The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52

Autores
Furtado, Ana Rita; Essid, Miriam; Perrinet, Stéphenie; Balaña, Maria Eugenia; Yoder, Nicholas; Dehoux, Pierre; Subtil, Agathe
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Chlamydia are obligate intracellular pathogens. Upon contact with the host, they use type III secretion to deliver proteins into the cell, thereby triggering actin-dependent entry and establishing the infection. We observed that Chlamydia caviae elicited a local and transient accumulation of ubiquitinated proteins at the entry sites, which disappeared within 20 min. We investigated the mechanism for the rapid clearance of ubiquitin. We showed that the OTU-like domain containing protein CCA00261, predicted to have deubiquitinase activity, was detected in infectious particles and was a type III secretion effector. This protein is present in several Chlamydia strains, including the human pathogen Chlamydia pneumoniae, and we further designate it as ChlaOTU. We demonstrated that ChlaOTU bound ubiquitin and NDP52, and we mapped these interactions to distinct domains. NDP52 was recruited to Chlamydia entry sites and was dispensable for infection and for bacterial growth. ChlaOTU functioned as a deubiquitinase in vitro. Heterologousexpression of ChlaOTU reduced ubiquitin accumulation at the entry sites, while a catalytic mutant of the deubiquitinase activity had the opposite effect. Altogether, we have identified a novel secreted protein of chlamydiae. ChlaOTU targets both ubiquitin and NDP52 and likely participates in the clearance of ubiquitin at the invasion sites.
Fil: Furtado, Ana Rita. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Fil: Essid, Miriam. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Fil: Perrinet, Stéphenie. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Fil: Balaña, Maria Eugenia. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencias y Tecnología "Dr. Cesar Milstein"; Argentina
Fil: Yoder, Nicholas. Nine Cambridge Center. Whitehead Institute for Biomedical Research; Estados Unidos
Fil: Dehoux, Pierre. Institut Pasteur. Plateforme Intégration et Analyse Génomique; Francia
Fil: Subtil, Agathe. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Materia
Chlamydia
Ubiquitin
Invasion Sites
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:11336/4027
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/4027
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52Furtado, Ana RitaEssid, MiriamPerrinet, StéphenieBalaña, Maria EugeniaYoder, NicholasDehoux, PierreSubtil, AgatheChlamydiaUbiquitinInvasion Siteshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Chlamydia are obligate intracellular pathogens. Upon contact with the host, they use type III secretion to deliver proteins into the cell, thereby triggering actin-dependent entry and establishing the infection. We observed that Chlamydia caviae elicited a local and transient accumulation of ubiquitinated proteins at the entry sites, which disappeared within 20 min. We investigated the mechanism for the rapid clearance of ubiquitin. We showed that the OTU-like domain containing protein CCA00261, predicted to have deubiquitinase activity, was detected in infectious particles and was a type III secretion effector. This protein is present in several Chlamydia strains, including the human pathogen Chlamydia pneumoniae, and we further designate it as ChlaOTU. We demonstrated that ChlaOTU bound ubiquitin and NDP52, and we mapped these interactions to distinct domains. NDP52 was recruited to Chlamydia entry sites and was dispensable for infection and for bacterial growth. ChlaOTU functioned as a deubiquitinase in vitro. Heterologousexpression of ChlaOTU reduced ubiquitin accumulation at the entry sites, while a catalytic mutant of the deubiquitinase activity had the opposite effect. Altogether, we have identified a novel secreted protein of chlamydiae. ChlaOTU targets both ubiquitin and NDP52 and likely participates in the clearance of ubiquitin at the invasion sites.Fil: Furtado, Ana Rita. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; FranciaFil: Essid, Miriam. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; FranciaFil: Perrinet, Stéphenie. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; FranciaFil: Balaña, Maria Eugenia. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencias y Tecnología "Dr. Cesar Milstein"; ArgentinaFil: Yoder, Nicholas. Nine Cambridge Center. Whitehead Institute for Biomedical Research; Estados UnidosFil: Dehoux, Pierre. Institut Pasteur. Plateforme Intégration et Analyse Génomique; FranciaFil: Subtil, Agathe. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; FranciaWiley2013-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4027Furtado, Ana Rita; Essid, Miriam; Perrinet, Stéphenie; Balaña, Maria Eugenia; Yoder, Nicholas; et al.; The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52; Wiley; Cellular Microbiology (print); 15; 12; 8-2013; 2064–20791462-5814enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/cmi.12171/abstractinfo:eu-repo/semantics/altIdentifier/doi/DOI:10.1111/cmi.12171info:eu-repo/semantics/altIdentifier/issn/1462-5814info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:08:31Zoai:ri.conicet.gov.ar:11336/4027instacron: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 13:08:31.656CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
title The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
