, Two-Dimensional Eukaryotic Initiation Factor-4E Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Viral In Vitro Techniques L Cells (Cell Line) Mice Microbiology Peptide Initiation Factors - metabolism Phosphorylation Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains RNA Caps - metabolism vaccinia virus Vaccinia virus - genetics Virology Virus Replication |
title | The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication |
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