The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/29603 http://dx.doi.org/10.1111/j.1462-5822.2006.00838.x |
Resumo: | The etiologic agent of Q fever Coxiella burnetii, is an intracellular obligate parasite that develops large vacuoles with phagolysosomal characteristics, containing multiple replicating bacteria. We have previously shown that Phase II C. burnetii replicative vacuoles generated after 24-48 h post infection are decorated with the autophagic protein LC3. the aim of the present study was to examine, at earlier stages of infection, the distribution and roles of the small GTPases Rab5 and Rab7, markers of early and late endosomes respectively, as well as of the protein LC3 on C. burnetii trafficking. Our results indicate that: (i) Coxiella phagosomes (Cph) acquire the two Rab proteins sequentially during infection; (ii) overexpression of a dominant negative mutant form of Rab5, but not of Rab7, impaired Coxiella entry, whereas both Rab5 and Rab7 dominant negative mutants inhibited vacuole formation; (iii) Cph colocalized with the protein LC3 as early as 5 min after infection; acquisition of this protein appeared to be a bacterially driven process, because it was inhibited by the bacteriostatic antibiotic chloramphenicol and (iv) C. burnetii delayed the arrival of the typical lysosomal protease cathepsin D to the Cph, which delay is further increased by starvation-induced autophagy. Based on our results we propose that C. burnetii transits through the normal endo/phagocytic pathway but actively interacts with autophagosomes at early times after infection. This intersection with the autophagic pathway delays fusion with the lysosomal compartment possibly favouring the intracellular differentiation and survival of the bacteria. |
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Romano, Patricia S.Gutierrez, Maximiliano G.Beron, WalterRabinovitch, Michel [UNIFESP]Colombo, Maria I.Univ Nacl CuyoUniversidade Federal de São Paulo (UNIFESP)2016-01-24T12:42:00Z2016-01-24T12:42:00Z2007-04-01Cellular Microbiology. Oxford: Blackwell Publishing, v. 9, n. 4, p. 891-909, 2007.1462-5814http://repositorio.unifesp.br/handle/11600/29603http://dx.doi.org/10.1111/j.1462-5822.2006.00838.x10.1111/j.1462-5822.2006.00838.xWOS:000244881900008The etiologic agent of Q fever Coxiella burnetii, is an intracellular obligate parasite that develops large vacuoles with phagolysosomal characteristics, containing multiple replicating bacteria. We have previously shown that Phase II C. burnetii replicative vacuoles generated after 24-48 h post infection are decorated with the autophagic protein LC3. the aim of the present study was to examine, at earlier stages of infection, the distribution and roles of the small GTPases Rab5 and Rab7, markers of early and late endosomes respectively, as well as of the protein LC3 on C. burnetii trafficking. Our results indicate that: (i) Coxiella phagosomes (Cph) acquire the two Rab proteins sequentially during infection; (ii) overexpression of a dominant negative mutant form of Rab5, but not of Rab7, impaired Coxiella entry, whereas both Rab5 and Rab7 dominant negative mutants inhibited vacuole formation; (iii) Cph colocalized with the protein LC3 as early as 5 min after infection; acquisition of this protein appeared to be a bacterially driven process, because it was inhibited by the bacteriostatic antibiotic chloramphenicol and (iv) C. burnetii delayed the arrival of the typical lysosomal protease cathepsin D to the Cph, which delay is further increased by starvation-induced autophagy. Based on our results we propose that C. burnetii transits through the normal endo/phagocytic pathway but actively interacts with autophagosomes at early times after infection. This intersection with the autophagic pathway delays fusion with the lysosomal compartment possibly favouring the intracellular differentiation and survival of the bacteria.Univ Nacl Cuyo, Lab Biol Celular & Mol, CONICET, IHEM,Fac Ciencias Med, RA-5500 Mendoza, ArgentinaUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, Escola Paulista Med, São Paulo, BrazilUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, Escola Paulista Med, São Paulo, BrazilWeb of Science891-909engBlackwell PublishingCellular MicrobiologyThe autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cellinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/296032022-09-27 09:48:37.479metadata only accessoai:repositorio.unifesp.br:11600/29603Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-09-27T12:48:37Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
