Probing the biophysical interplay between a viral genome and its capsid

Autores
Snijder, J.; Uetrecht, C.; Rose, R. J.; Sanchez Eugenia, R.; Marti, Gerardo Anibal; Agirre, J.; Guérin, D. M. A.; Wuite, G. J. L.; Heck, A; Roos, W. H.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The interaction between a viral capsid and its genome governs crucial steps in the life cycle of a virus, such as assembly and genome uncoating. Tuning cargo–capsid interactions is also essential for successful design and cargo delivery in engineered viral systems. Here we investigate the interplay between cargo and capsid for the picorna-like Triatoma virus using a combined native mass spectrometry and atomic force microscopy approach. We propose a topology and assembly model in which heterotrimeric pentons that consist of five copies of structural proteins VP1, VP2 and VP3 are the free principal units of assembly. The interpenton contacts are established primarily by VP2. The dual role of the genome is first to stabilize the densely packed virion and, on an increase in pH, second to trigger uncoating by relaxing the stabilizing interactions with the capsid. Uncoating occurs through a labile intermediate state of the virion that reversibly disassembles into pentons with the concomitant release of protein VP4.
Fil: Snijder, J.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos. Vrije Universiteit; Países Bajos
Fil: Uetrecht, C.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos
Fil: Rose, R. J.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos
Fil: Sanchez Eugenia, R.. Universidad del Pais Vasco; España
Fil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Centro de Estudios Parasitológicos y de Vectores (i); Argentina. Universidad Nacional de La Plata; Argentina
Fil: Agirre, J.. Universidad del Pais Vasco; España. Fundación Biofisica Bizkaia; España
Fil: Guérin, D. M. A.. Universidad del Pais Vasco; España. Fundación Biofisica Bizkaia; España
Fil: Wuite, G. J. L.. Vrije Universiteit; Países Bajos
Fil: Heck, A. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos
Fil: Roos, W. H.. Vrije Universiteit; Países Bajos
Materia
Triatoma Virus
Native Mass Spectrometry
Atomic Force Microscopy
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:11336/13827
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Probing the biophysical interplay between a viral genome and its capsidSnijder, J.Uetrecht, C.Rose, R. J.Sanchez Eugenia, R.Marti, Gerardo AnibalAgirre, J.Guérin, D. M. A.Wuite, G. J. L.Heck, ARoos, W. H.Triatoma VirusNative Mass SpectrometryAtomic Force Microscopyhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1The interaction between a viral capsid and its genome governs crucial steps in the life cycle of a virus, such as assembly and genome uncoating. Tuning cargo–capsid interactions is also essential for successful design and cargo delivery in engineered viral systems. Here we investigate the interplay between cargo and capsid for the picorna-like Triatoma virus using a combined native mass spectrometry and atomic force microscopy approach. We propose a topology and assembly model in which heterotrimeric pentons that consist of five copies of structural proteins VP1, VP2 and VP3 are the free principal units of assembly. The interpenton contacts are established primarily by VP2. The dual role of the genome is first to stabilize the densely packed virion and, on an increase in pH, second to trigger uncoating by relaxing the stabilizing interactions with the capsid. Uncoating occurs through a labile intermediate state of the virion that reversibly disassembles into pentons with the concomitant release of protein VP4.Fil: Snijder, J.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos. Vrije Universiteit; Países BajosFil: Uetrecht, C.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países BajosFil: Rose, R. J.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países BajosFil: Sanchez Eugenia, R.. Universidad del Pais Vasco; EspañaFil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Centro de Estudios Parasitológicos y de Vectores (i); Argentina. Universidad Nacional de La Plata; ArgentinaFil: Agirre, J.. Universidad del Pais Vasco; España. Fundación Biofisica Bizkaia; EspañaFil: Guérin, D. M. A.. Universidad del Pais Vasco; España. Fundación Biofisica Bizkaia; EspañaFil: Wuite, G. J. L.. Vrije Universiteit; Países BajosFil: Heck, A. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países BajosFil: Roos, W. H.. Vrije Universiteit; Países BajosNature Publishing Group2013-04-28info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13827Snijder, J.; Uetrecht, C.; Rose, R. J.; Sanchez Eugenia, R.; Marti, Gerardo Anibal; et al.; Probing the biophysical interplay between a viral genome and its capsid; Nature Publishing Group; Nature Chemistry; 5; 28-4-2013; 502-5091755-4330enginfo:eu-repo/semantics/altIdentifier/doi/10.1038/NCHEM.1627info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/nchem/journal/v5/n6/full/nchem.1627.htmlinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:20:19Zoai:ri.conicet.gov.ar:11336/13827instacron: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:34982025-10-22 11:20:20.272CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Probing the biophysical interplay between a viral genome and its capsid
title Probing the biophysical interplay between a viral genome and its capsid
spellingShingle Probing the biophysical interplay between a viral genome and its capsid
Snijder, J.
