Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication

Autores
Leiva, Natalia Lorena; Capmany, Anahi; Damiani, Maria Teresa
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Chlamydia trachomatis, an obligate intracellular pathogen, survives within host cells in a special compartment named ‘inclusion’ and takes advantage of host vesicular transport pathways for its growth and replication. Rab GTPases are key regulatory proteins of intracellular trafficking. Several Rabs, among them Rab11 and Rab14, are implicated in chlamydial development. FIP2, a member of the Rab11-Family of Interacting Proteins, presents at the C-terminus a Rab-binding domain that interacts with both Rab11 and Rab14. In this study, we determined and characterized the recruitment of endogenous and GFP-tagged FIP2 to the chlamydial inclusions. The recruitment of FIP2 is specific since other members of the Rab11- Family of Interacting Proteins do not associate with the chlamydial inclusions. The Rab-binding domain of FIP2 is essential for its association. Our results indicate that FIP2 binds to Rab11 at the chlamydial inclusion membrane through its Rabbinding domain. The presence of FIP2 at the chlamydial inclusion favours the recruitment of Rab14. Furthermore, our results show that FIP2 promotes inclusion development and bacterial replication. In agreement, the silencing of FIP2 decreases the bacterial progeny. C. trachomatis likely recruits FIP2 to hijack host intracellular traf- ficking to redirect vesicles full of nutrients towards the inclusion.
Fil: Leiva, Natalia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina
Fil: Capmany, Anahi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina
Fil: Damiani, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina
Materia
Fip2
Chlamydia Trachomatis
Intracellular Transport
Chlamydial Inclusions
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:11336/10173
Acceder
id CONICETDig_652adc2b35be94465939c23b512df9e4
oai_identifier_str oai:ri.conicet.gov.ar:11336/10173
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplicationLeiva, Natalia LorenaCapmany, AnahiDamiani, Maria TeresaFip2Chlamydia TrachomatisIntracellular TransportChlamydial Inclusionshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Chlamydia trachomatis, an obligate intracellular pathogen, survives within host cells in a special compartment named ‘inclusion’ and takes advantage of host vesicular transport pathways for its growth and replication. Rab GTPases are key regulatory proteins of intracellular trafficking. Several Rabs, among them Rab11 and Rab14, are implicated in chlamydial development. FIP2, a member of the Rab11-Family of Interacting Proteins, presents at the C-terminus a Rab-binding domain that interacts with both Rab11 and Rab14. In this study, we determined and characterized the recruitment of endogenous and GFP-tagged FIP2 to the chlamydial inclusions. The recruitment of FIP2 is specific since other members of the Rab11- Family of Interacting Proteins do not associate with the chlamydial inclusions. The Rab-binding domain of FIP2 is essential for its association. Our results indicate that FIP2 binds to Rab11 at the chlamydial inclusion membrane through its Rabbinding domain. The presence of FIP2 at the chlamydial inclusion favours the recruitment of Rab14. Furthermore, our results show that FIP2 promotes inclusion development and bacterial replication. In agreement, the silencing of FIP2 decreases the bacterial progeny. C. trachomatis likely recruits FIP2 to hijack host intracellular traf- ficking to redirect vesicles full of nutrients towards the inclusion.Fil: Leiva, Natalia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; ArgentinaFil: Capmany, Anahi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; ArgentinaFil: Damiani, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; ArgentinaWiley2012-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10173Leiva, Natalia Lorena; Capmany, Anahi; Damiani, Maria Teresa; Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication; Wiley; Cellular Microbiology; 15; 1; 1-11-2012; 114-1291462-5814enginfo:eu-repo/semantics/altIdentifier/doi/10.1111/cmi.12035info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/cmi.12035/abstractinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:23:44Zoai:ri.conicet.gov.ar:11336/10173instacron: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:34982025-09-10 13:23:44.814CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
title Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
spellingShingle Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
Leiva, Natalia Lorena
Fip2
Chlamydia Trachomatis
Intracellular Transport
Chlamydial Inclusions
title_short Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
