The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.

Autores
Delgui, Laura Ruth; Rodriguez, José F.; Colombo, Maria Isabel
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Infectious bursal disease virus (IBDV), a double-stranded RNA virus belonging to the Birnaviridae family, causes immunosuppression in chickens. In this study, we defined the localization of IBDV replication complexes based on colocalization analysis of VP3, the major protein component of IBDV ribonucleoproteins (RNPs). Our results indicate that VP3 localizes to vesicular structures bearing features of early and late endocytic compartments located in the juxtanuclear region. Interfering with the endocytic pathway with a dominant negative version of Rab5 after the internalization step leads to a reduction in virus titer. Triple-immunostaining studies between VP3, the viral RNA-dependent RNA polymerase VP1, and viral double-stranded RNA (dsRNA) showed a well-defined colocalization, indicating that the three critical components of the RNPs colocalize in the same structure, likely representing replication complexes. Interestingly, recombinant expressed VP3 also localizes to endosomes. Employing Golgi markers, we found that VP3-containing vesicles were closely associated with this organelle. Depolymerization of microtubules with nocodazole caused a profound change in VP3 localization, showing a punctate distribution scattered throughout the cytoplasm. However, these VP3-positive structures remained associated with Golgi ministacks. Similarly, brefeldin A (BFA) treatment led to a punctate distribution of VP3, scattered throughout the cytoplasm of infected cells. In addition, analysis of intra- and extracellular viral infective particles after BFA treatment of avian cells suggested a role for the Golgi complex in viral assembly. These results constitute the first study elucidating the localization of IBDV replication complexes (i.e., in endocytic compartments) and establishing a role for the Golgi apparatus in the assembly step of a birnavirus.
Fil: Delgui, Laura Ruth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: Rodriguez, José F.. Consejo Superior de Investigaciones Cientificas. Centro Nacional de Biotecnologia; España
Fil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina; Argentina; Argentina
Materia
Ibdv
Virus
Endocytosis
Golgi
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:11336/10075
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/10075
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.Delgui, Laura RuthRodriguez, José F.Colombo, Maria IsabelIbdvVirusEndocytosisGolgihttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Infectious bursal disease virus (IBDV), a double-stranded RNA virus belonging to the Birnaviridae family, causes immunosuppression in chickens. In this study, we defined the localization of IBDV replication complexes based on colocalization analysis of VP3, the major protein component of IBDV ribonucleoproteins (RNPs). Our results indicate that VP3 localizes to vesicular structures bearing features of early and late endocytic compartments located in the juxtanuclear region. Interfering with the endocytic pathway with a dominant negative version of Rab5 after the internalization step leads to a reduction in virus titer. Triple-immunostaining studies between VP3, the viral RNA-dependent RNA polymerase VP1, and viral double-stranded RNA (dsRNA) showed a well-defined colocalization, indicating that the three critical components of the RNPs colocalize in the same structure, likely representing replication complexes. Interestingly, recombinant expressed VP3 also localizes to endosomes. Employing Golgi markers, we found that VP3-containing vesicles were closely associated with this organelle. Depolymerization of microtubules with nocodazole caused a profound change in VP3 localization, showing a punctate distribution scattered throughout the cytoplasm. However, these VP3-positive structures remained associated with Golgi ministacks. Similarly, brefeldin A (BFA) treatment led to a punctate distribution of VP3, scattered throughout the cytoplasm of infected cells. In addition, analysis of intra- and extracellular viral infective particles after BFA treatment of avian cells suggested a role for the Golgi complex in viral assembly. These results constitute the first study elucidating the localization of IBDV replication complexes (i.e., in endocytic compartments) and establishing a role for the Golgi apparatus in the assembly step of a birnavirus.Fil: Delgui, Laura Ruth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; ArgentinaFil: Rodriguez, José F.. Consejo Superior de Investigaciones Cientificas. Centro Nacional de Biotecnologia; EspañaFil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina; Argentina; ArgentinaAmerican Society For Microbiology2013-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10075Delgui, Laura Ruth; Rodriguez, José F.; Colombo, Maria Isabel; The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.; American Society For Microbiology; Journal Of Virology; 87; 16; 8-2013; 8993-90070022-538Xenginfo:eu-repo/semantics/altIdentifier/url/http://jvi.asm.org/content/87/16/8993info:eu-repo/semantics/altIdentifier/doi/10.1128/JVI.03152-12info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:34Zoai:ri.conicet.gov.ar:11336/10075instacron: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 09:59:34.878CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
title The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
spellingShingle The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
Delgui, Laura Ruth
Ibdv
Virus
Endocytosis
Golgi
title_short The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
title_full The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
title_fullStr The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
title_full_unstemmed The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
title_sort The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.
dc.creator.none.fl_str_mv Delgui, Laura Ruth
Rodriguez, José F.