Triatoma Virus
Native Mass Spectrometry
Atomic Force Microscopy
title_short Probing the biophysical interplay between a viral genome and its capsid
title_full Probing the biophysical interplay between a viral genome and its capsid
title_fullStr Probing the biophysical interplay between a viral genome and its capsid
title_full_unstemmed Probing the biophysical interplay between a viral genome and its capsid
title_sort Probing the biophysical interplay between a viral genome and its capsid
dc.creator.none.fl_str_mv Snijder, J.
Uetrecht, C.
Rose, R. J.
Sanchez Eugenia, R.
Marti, Gerardo Anibal
Agirre, J.
Guérin, D. M. A.
Wuite, G. J. L.
Heck, A
Roos, W. H.
author Snijder, J.
author_facet Snijder, J.
Uetrecht, C.
Rose, R. J.
Sanchez Eugenia, R.
Marti, Gerardo Anibal
Agirre, J.
Guérin, D. M. A.
Wuite, G. J. L.
Heck, A
Roos, W. H.
author_role author
author2 Uetrecht, C.
Rose, R. J.
Sanchez Eugenia, R.
Marti, Gerardo Anibal
Agirre, J.
Guérin, D. M. A.
Wuite, G. J. L.
Heck, A
Roos, W. H.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Triatoma Virus
Native Mass Spectrometry
Atomic Force Microscopy
topic Triatoma Virus
Native Mass Spectrometry
Atomic Force Microscopy
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 interaction between a viral capsid and its genome governs crucial steps in the life cycle of a virus, such as assembly and genome uncoating. Tuning cargo–capsid interactions is also essential for successful design and cargo delivery in engineered viral systems. Here we investigate the interplay between cargo and capsid for the picorna-like Triatoma virus using a combined native mass spectrometry and atomic force microscopy approach. We propose a topology and assembly model in which heterotrimeric pentons that consist of five copies of structural proteins VP1, VP2 and VP3 are the free principal units of assembly. The interpenton contacts are established primarily by VP2. The dual role of the genome is first to stabilize the densely packed virion and, on an increase in pH, second to trigger uncoating by relaxing the stabilizing interactions with the capsid. Uncoating occurs through a labile intermediate state of the virion that reversibly disassembles into pentons with the concomitant release of protein VP4.
Fil: Snijder, J.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos. Vrije Universiteit; Países Bajos
Fil: Uetrecht, C.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos
Fil: Rose, R. J.. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos
Fil: Sanchez Eugenia, R.. Universidad del Pais Vasco; España
Fil: Marti, Gerardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Centro de Estudios Parasitológicos y de Vectores (i); Argentina. Universidad Nacional de La Plata; Argentina
Fil: Agirre, J.. Universidad del Pais Vasco; España. Fundación Biofisica Bizkaia; España
Fil: Guérin, D. M. A.. Universidad del Pais Vasco; España. Fundación Biofisica Bizkaia; España
Fil: Wuite, G. J. L.. Vrije Universiteit; Países Bajos
Fil: Heck, A. Netherlands Proteomics Centre; Países Bajos. Utrecht Univeristy; Países Bajos
Fil: Roos, W. H.. Vrije Universiteit; Países Bajos
description The interaction between a viral capsid and its genome governs crucial steps in the life cycle of a virus, such as assembly and genome uncoating. Tuning cargo–capsid interactions is also essential for successful design and cargo delivery in engineered viral systems. Here we investigate the interplay between cargo and capsid for the picorna-like Triatoma virus using a combined native mass spectrometry and atomic force microscopy approach. We propose a topology and assembly model in which heterotrimeric pentons that consist of five copies of structural proteins VP1, VP2 and VP3 are the free principal units of assembly. The interpenton contacts are established primarily by VP2. The dual role of the genome is first to stabilize the densely packed virion and, on an increase in pH, second to trigger uncoating by relaxing the stabilizing interactions with the capsid. Uncoating occurs through a labile intermediate state of the virion that reversibly disassembles into pentons with the concomitant release of protein VP4.
publishDate 2013
dc.date.none.fl_str_mv 2013-04-28
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/11336/13827
Snijder, J.; Uetrecht, C.; Rose, R. J.; Sanchez Eugenia, R.; Marti, Gerardo Anibal; et al.; Probing the biophysical interplay between a viral genome and its capsid; Nature Publishing Group; Nature Chemistry; 5; 28-4-2013; 502-509
1755-4330
url http://hdl.handle.net/11336/13827
identifier_str_mv Snijder, J.; Uetrecht, C.; Rose, R. J.; Sanchez Eugenia, R.; Marti, Gerardo Anibal; et al.; Probing the biophysical interplay between a viral genome and its capsid; Nature Publishing Group; Nature Chemistry; 5; 28-4-2013; 502-509
1755-4330
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1038/NCHEM.1627
info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/nchem/journal/v5/n6/full/nchem.1627.html
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
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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 12.982451

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