Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection

[Background]: The genomes of plant viruses have limited coding capacity, and to complete their infectious cycles, viral factors must target, direct or indirectly, many host elements. However, the interaction networks between viruses and host factors are poorly understood. The genus Potyvirus is the...

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Autores: Martínez, Fernando, Rodrigo, Guillermo, Aragonés, Verónica, Ruiz, Marta, Lodewijk, Iris, Fernández, Unai, Elena, Santiago F., Daròs Arnau, José Antonio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2016
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/128476
Acceso en línea:http://hdl.handle.net/10261/128476
Access Level:acceso abierto
Palabra clave:Host-virus systems biology
Protein interaction network
RNA virus
Plant virus
Potyvirus
Nuclear inclusion a protein
Affinity purification mass spectrometry
Arabidopsis thaliana
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oai_identifier_str oai:digital.csic.es:10261/128476
network_acronym_str ES
network_name_str España
repository_id_str
dc.title.none.fl_str_mv Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
title Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
spellingShingle Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
Martínez, Fernando
Host-virus systems biology
Protein interaction network
RNA virus
Plant virus
Potyvirus
Nuclear inclusion a protein
Affinity purification mass spectrometry
Arabidopsis thaliana
title_short Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
title_full Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
title_fullStr Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
title_full_unstemmed Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
title_sort Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infection
dc.creator.none.fl_str_mv Martínez, Fernando
Rodrigo, Guillermo
Aragonés, Verónica
Ruiz, Marta
Lodewijk, Iris
Fernández, Unai
Elena, Santiago F.
Daròs Arnau, José Antonio
author Martínez, Fernando
author_facet Martínez, Fernando
Rodrigo, Guillermo
Aragonés, Verónica
Ruiz, Marta
Lodewijk, Iris
Fernández, Unai
Elena, Santiago F.
Daròs Arnau, José Antonio
author_role author
author2 Rodrigo, Guillermo
Aragonés, Verónica
Ruiz, Marta
Lodewijk, Iris
Fernández, Unai
Elena, Santiago F.
Daròs Arnau, José Antonio
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Generalitat Valenciana
Universidad Politécnica de Valencia
CSIC - Unidad de Recursos de Información Científica para la Investigación (URICI)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Host-virus systems biology
Protein interaction network
RNA virus
Plant virus
Potyvirus
Nuclear inclusion a protein
Affinity purification mass spectrometry
Arabidopsis thaliana
topic Host-virus systems biology
Protein interaction network
RNA virus
Plant virus
Potyvirus
Nuclear inclusion a protein
Affinity purification mass spectrometry
Arabidopsis thaliana
description [Background]: The genomes of plant viruses have limited coding capacity, and to complete their infectious cycles, viral factors must target, direct or indirectly, many host elements. However, the interaction networks between viruses and host factors are poorly understood. The genus Potyvirus is the largest group of plus-strand RNA viruses infecting plants. Potyviral nuclear inclusion a (NIa) plays many roles during infection. NIa is a polyprotein consisting of two domains, viral protein genome-linked (VPg) and protease (NIaPro), separated by an inefficiently utilized self-proteolytic site. To gain insights about the interaction between potyviral NIa and the host cell during infection, we constructed Tobacco etch virus (TEV, genus Potyvirus) infectious clones in which the VPg or the NIaPro domains of NIa were tagged with the affinity polypeptide Twin-Strep-tag and identified the host proteins targeted by the viral proteins by affinity purification followed by mass spectrometry analysis (AP-MS).
publishDate 2016
dc.date.none.fl_str_mv 2016
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/128476
url http://hdl.handle.net/10261/128476
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2014-54269-R
http://dx.doi.org/10.1186/s12864-016-2394-y

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv BioMed Central
publisher.none.fl_str_mv BioMed Central
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
repository.name.fl_str_mv
repository.mail.fl_str_mv
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spelling Interaction network of tobacco etch potyvirus NIa protein with the host proteome during infectionMartínez, FernandoRodrigo, GuillermoAragonés, VerónicaRuiz, MartaLodewijk, IrisFernández, UnaiElena, Santiago F.Daròs Arnau, José AntonioHost-virus systems biologyProtein interaction networkRNA virusPlant virusPotyvirusNuclear inclusion a proteinAffinity purification mass spectrometryArabidopsis thaliana[Background]: The genomes of plant viruses have limited coding capacity, and to complete their infectious cycles, viral factors must target, direct or indirectly, many host elements. However, the interaction networks between viruses and host factors are poorly understood. The genus Potyvirus is the largest group of plus-strand RNA viruses infecting plants. Potyviral nuclear inclusion a (NIa) plays many roles during infection. NIa is a polyprotein consisting of two domains, viral protein genome-linked (VPg) and protease (NIaPro), separated by an inefficiently utilized self-proteolytic site. To gain insights about the interaction between potyviral NIa and the host cell during infection, we constructed Tobacco etch virus (TEV, genus Potyvirus) infectious clones in which the VPg or the NIaPro domains of NIa were tagged with the affinity polypeptide Twin-Strep-tag and identified the host proteins targeted by the viral proteins by affinity purification followed by mass spectrometry analysis (AP-MS).[Results]: We identified 232 different Arabidopsis thaliana proteins forming part of complexes in which TEV NIa products were also involved. VPg and NIaPro specifically targeted 89 and 76 of these proteins, respectively, whereas 67 proteins were targeted by both domains and considered full-length NIa targets. Taking advantage of the currently known A. thaliana interactome, we constructed a protein interaction network between TEV NIa domains and 516 host proteins. The most connected elements specifically targeted by VPg were G-box regulating factor 6 and mitochondrial ATP synthase δ subunit; those specifically targeted by NIaPro were plasma membrane aquaporin PIP2;7 and actin 7, whereas those targeted by full-length NIa were heat shock protein 70–1 and photosystem protein LHCA3. Moreover, a contextualization in the global A. thaliana interactome showed that NIa targets are not more connected with other host proteins than expected by chance, but are in a position that allows them to connect with other host proteins in shorter paths. Further analysis of NIa-targeted host proteins revealed that they are mainly involved in response to stress, metabolism, photosynthesis, and localization. Many of these proteins are connected with the phytohormone ethylene.[Conclusions]: Potyviral NIa targets many host elements during infection, establishing a network in which information is efficiently transmitted.This work was supported by grants BIO2011-26741, BIO2014-54269-R and BFU2012-30805 from Ministerio de Economía y Competitividad (Spain) and PROMETEOII/2014/021 from Generalitat Valenciana. F.M. was the recipient of a predoctoral fellowship from Universidad Politécnica de Valencia.We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI).BioMed CentralMinisterio de Economía y Competitividad (España)Generalitat ValencianaUniversidad Politécnica de ValenciaCSIC - Unidad de Recursos de Información Científica para la Investigación (URICI)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2016201620162016info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/128476reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2014-54269-Rhttp://dx.doi.org/10.1186/s12864-016-2394-ySíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1284762026-05-22T06:33:51Z
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