Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets

Autores
Iglesias, Nestor Gabriel; Mondotte, Juan Alberto; Byk, Laura Andrea; de Maio, Federico Andres; Samsa, Marcelo Mario Alejandro; Alvarez, Cecilia Ines; Gamarnik, Andrea Vanesa
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Dengue viruses cause the most important human viral disease transmittedby mosquitoes. In recent years, a great deal has been learnedabout molecular details of dengue virus genome replication; however,little is known about genome encapsidation and the functions of theviral capsid protein. During infection, dengue virus capsid progressivelyaccumulates around lipid droplets (LDs) by an unknown mechanism.Here, we examined the process by which the viral capsid is transportedfrom the endoplasmic reticulum (ER) membrane, where the protein issynthesized, to LDs. Using different methods of intervention, we foundthat the GBF1-Arf1/Arf4-COPI pathway is necessary for capsid transportto LDs, while the process is independent of both COPII componentsand Golgi integrity. The transport was sensitive to Brefeldin A, while adrug resistant form of GBF1 was sufficient to restore capsid subcellulardistribution in infected cells. The mechanism by which LDs gain or loseproteins is still an open question. Our results support a model in whichthe virus uses a non-canonical function of the COPI system for capsidaccumulation on LDs, providing new ideas for antiviral strategies.
Fil: Iglesias, Nestor Gabriel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Mondotte, Juan Alberto. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Byk, Laura Andrea. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: de Maio, Federico Andres. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Samsa, Marcelo Mario Alejandro. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Bioquímica Clínica E Inmunología; Argentina
Fil: Gamarnik, Andrea Vanesa. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Capsid Protein
Copi
Dengue Virus
Flavivirus
Gbf1
Lipid Droplets
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:11336/7808
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/7808
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid DropletsIglesias, Nestor GabrielMondotte, Juan AlbertoByk, Laura Andreade Maio, Federico AndresSamsa, Marcelo Mario AlejandroAlvarez, Cecilia InesGamarnik, Andrea VanesaCapsid ProteinCopiDengue VirusFlavivirusGbf1Lipid Dropletshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Dengue viruses cause the most important human viral disease transmittedby mosquitoes. In recent years, a great deal has been learnedabout molecular details of dengue virus genome replication; however,little is known about genome encapsidation and the functions of theviral capsid protein. During infection, dengue virus capsid progressivelyaccumulates around lipid droplets (LDs) by an unknown mechanism.Here, we examined the process by which the viral capsid is transportedfrom the endoplasmic reticulum (ER) membrane, where the protein issynthesized, to LDs. Using different methods of intervention, we foundthat the GBF1-Arf1/Arf4-COPI pathway is necessary for capsid transportto LDs, while the process is independent of both COPII componentsand Golgi integrity. The transport was sensitive to Brefeldin A, while adrug resistant form of GBF1 was sufficient to restore capsid subcellulardistribution in infected cells. The mechanism by which LDs gain or loseproteins is still an open question. Our results support a model in whichthe virus uses a non-canonical function of the COPI system for capsidaccumulation on LDs, providing new ideas for antiviral strategies.Fil: Iglesias, Nestor Gabriel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Mondotte, Juan Alberto. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Byk, Laura Andrea. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: de Maio, Federico Andres. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Samsa, Marcelo Mario Alejandro. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Bioquímica Clínica E Inmunología; ArgentinaFil: Gamarnik, Andrea Vanesa. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaWiley2015-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7808Iglesias, Nestor Gabriel; Mondotte, Juan Alberto; Byk, Laura Andrea; de Maio, Federico Andres; Samsa, Marcelo Mario Alejandro; et al.; Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets; Wiley; Traffic; 16; 9; 6-2015; 962-9771398-9219enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/tra.12305/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1111/tra.12305info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:04:35Zoai:ri.conicet.gov.ar:11336/7808instacron: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:34982025-09-29 10:04:35.513CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
title Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
spellingShingle Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
Iglesias, Nestor Gabriel
