Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G

The infection of baby hamster kidney (BHK) cells by Sindbis virus gives rise to a drastic inhibition of cellular translation, while under these conditions the synthesis of viral structural proteins directed by the subgenomic 26 S mRNA takes place efficiently. Here, the requirement for intact initiat...

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Autores: Castelló, Alfredo, Sanz, Miguel Ángel, Molina, Susana, Carrasco Llamas, Luis
Formato: artículo
Fecha de publicación:2005
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/5044
Acesso em linha:http://hdl.handle.net/10261/5044
Access Level:acceso abierto
Palavra-chave:Alphavirus translation
Sindbis virus
eIF4G
Regulation of translation
Translation initiation factors
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spelling Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4GCastelló, AlfredoSanz, Miguel ÁngelMolina, SusanaCarrasco Llamas, LuisAlphavirus translationSindbis viruseIF4GRegulation of translationTranslation initiation factorsThe infection of baby hamster kidney (BHK) cells by Sindbis virus gives rise to a drastic inhibition of cellular translation, while under these conditions the synthesis of viral structural proteins directed by the subgenomic 26 S mRNA takes place efficiently. Here, the requirement for intact initiation factor eIF4G for the translation of this subgenomic mRNA has been examined. To this end, SV replicons that contain the protease of human immunodeficiency virus type 1 (HIV-1) or the poliovirus 2Apro replacing the sequences of SV glycoproteins have been constructed. BHK cells electroporated with the different RNAs synthesize protein C and the corresponding protease at late times. Notably, the proteolysis of eIF4G by both proteases has little effect on the translation of the 26 S mRNA. In addition, recombinant viable SVs were engineered that encode HIV-1 PR or poliovirus 2A protease under the control of a duplicated late promoter. Viral protein synthesis at late times of infection by the recombinant viruses is slightly affected in BHK cells that contain proteolysed eIF4G. The translatability of SV genomic 49 S mRNA was assayed in BHK cells infected with a recombinant virus that synthesizes luciferase and transfected with a replicon that expresses poliovirus 2Apro. Under conditions where eIF4G has been hydrolysed significantly the translation of genomic SV RNA was deeply inhibited. These findings indicate a different requirement for intact eIF4G in the translation of genomic and subgenomic SV mRNAs. Finally, the translation of the reporter gene that encodes green fluorescent protein, placed under the control of a second duplicate late promoter, is also resistant to the cleavage of eIF4G. In conclusion, despite the presence of a cap structure in the 5′ end of the subgenomic SV mRNA, intact eIF4G is not necessary for its translationThis study was support by grants from DGICYT (number BMC2003-00494), CAM (number 07B/0010/2002) and an Institutional Grant awarded to the Centro de Biología Molecular “Severo Ochoa” by the Fundación Ramón Areces. We are grateful to EU program EVA/MRC Centralised Facility for AIDS Reagents, NIBSC, UK for providing anti-HIV-1PR antibody. A.C. is the holder of an FPI FellowshipPeer reviewedElsevierMinisterio de Economía y Competitividad (España)Comunidad de MadridFundación Ramón Areces200820082005info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501194016 bytesapplication/pdfhttp://hdl.handle.net/10261/5044reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.jmb.2005.11.024info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/50442026-05-22T06:33:51Z
dc.title.none.fl_str_mv Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
title Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
spellingShingle Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
Castelló, Alfredo
Alphavirus translation
Sindbis virus
eIF4G
Regulation of translation
Translation initiation factors
title_short Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
title_full Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
title_fullStr Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
title_full_unstemmed Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
title_sort Translation of Sindbis Virus 26 S mRNA Does Not Require Intact Eukariotic Initiation Factor 4G
dc.creator.none.fl_str_mv Castelló, Alfredo
Sanz, Miguel Ángel
Molina, Susana
Carrasco Llamas, Luis
author Castelló, Alfredo
author_facet Castelló, Alfredo
Sanz, Miguel Ángel
Molina, Susana
Carrasco Llamas, Luis
author_role author
author2 Sanz, Miguel Ángel
Molina, Susana
Carrasco Llamas, Luis
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Comunidad de Madrid
Fundación Ramón Areces
dc.subject.none.fl_str_mv Alphavirus translation
Sindbis virus
eIF4G
Regulation of translation
Translation initiation factors
topic Alphavirus translation
Sindbis virus
eIF4G
Regulation of translation
Translation initiation factors
description The infection of baby hamster kidney (BHK) cells by Sindbis virus gives rise to a drastic inhibition of cellular translation, while under these conditions the synthesis of viral structural proteins directed by the subgenomic 26 S mRNA takes place efficiently. Here, the requirement for intact initiation factor eIF4G for the translation of this subgenomic mRNA has been examined. To this end, SV replicons that contain the protease of human immunodeficiency virus type 1 (HIV-1) or the poliovirus 2Apro replacing the sequences of SV glycoproteins have been constructed. BHK cells electroporated with the different RNAs synthesize protein C and the corresponding protease at late times. Notably, the proteolysis of eIF4G by both proteases has little effect on the translation of the 26 S mRNA. In addition, recombinant viable SVs were engineered that encode HIV-1 PR or poliovirus 2A protease under the control of a duplicated late promoter. Viral protein synthesis at late times of infection by the recombinant viruses is slightly affected in BHK cells that contain proteolysed eIF4G. The translatability of SV genomic 49 S mRNA was assayed in BHK cells infected with a recombinant virus that synthesizes luciferase and transfected with a replicon that expresses poliovirus 2Apro. Under conditions where eIF4G has been hydrolysed significantly the translation of genomic SV RNA was deeply inhibited. These findings indicate a different requirement for intact eIF4G in the translation of genomic and subgenomic SV mRNAs. Finally, the translation of the reporter gene that encodes green fluorescent protein, placed under the control of a second duplicate late promoter, is also resistant to the cleavage of eIF4G. In conclusion, despite the presence of a cap structure in the 5′ end of the subgenomic SV mRNA, intact eIF4G is not necessary for its translation
publishDate 2005
dc.date.none.fl_str_mv 2005
2008
2008
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/5044
url http://hdl.handle.net/10261/5044
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.jmb.2005.11.024
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 194016 bytes
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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