Plant viral proteases: Beyond the role of peptide cutters

Almost half of known plant viral species rely on proteolytic cleavages as key co-and post-translational modifications throughout their infection cycle. Most of these viruses encode their own endopeptidases, proteases with high substrate specificity that internally cleave large polyprotein precursors...

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Detalles Bibliográficos
Autores: Rodamilans, Bernardo, Shan, Huanyuan, Pasin, Fabio, García, Juan Antonio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/205836
Acceso en línea:http://hdl.handle.net/10261/205836
Access Level:acceso abierto
Palabra clave:Viral proteases
Viral polyprotein
Plant viruses
Viral replication
Virion formation
Host range
Defense and counterdefense
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spelling Plant viral proteases: Beyond the role of peptide cuttersRodamilans, BernardoShan, HuanyuanPasin, FabioGarcía, Juan AntonioViral proteasesViral polyproteinPlant virusesViral replicationVirion formationHost rangeDefense and counterdefenseAlmost half of known plant viral species rely on proteolytic cleavages as key co-and post-translational modifications throughout their infection cycle. Most of these viruses encode their own endopeptidases, proteases with high substrate specificity that internally cleave large polyprotein precursors for the release of functional subunits. Processing of the polyprotein, however, is not an all-or-nothing process in which endopeptidases act as simple peptide cutters. On the contrary, spatial-temporal modulation of these polyprotein cleavage events is crucial for a successful viral infection. In this way, the processing of the polyprotein coordinates viral replication, assembly and movement, and has significant impact on pathogen fitness and virulence. In this mini-review, we give an overview of plant viral proteases emphasizing their importance during viral infections and the varied functionalities that result from their proteolytic activities.HS was supported by the China Scholarship Council; FP was supported by a post-doctoral fellowship from Academia Sinica. This work was funded by Grant No. BIO2016-80572-R and the FEDER program.Frontiers MediaChina Scholarship CouncilAcademia Sinica (Taiwan)Ministerio de Economía y Competitividad (España)European CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2020202020182020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/205836reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.3389/fpls.2018.00666Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2058362026-05-22T06:33:51Z
dc.title.none.fl_str_mv Plant viral proteases: Beyond the role of peptide cutters
title Plant viral proteases: Beyond the role of peptide cutters
spellingShingle Plant viral proteases: Beyond the role of peptide cutters
Rodamilans, Bernardo
Viral proteases
Viral polyprotein
Plant viruses
Viral replication
Virion formation
Host range
Defense and counterdefense
title_short Plant viral proteases: Beyond the role of peptide cutters
title_full Plant viral proteases: Beyond the role of peptide cutters
title_fullStr Plant viral proteases: Beyond the role of peptide cutters
title_full_unstemmed Plant viral proteases: Beyond the role of peptide cutters
title_sort Plant viral proteases: Beyond the role of peptide cutters
dc.creator.none.fl_str_mv Rodamilans, Bernardo
Shan, Huanyuan
Pasin, Fabio
García, Juan Antonio
author Rodamilans, Bernardo
author_facet Rodamilans, Bernardo
Shan, Huanyuan
Pasin, Fabio
García, Juan Antonio
author_role author
author2 Shan, Huanyuan
Pasin, Fabio
García, Juan Antonio
author2_role author
author
author
dc.contributor.none.fl_str_mv China Scholarship Council
Academia Sinica (Taiwan)
Ministerio de Economía y Competitividad (España)
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Viral proteases
Viral polyprotein
Plant viruses
Viral replication
Virion formation
Host range
Defense and counterdefense
topic Viral proteases
Viral polyprotein
Plant viruses
Viral replication
Virion formation
Host range
Defense and counterdefense
description Almost half of known plant viral species rely on proteolytic cleavages as key co-and post-translational modifications throughout their infection cycle. Most of these viruses encode their own endopeptidases, proteases with high substrate specificity that internally cleave large polyprotein precursors for the release of functional subunits. Processing of the polyprotein, however, is not an all-or-nothing process in which endopeptidases act as simple peptide cutters. On the contrary, spatial-temporal modulation of these polyprotein cleavage events is crucial for a successful viral infection. In this way, the processing of the polyprotein coordinates viral replication, assembly and movement, and has significant impact on pathogen fitness and virulence. In this mini-review, we give an overview of plant viral proteases emphasizing their importance during viral infections and the varied functionalities that result from their proteolytic activities.
publishDate 2018
dc.date.none.fl_str_mv 2018
2020
2020
2020
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/10261/205836
url http://hdl.handle.net/10261/205836
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.3389/fpls.2018.00666
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
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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score 15,812429

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