spellingShingle The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
Furtado, Ana Rita
Chlamydia
Ubiquitin
Invasion Sites
title_short The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
title_full The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
title_fullStr The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
title_full_unstemmed The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
title_sort The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52
dc.creator.none.fl_str_mv Furtado, Ana Rita
Essid, Miriam
Perrinet, Stéphenie
Balaña, Maria Eugenia
Yoder, Nicholas
Dehoux, Pierre
Subtil, Agathe
author Furtado, Ana Rita
author_facet Furtado, Ana Rita
Essid, Miriam
Perrinet, Stéphenie
Balaña, Maria Eugenia
Yoder, Nicholas
Dehoux, Pierre
Subtil, Agathe
author_role author
author2 Essid, Miriam
Perrinet, Stéphenie
Balaña, Maria Eugenia
Yoder, Nicholas
Dehoux, Pierre
Subtil, Agathe
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Chlamydia
Ubiquitin
Invasion Sites
topic Chlamydia
Ubiquitin
Invasion Sites
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 are obligate intracellular pathogens. Upon contact with the host, they use type III secretion to deliver proteins into the cell, thereby triggering actin-dependent entry and establishing the infection. We observed that Chlamydia caviae elicited a local and transient accumulation of ubiquitinated proteins at the entry sites, which disappeared within 20 min. We investigated the mechanism for the rapid clearance of ubiquitin. We showed that the OTU-like domain containing protein CCA00261, predicted to have deubiquitinase activity, was detected in infectious particles and was a type III secretion effector. This protein is present in several Chlamydia strains, including the human pathogen Chlamydia pneumoniae, and we further designate it as ChlaOTU. We demonstrated that ChlaOTU bound ubiquitin and NDP52, and we mapped these interactions to distinct domains. NDP52 was recruited to Chlamydia entry sites and was dispensable for infection and for bacterial growth. ChlaOTU functioned as a deubiquitinase in vitro. Heterologousexpression of ChlaOTU reduced ubiquitin accumulation at the entry sites, while a catalytic mutant of the deubiquitinase activity had the opposite effect. Altogether, we have identified a novel secreted protein of chlamydiae. ChlaOTU targets both ubiquitin and NDP52 and likely participates in the clearance of ubiquitin at the invasion sites.
Fil: Furtado, Ana Rita. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Fil: Essid, Miriam. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Fil: Perrinet, Stéphenie. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
Fil: Balaña, Maria Eugenia. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Ciencias y Tecnología "Dr. Cesar Milstein"; Argentina
Fil: Yoder, Nicholas. Nine Cambridge Center. Whitehead Institute for Biomedical Research; Estados Unidos
Fil: Dehoux, Pierre. Institut Pasteur. Plateforme Intégration et Analyse Génomique; Francia
Fil: Subtil, Agathe. Institut Pasteur. Unité de Biologie des Interactions Cellulaires; Francia
description Chlamydia are obligate intracellular pathogens. Upon contact with the host, they use type III secretion to deliver proteins into the cell, thereby triggering actin-dependent entry and establishing the infection. We observed that Chlamydia caviae elicited a local and transient accumulation of ubiquitinated proteins at the entry sites, which disappeared within 20 min. We investigated the mechanism for the rapid clearance of ubiquitin. We showed that the OTU-like domain containing protein CCA00261, predicted to have deubiquitinase activity, was detected in infectious particles and was a type III secretion effector. This protein is present in several Chlamydia strains, including the human pathogen Chlamydia pneumoniae, and we further designate it as ChlaOTU. We demonstrated that ChlaOTU bound ubiquitin and NDP52, and we mapped these interactions to distinct domains. NDP52 was recruited to Chlamydia entry sites and was dispensable for infection and for bacterial growth. ChlaOTU functioned as a deubiquitinase in vitro. Heterologousexpression of ChlaOTU reduced ubiquitin accumulation at the entry sites, while a catalytic mutant of the deubiquitinase activity had the opposite effect. Altogether, we have identified a novel secreted protein of chlamydiae. ChlaOTU targets both ubiquitin and NDP52 and likely participates in the clearance of ubiquitin at the invasion sites.
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/11336/4027
Furtado, Ana Rita; Essid, Miriam; Perrinet, Stéphenie; Balaña, Maria Eugenia; Yoder, Nicholas; et al.; The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52; Wiley; Cellular Microbiology (print); 15; 12; 8-2013; 2064–2079
1462-5814
url http://hdl.handle.net/11336/4027
identifier_str_mv Furtado, Ana Rita; Essid, Miriam; Perrinet, Stéphenie; Balaña, Maria Eugenia; Yoder, Nicholas; et al.; The chlamydial OTU domain-containing protein ChlaOTU is an early type III secretion effector targeting ubiquitin and NDP52; Wiley; Cellular Microbiology (print); 15; 12; 8-2013; 2064–2079
1462-5814
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/cmi.12171/abstract
info:eu-repo/semantics/altIdentifier/doi/DOI:10.1111/cmi.12171
info:eu-repo/semantics/altIdentifier/issn/1462-5814
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 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 12.993085

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