Structure of the Triatoma virus capsid

Autores
Squires, Gaëlle; Pous, Joan; Aguirre, Jon; Rozas Dennis, Gabriela Susana; Costabel, Marcelo Daniel; Marti, Gerardo Anibal; Navaza, Jorge; Bressanelli, Stéphane; Guérin, Diego Marcelo Alejandro; Rey, Felix A.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The members of the Dicistroviridae family are non-enveloped positive-sense single-stranded RNA (+ssRNA) viruses pathogenic to beneficial arthropods as well as insect pests of medical importance. Triatoma virus (TrV), a member of this family, infects several species of triatomine insects (popularly named kissing bugs), which are vectors for human trypanosomiasis, more commonly known as Chagas disease. The potential use of dicistroviruses as biological control agents has drawn considerable attention in the past decade, and several viruses of this family have been identified, with their targets covering honey bees, aphids and field crickets, among others. Here, the crystal structure of the TrV capsid at 2.5 A ˚ resolution is reported, showing that as expected it is very similar to that of Cricket paralysis virus (CrPV). Nevertheless, a number of distinguishing structural features support the introduction of a new genus (Triatovirus; type species TrV) under the Dicistroviridae family. The most striking differences are the absence of icosahedrally ordered VP4 within the infectious particle and the presence of prominent projections that surround the fivefold axis. Furthermore, the structure identifies a second putative autoproteolytic DDF motif in protein VP3, in addition to the conserved one in VP1 which is believed to be responsible for VP0 cleavage during capsid maturation. The potential meaning of these new findings is discussed
Fil: Squires, Gaëlle. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moléculaire et Structurale; Francia
Fil: Pous, Joan. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moléculaire et Structurale; Francia
Fil: Aguirre, Jon. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España. Fundación Biofísica Bizkaia; España
Fil: Rozas Dennis, Gabriela Susana. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina
Fil: Navaza, Jorge. Laboratoire de Virologie Moléculaire et Structurale; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Bressanelli, Stéphane. Laboratoire de Virologie Moleculaire Et Structurale; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina. Fundación Biofísica Bizkaia; España. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; España
Fil: Rey, Felix A.. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moleculaire Et Structurale; Francia
Materia
Triatoma virus
Trv
Cripavirus
Dicistroviridae
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/101866
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/101866
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structure of the Triatoma virus capsidSquires, GaëllePous, JoanAguirre, JonRozas Dennis, Gabriela SusanaCostabel, Marcelo DanielMarti, Gerardo AnibalNavaza, JorgeBressanelli, StéphaneGuérin, Diego Marcelo AlejandroRey, Felix A.Triatoma virusTrvCripavirusDicistroviridaehttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1The members of the Dicistroviridae family are non-enveloped positive-sense single-stranded RNA (+ssRNA) viruses pathogenic to beneficial arthropods as well as insect pests of medical importance. Triatoma virus (TrV), a member of this family, infects several species of triatomine insects (popularly named kissing bugs), which are vectors for human trypanosomiasis, more commonly known as Chagas disease. The potential use of dicistroviruses as biological control agents has drawn considerable attention in the past decade, and several viruses of this family have been identified, with their targets covering honey bees, aphids and field crickets, among others. Here, the crystal structure of the TrV capsid at 2.5 A ˚ resolution is reported, showing that as expected it is very similar to that of Cricket paralysis virus (CrPV). Nevertheless, a number of distinguishing structural features support the introduction of a new genus (Triatovirus; type species TrV) under the Dicistroviridae family. The most striking differences are the absence of icosahedrally ordered VP4 within the infectious particle and the presence of prominent projections that surround the fivefold axis. Furthermore, the structure identifies a second putative autoproteolytic DDF motif in protein VP3, in addition to the conserved one in VP1 which is believed to be responsible for VP0 cleavage during capsid maturation. The potential meaning of these new findings is discussedFil: Squires, Gaëlle. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moléculaire et Structurale; FranciaFil: Pous, Joan. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moléculaire et Structurale; FranciaFil: Aguirre, Jon. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España. Fundación Biofísica Bizkaia; EspañaFil: Rozas Dennis, Gabriela Susana. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; ArgentinaFil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaFil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; ArgentinaFil: Navaza, Jorge. Laboratoire de Virologie Moléculaire et Structurale; Francia. Centre National de la Recherche Scientifique; FranciaFil: Bressanelli, Stéphane. Laboratoire de Virologie Moleculaire Et Structurale; Francia. Centre National de la Recherche Scientifique; FranciaFil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina. Fundación Biofísica Bizkaia; España. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; EspañaFil: Rey, Felix A.. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moleculaire Et Structurale; FranciaWiley Blackwell Publishing, Inc2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/101866Squires, Gaëlle; Pous, Joan; Aguirre, Jon; Rozas Dennis, Gabriela Susana; Costabel, Marcelo Daniel; et al.; Structure of the Triatoma virus capsid; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 69; 4-2013; 1026-10370907-4449CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S0907444913004617info:eu-repo/semantics/altIdentifier/doi/10.1107/S0907444913004617info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:56:09Zoai:ri.conicet.gov.ar:11336/101866instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:56:09.953CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure of the Triatoma virus capsid
title Structure of the Triatoma virus capsid
spellingShingle Structure of the Triatoma virus capsid
Squires, Gaëlle
Triatoma virus
Trv
Cripavirus
Dicistroviridae
title_short Structure of the Triatoma virus capsid
title_full Structure of the Triatoma virus capsid
title_fullStr Structure of the Triatoma virus capsid
title_full_unstemmed Structure of the Triatoma virus capsid
title_sort Structure of the Triatoma virus capsid
dc.creator.none.fl_str_mv Squires, Gaëlle
Pous, Joan
Aguirre, Jon
Rozas Dennis, Gabriela Susana
Costabel, Marcelo Daniel
Marti, Gerardo Anibal
Navaza, Jorge
Bressanelli, Stéphane
Guérin, Diego Marcelo Alejandro
Rey, Felix A.