Capsid Protein
Copi
Dengue Virus
Flavivirus
Gbf1
Lipid Droplets
title_short Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
title_full Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
title_fullStr Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
title_full_unstemmed Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
title_sort Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets
dc.creator.none.fl_str_mv Iglesias, Nestor Gabriel
Mondotte, Juan Alberto
Byk, Laura Andrea
de Maio, Federico Andres
Samsa, Marcelo Mario Alejandro
Alvarez, Cecilia Ines
Gamarnik, Andrea Vanesa
author Iglesias, Nestor Gabriel
author_facet Iglesias, Nestor Gabriel
Mondotte, Juan Alberto
Byk, Laura Andrea
de Maio, Federico Andres
Samsa, Marcelo Mario Alejandro
Alvarez, Cecilia Ines
Gamarnik, Andrea Vanesa
author_role author
author2 Mondotte, Juan Alberto
Byk, Laura Andrea
de Maio, Federico Andres
Samsa, Marcelo Mario Alejandro
Alvarez, Cecilia Ines
Gamarnik, Andrea Vanesa
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Capsid Protein
Copi
Dengue Virus
Flavivirus
Gbf1
Lipid Droplets
topic Capsid Protein
Copi
Dengue Virus
Flavivirus
Gbf1
Lipid Droplets
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Dengue viruses cause the most important human viral disease transmittedby mosquitoes. In recent years, a great deal has been learnedabout molecular details of dengue virus genome replication; however,little is known about genome encapsidation and the functions of theviral capsid protein. During infection, dengue virus capsid progressivelyaccumulates around lipid droplets (LDs) by an unknown mechanism.Here, we examined the process by which the viral capsid is transportedfrom the endoplasmic reticulum (ER) membrane, where the protein issynthesized, to LDs. Using different methods of intervention, we foundthat the GBF1-Arf1/Arf4-COPI pathway is necessary for capsid transportto LDs, while the process is independent of both COPII componentsand Golgi integrity. The transport was sensitive to Brefeldin A, while adrug resistant form of GBF1 was sufficient to restore capsid subcellulardistribution in infected cells. The mechanism by which LDs gain or loseproteins is still an open question. Our results support a model in whichthe virus uses a non-canonical function of the COPI system for capsidaccumulation on LDs, providing new ideas for antiviral strategies.
Fil: Iglesias, Nestor Gabriel. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Mondotte, Juan Alberto. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Byk, Laura Andrea. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: de Maio, Federico Andres. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Samsa, Marcelo Mario Alejandro. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Bioquímica Clínica E Inmunología; Argentina
Fil: Gamarnik, Andrea Vanesa. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Dengue viruses cause the most important human viral disease transmittedby mosquitoes. In recent years, a great deal has been learnedabout molecular details of dengue virus genome replication; however,little is known about genome encapsidation and the functions of theviral capsid protein. During infection, dengue virus capsid progressivelyaccumulates around lipid droplets (LDs) by an unknown mechanism.Here, we examined the process by which the viral capsid is transportedfrom the endoplasmic reticulum (ER) membrane, where the protein issynthesized, to LDs. Using different methods of intervention, we foundthat the GBF1-Arf1/Arf4-COPI pathway is necessary for capsid transportto LDs, while the process is independent of both COPII componentsand Golgi integrity. The transport was sensitive to Brefeldin A, while adrug resistant form of GBF1 was sufficient to restore capsid subcellulardistribution in infected cells. The mechanism by which LDs gain or loseproteins is still an open question. Our results support a model in whichthe virus uses a non-canonical function of the COPI system for capsidaccumulation on LDs, providing new ideas for antiviral strategies.
publishDate 2015
dc.date.none.fl_str_mv 2015-06
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/11336/7808
Iglesias, Nestor Gabriel; Mondotte, Juan Alberto; Byk, Laura Andrea; de Maio, Federico Andres; Samsa, Marcelo Mario Alejandro; et al.; Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets; Wiley; Traffic; 16; 9; 6-2015; 962-977
1398-9219
url http://hdl.handle.net/11336/7808
identifier_str_mv Iglesias, Nestor Gabriel; Mondotte, Juan Alberto; Byk, Laura Andrea; de Maio, Federico Andres; Samsa, Marcelo Mario Alejandro; et al.; Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets; Wiley; Traffic; 16; 9; 6-2015; 962-977
1398-9219
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/tra.12305/abstract
info:eu-repo/semantics/altIdentifier/doi/10.1111/tra.12305
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
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 13.070432

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