RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms

© 2015 by the author; licensee MDPI, Basel, Switzerland. RNA viruses typically encode their own RNA-dependent RNA polymerase (RdRP) to ensure genome replication within the infected cells. RdRP function is critical not only for the virus life cycle but also for its adaptive potential. The combination...

Descripción completa

Detalles Bibliográficos
Autores: Ferrer-Orta, Cristina, Ferrero, Diego, Verdaguer, Núria
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/124078
Acceso en línea:http://hdl.handle.net/10261/124078
Access Level:acceso abierto
Palabra clave:viral replication
RNA-dependent RNA polymerase
positive-strand RNA viruses
picornaviruses
replication fidelity
id ES_42a729ea0fa1de8ca751c0302bb178d8
oai_identifier_str oai:digital.csic.es:10261/124078
network_acronym_str ES
network_name_str España
repository_id_str
spelling RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanismsFerrer-Orta, CristinaFerrero, DiegoVerdaguer, Núriaviral replicationRNA-dependent RNA polymerasepositive-strand RNA virusespicornavirusesreplication fidelity© 2015 by the author; licensee MDPI, Basel, Switzerland. RNA viruses typically encode their own RNA-dependent RNA polymerase (RdRP) to ensure genome replication within the infected cells. RdRP function is critical not only for the virus life cycle but also for its adaptive potential. The combination of low fidelity of replication and the absence of proofreading and excision activities within the RdRPs result in high mutation frequencies that allow these viruses a rapid adaptation to changing environments. In this review, we summarize the current knowledge about structural and functional aspects on RdRP catalytic complexes, focused mainly in the Picornaviridae family. The structural data currently available from these viruses provided high-resolution snapshots for a range of conformational states associated to RNA template-primer binding, rNTP recognition, catalysis and chain translocation. As these enzymes are major targets for the development of antiviral compounds, such structural information is essential for the design of new therapies.Núria Verdaguer acknowledges funding from the Spanish Ministry of Economy and Competitiveness (BIO2011-24333). We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI).Peer ReviewedMultidisciplinary Digital Publishing InstituteConsejo Superior de Investigaciones Científicas (España)Ministerio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2015201520152015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/124078reponame: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/BIO2011-24333http://dx.doi.org/10.3390/v7082829Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1240782026-05-22T06:33:51Z
dc.title.none.fl_str_mv RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
title RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
spellingShingle RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
Ferrer-Orta, Cristina
viral replication
RNA-dependent RNA polymerase
positive-strand RNA viruses
picornaviruses
replication fidelity
title_short RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
title_full RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
title_fullStr RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
title_full_unstemmed RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
title_sort RNA-dependent RNA polymerases of picornaviruses: From the structure to regulatory mechanisms
dc.creator.none.fl_str_mv Ferrer-Orta, Cristina
Ferrero, Diego
Verdaguer, Núria
author Ferrer-Orta, Cristina
author_facet Ferrer-Orta, Cristina
Ferrero, Diego
Verdaguer, Núria
author_role author
author2 Ferrero, Diego
Verdaguer, Núria
author2_role author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas (España)
Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv viral replication
RNA-dependent RNA polymerase
positive-strand RNA viruses
picornaviruses
replication fidelity
topic viral replication
RNA-dependent RNA polymerase
positive-strand RNA viruses
picornaviruses
replication fidelity
description © 2015 by the author; licensee MDPI, Basel, Switzerland. RNA viruses typically encode their own RNA-dependent RNA polymerase (RdRP) to ensure genome replication within the infected cells. RdRP function is critical not only for the virus life cycle but also for its adaptive potential. The combination of low fidelity of replication and the absence of proofreading and excision activities within the RdRPs result in high mutation frequencies that allow these viruses a rapid adaptation to changing environments. In this review, we summarize the current knowledge about structural and functional aspects on RdRP catalytic complexes, focused mainly in the Picornaviridae family. The structural data currently available from these viruses provided high-resolution snapshots for a range of conformational states associated to RNA template-primer binding, rNTP recognition, catalysis and chain translocation. As these enzymes are major targets for the development of antiviral compounds, such structural information is essential for the design of new therapies.
publishDate 2015
dc.date.none.fl_str_mv 2015
2015
2015
2015
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/10261/124078
url http://hdl.handle.net/10261/124078
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/BIO2011-24333
http://dx.doi.org/10.3390/v7082829
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
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
_version_ 1869406954283073536
score 15,81155

Similares en LA Referencia