author Squires, Gaëlle
author_facet Squires, Gaëlle
Pous, Joan
Aguirre, Jon
Rozas Dennis, Gabriela Susana
Costabel, Marcelo Daniel
Marti, Gerardo Anibal
Navaza, Jorge
Bressanelli, Stéphane
Guérin, Diego Marcelo Alejandro
Rey, Felix A.
author_role author
author2 Pous, Joan
Aguirre, Jon
Rozas Dennis, Gabriela Susana
Costabel, Marcelo Daniel
Marti, Gerardo Anibal
Navaza, Jorge
Bressanelli, Stéphane
Guérin, Diego Marcelo Alejandro
Rey, Felix A.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Triatoma virus
Trv
Cripavirus
Dicistroviridae
topic Triatoma virus
Trv
Cripavirus
Dicistroviridae
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The members of the Dicistroviridae family are non-enveloped positive-sense single-stranded RNA (+ssRNA) viruses pathogenic to beneficial arthropods as well as insect pests of medical importance. Triatoma virus (TrV), a member of this family, infects several species of triatomine insects (popularly named kissing bugs), which are vectors for human trypanosomiasis, more commonly known as Chagas disease. The potential use of dicistroviruses as biological control agents has drawn considerable attention in the past decade, and several viruses of this family have been identified, with their targets covering honey bees, aphids and field crickets, among others. Here, the crystal structure of the TrV capsid at 2.5 A ˚ resolution is reported, showing that as expected it is very similar to that of Cricket paralysis virus (CrPV). Nevertheless, a number of distinguishing structural features support the introduction of a new genus (Triatovirus; type species TrV) under the Dicistroviridae family. The most striking differences are the absence of icosahedrally ordered VP4 within the infectious particle and the presence of prominent projections that surround the fivefold axis. Furthermore, the structure identifies a second putative autoproteolytic DDF motif in protein VP3, in addition to the conserved one in VP1 which is believed to be responsible for VP0 cleavage during capsid maturation. The potential meaning of these new findings is discussed
Fil: Squires, Gaëlle. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moléculaire et Structurale; Francia
Fil: Pous, Joan. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moléculaire et Structurale; Francia
Fil: Aguirre, Jon. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España. Fundación Biofísica Bizkaia; España
Fil: Rozas Dennis, Gabriela Susana. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina
Fil: Navaza, Jorge. Laboratoire de Virologie Moléculaire et Structurale; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Bressanelli, Stéphane. Laboratoire de Virologie Moleculaire Et Structurale; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Guérin, Diego Marcelo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina. Fundación Biofísica Bizkaia; España. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; España
Fil: Rey, Felix A.. Centre National de la Recherche Scientifique; Francia. Laboratoire de Virologie Moleculaire Et Structurale; Francia
description The members of the Dicistroviridae family are non-enveloped positive-sense single-stranded RNA (+ssRNA) viruses pathogenic to beneficial arthropods as well as insect pests of medical importance. Triatoma virus (TrV), a member of this family, infects several species of triatomine insects (popularly named kissing bugs), which are vectors for human trypanosomiasis, more commonly known as Chagas disease. The potential use of dicistroviruses as biological control agents has drawn considerable attention in the past decade, and several viruses of this family have been identified, with their targets covering honey bees, aphids and field crickets, among others. Here, the crystal structure of the TrV capsid at 2.5 A ˚ resolution is reported, showing that as expected it is very similar to that of Cricket paralysis virus (CrPV). Nevertheless, a number of distinguishing structural features support the introduction of a new genus (Triatovirus; type species TrV) under the Dicistroviridae family. The most striking differences are the absence of icosahedrally ordered VP4 within the infectious particle and the presence of prominent projections that surround the fivefold axis. Furthermore, the structure identifies a second putative autoproteolytic DDF motif in protein VP3, in addition to the conserved one in VP1 which is believed to be responsible for VP0 cleavage during capsid maturation. The potential meaning of these new findings is discussed
publishDate 2013
dc.date.none.fl_str_mv 2013-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/101866
Squires, Gaëlle; Pous, Joan; Aguirre, Jon; Rozas Dennis, Gabriela Susana; Costabel, Marcelo Daniel; et al.; Structure of the Triatoma virus capsid; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 69; 4-2013; 1026-1037
0907-4449
CONICET Digital
CONICET
url http://hdl.handle.net/11336/101866
identifier_str_mv Squires, Gaëlle; Pous, Joan; Aguirre, Jon; Rozas Dennis, Gabriela Susana; Costabel, Marcelo Daniel; et al.; Structure of the Triatoma virus capsid; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 69; 4-2013; 1026-1037
0907-4449
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S0907444913004617
info:eu-repo/semantics/altIdentifier/doi/10.1107/S0907444913004617
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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