title |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
spellingShingle |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell Romano, Patricia S. |
title_short |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
title_full |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
title_fullStr |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
title_full_unstemmed |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
title_sort |
The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell |
author |
Romano, Patricia S. |
author_facet |
Romano, Patricia S. Gutierrez, Maximiliano G. Beron, Walter Rabinovitch, Michel [UNIFESP] Colombo, Maria I. |
author_role |
author |
author2 |
Gutierrez, Maximiliano G. Beron, Walter Rabinovitch, Michel [UNIFESP] Colombo, Maria I. |
author2_role |
author author author author |
dc.contributor.institution.none.fl_str_mv |
Univ Nacl Cuyo Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Romano, Patricia S. Gutierrez, Maximiliano G. Beron, Walter Rabinovitch, Michel [UNIFESP] Colombo, Maria I. |
description |
The etiologic agent of Q fever Coxiella burnetii, is an intracellular obligate parasite that develops large vacuoles with phagolysosomal characteristics, containing multiple replicating bacteria. We have previously shown that Phase II C. burnetii replicative vacuoles generated after 24-48 h post infection are decorated with the autophagic protein LC3. the aim of the present study was to examine, at earlier stages of infection, the distribution and roles of the small GTPases Rab5 and Rab7, markers of early and late endosomes respectively, as well as of the protein LC3 on C. burnetii trafficking. Our results indicate that: (i) Coxiella phagosomes (Cph) acquire the two Rab proteins sequentially during infection; (ii) overexpression of a dominant negative mutant form of Rab5, but not of Rab7, impaired Coxiella entry, whereas both Rab5 and Rab7 dominant negative mutants inhibited vacuole formation; (iii) Cph colocalized with the protein LC3 as early as 5 min after infection; acquisition of this protein appeared to be a bacterially driven process, because it was inhibited by the bacteriostatic antibiotic chloramphenicol and (iv) C. burnetii delayed the arrival of the typical lysosomal protease cathepsin D to the Cph, which delay is further increased by starvation-induced autophagy. Based on our results we propose that C. burnetii transits through the normal endo/phagocytic pathway but actively interacts with autophagosomes at early times after infection. This intersection with the autophagic pathway delays fusion with the lysosomal compartment possibly favouring the intracellular differentiation and survival of the bacteria. |
publishDate |
2007 |
dc.date.issued.fl_str_mv |
2007-04-01 |
dc.date.accessioned.fl_str_mv |
2016-01-24T12:42:00Z |
dc.date.available.fl_str_mv |
2016-01-24T12:42:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Cellular Microbiology. Oxford: Blackwell Publishing, v. 9, n. 4, p. 891-909, 2007. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/29603 http://dx.doi.org/10.1111/j.1462-5822.2006.00838.x |
dc.identifier.issn.none.fl_str_mv |
1462-5814 |
dc.identifier.doi.none.fl_str_mv |
10.1111/j.1462-5822.2006.00838.x |
dc.identifier.wos.none.fl_str_mv |
WOS:000244881900008 |
identifier_str_mv |
Cellular Microbiology. Oxford: Blackwell Publishing, v. 9, n. 4, p. 891-909, 2007. 1462-5814 10.1111/j.1462-5822.2006.00838.x WOS:000244881900008 |
url |
http://repositorio.unifesp.br/handle/11600/29603 http://dx.doi.org/10.1111/j.1462-5822.2006.00838.x |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Cellular Microbiology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
891-909 |
dc.publisher.none.fl_str_mv |
Blackwell Publishing |
publisher.none.fl_str_mv |
Blackwell Publishing |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
_version_ |
1802764164861526016 |