Colombo, Maria Isabel
author Delgui, Laura Ruth
author_facet Delgui, Laura Ruth
Rodriguez, José F.
Colombo, Maria Isabel
author_role author
author2 Rodriguez, José F.
Colombo, Maria Isabel
author2_role author
author
dc.subject.none.fl_str_mv Ibdv
Virus
Endocytosis
Golgi
topic Ibdv
Virus
Endocytosis
Golgi
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Infectious bursal disease virus (IBDV), a double-stranded RNA virus belonging to the Birnaviridae family, causes immunosuppression in chickens. In this study, we defined the localization of IBDV replication complexes based on colocalization analysis of VP3, the major protein component of IBDV ribonucleoproteins (RNPs). Our results indicate that VP3 localizes to vesicular structures bearing features of early and late endocytic compartments located in the juxtanuclear region. Interfering with the endocytic pathway with a dominant negative version of Rab5 after the internalization step leads to a reduction in virus titer. Triple-immunostaining studies between VP3, the viral RNA-dependent RNA polymerase VP1, and viral double-stranded RNA (dsRNA) showed a well-defined colocalization, indicating that the three critical components of the RNPs colocalize in the same structure, likely representing replication complexes. Interestingly, recombinant expressed VP3 also localizes to endosomes. Employing Golgi markers, we found that VP3-containing vesicles were closely associated with this organelle. Depolymerization of microtubules with nocodazole caused a profound change in VP3 localization, showing a punctate distribution scattered throughout the cytoplasm. However, these VP3-positive structures remained associated with Golgi ministacks. Similarly, brefeldin A (BFA) treatment led to a punctate distribution of VP3, scattered throughout the cytoplasm of infected cells. In addition, analysis of intra- and extracellular viral infective particles after BFA treatment of avian cells suggested a role for the Golgi complex in viral assembly. These results constitute the first study elucidating the localization of IBDV replication complexes (i.e., in endocytic compartments) and establishing a role for the Golgi apparatus in the assembly step of a birnavirus.
Fil: Delgui, Laura Ruth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: Rodriguez, José F.. Consejo Superior de Investigaciones Cientificas. Centro Nacional de Biotecnologia; España
Fil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina; Argentina; Argentina
description Infectious bursal disease virus (IBDV), a double-stranded RNA virus belonging to the Birnaviridae family, causes immunosuppression in chickens. In this study, we defined the localization of IBDV replication complexes based on colocalization analysis of VP3, the major protein component of IBDV ribonucleoproteins (RNPs). Our results indicate that VP3 localizes to vesicular structures bearing features of early and late endocytic compartments located in the juxtanuclear region. Interfering with the endocytic pathway with a dominant negative version of Rab5 after the internalization step leads to a reduction in virus titer. Triple-immunostaining studies between VP3, the viral RNA-dependent RNA polymerase VP1, and viral double-stranded RNA (dsRNA) showed a well-defined colocalization, indicating that the three critical components of the RNPs colocalize in the same structure, likely representing replication complexes. Interestingly, recombinant expressed VP3 also localizes to endosomes. Employing Golgi markers, we found that VP3-containing vesicles were closely associated with this organelle. Depolymerization of microtubules with nocodazole caused a profound change in VP3 localization, showing a punctate distribution scattered throughout the cytoplasm. However, these VP3-positive structures remained associated with Golgi ministacks. Similarly, brefeldin A (BFA) treatment led to a punctate distribution of VP3, scattered throughout the cytoplasm of infected cells. In addition, analysis of intra- and extracellular viral infective particles after BFA treatment of avian cells suggested a role for the Golgi complex in viral assembly. These results constitute the first study elucidating the localization of IBDV replication complexes (i.e., in endocytic compartments) and establishing a role for the Golgi apparatus in the assembly step of a birnavirus.
publishDate 2013
dc.date.none.fl_str_mv 2013-08
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/11336/10075
Delgui, Laura Ruth; Rodriguez, José F.; Colombo, Maria Isabel; The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.; American Society For Microbiology; Journal Of Virology; 87; 16; 8-2013; 8993-9007
0022-538X
url http://hdl.handle.net/11336/10075
identifier_str_mv Delgui, Laura Ruth; Rodriguez, José F.; Colombo, Maria Isabel; The endosomal pathway and the Golgi complex are involved in the Infectious bursal disease virus life cycle.; American Society For Microbiology; Journal Of Virology; 87; 16; 8-2013; 8993-9007
0022-538X
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://jvi.asm.org/content/87/16/8993
info:eu-repo/semantics/altIdentifier/doi/10.1128/JVI.03152-12
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 American Society For Microbiology
publisher.none.fl_str_mv American Society For Microbiology
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 13.11938

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