title_full Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
title_fullStr Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
title_full_unstemmed Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
title_sort Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication
dc.creator.none.fl_str_mv Leiva, Natalia Lorena
Capmany, Anahi
Damiani, Maria Teresa
author Leiva, Natalia Lorena
author_facet Leiva, Natalia Lorena
Capmany, Anahi
Damiani, Maria Teresa
author_role author
author2 Capmany, Anahi
Damiani, Maria Teresa
author2_role author
author
dc.subject.none.fl_str_mv Fip2
Chlamydia Trachomatis
Intracellular Transport
Chlamydial Inclusions
topic Fip2
Chlamydia Trachomatis
Intracellular Transport
Chlamydial Inclusions
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Chlamydia trachomatis, an obligate intracellular pathogen, survives within host cells in a special compartment named ‘inclusion’ and takes advantage of host vesicular transport pathways for its growth and replication. Rab GTPases are key regulatory proteins of intracellular trafficking. Several Rabs, among them Rab11 and Rab14, are implicated in chlamydial development. FIP2, a member of the Rab11-Family of Interacting Proteins, presents at the C-terminus a Rab-binding domain that interacts with both Rab11 and Rab14. In this study, we determined and characterized the recruitment of endogenous and GFP-tagged FIP2 to the chlamydial inclusions. The recruitment of FIP2 is specific since other members of the Rab11- Family of Interacting Proteins do not associate with the chlamydial inclusions. The Rab-binding domain of FIP2 is essential for its association. Our results indicate that FIP2 binds to Rab11 at the chlamydial inclusion membrane through its Rabbinding domain. The presence of FIP2 at the chlamydial inclusion favours the recruitment of Rab14. Furthermore, our results show that FIP2 promotes inclusion development and bacterial replication. In agreement, the silencing of FIP2 decreases the bacterial progeny. C. trachomatis likely recruits FIP2 to hijack host intracellular traf- ficking to redirect vesicles full of nutrients towards the inclusion.
Fil: Leiva, Natalia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina
Fil: Capmany, Anahi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina
Fil: Damiani, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto Histologia y Embriología de Mendoza "Dr. M. Burgos"; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina
description Chlamydia trachomatis, an obligate intracellular pathogen, survives within host cells in a special compartment named ‘inclusion’ and takes advantage of host vesicular transport pathways for its growth and replication. Rab GTPases are key regulatory proteins of intracellular trafficking. Several Rabs, among them Rab11 and Rab14, are implicated in chlamydial development. FIP2, a member of the Rab11-Family of Interacting Proteins, presents at the C-terminus a Rab-binding domain that interacts with both Rab11 and Rab14. In this study, we determined and characterized the recruitment of endogenous and GFP-tagged FIP2 to the chlamydial inclusions. The recruitment of FIP2 is specific since other members of the Rab11- Family of Interacting Proteins do not associate with the chlamydial inclusions. The Rab-binding domain of FIP2 is essential for its association. Our results indicate that FIP2 binds to Rab11 at the chlamydial inclusion membrane through its Rabbinding domain. The presence of FIP2 at the chlamydial inclusion favours the recruitment of Rab14. Furthermore, our results show that FIP2 promotes inclusion development and bacterial replication. In agreement, the silencing of FIP2 decreases the bacterial progeny. C. trachomatis likely recruits FIP2 to hijack host intracellular traf- ficking to redirect vesicles full of nutrients towards the inclusion.
publishDate 2012
dc.date.none.fl_str_mv 2012-11-01
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/11336/10173
Leiva, Natalia Lorena; Capmany, Anahi; Damiani, Maria Teresa; Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication; Wiley; Cellular Microbiology; 15; 1; 1-11-2012; 114-129
1462-5814
url http://hdl.handle.net/11336/10173
identifier_str_mv Leiva, Natalia Lorena; Capmany, Anahi; Damiani, Maria Teresa; Rab11-Family of Interacting Protein 2 associates with chlamydial inclusions through its Rab-binding domain and promotes bacterial multiplication; Wiley; Cellular Microbiology; 15; 1; 1-11-2012; 114-129
1462-5814
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/cmi.12035
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/cmi.12035/abstract
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
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
_version_ 1842981312785285120
score 12.48226

Publicaciones similares