Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages

Autores
Vazquez, Cristina Lourdes; Bianco, María Veronica; Blanco, Federico Carlos; Forrellad, Marina Andrea; Gutierrez, Maximiliano Gabriel; Bigi, Fabiana
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Mycobacterium bovis causes tuberculosis in a wide variety of mammals, with strong tropism for cattle and eventually humans. P27, also called LprG, is among the proteins involved in the mechanisms of the virulence and persistence of M. bovis and Mycobacterium tuberculosis. Here, we describe a novel function of P27 in the interaction of M. bovis with its natural host cell, the bovine macrophage. We found that a deletion in the p27-p55 operon impairs the replication of M. bovis in bovine macrophages. Importantly, we show for the first time that M. bovis arrests phagosome maturation in a process that depends on P27. This effect is P27 specific since complementation with wild-type p27 but not p55 fully restored the wild-type phenotype of the mutant strain; this indicates that P55 plays no important role during the early events of M. bovis infection. In addition, we also showed that the presence of P27 from M. smegmatis decreases the association of LAMP-3 with bead phagosomes, indicating that P27 itself blocks phagosome-lysosome fusion by modulating the traffic machinery in the cell host.
Instituto de Biotecnología
Fil: Vazquez, Cristina Lourdes. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Bianco, María Veronica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Blanco, Federico Carlos. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Forrellad, Marina Andrea. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Gutierrez, Maximiliano Gabriel. The Francis Crick Institute, Host-Pathogen Interactions in Tuberculosis Laboratory; Reino Unido
Fil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fuente
Infection and immunity 85 (3): e00720-16. (2017 Mar.)
Materia
Mycobacterium Bovis
Enfermedades de los Animales
Tuberculosis
Macrofagos
Ganado Bovino
Animal Diseases
Macrophages
Cattle
LprG
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/552
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spelling Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophagesVazquez, Cristina LourdesBianco, María VeronicaBlanco, Federico CarlosForrellad, Marina AndreaGutierrez, Maximiliano GabrielBigi, FabianaMycobacterium BovisEnfermedades de los AnimalesTuberculosisMacrofagosGanado BovinoAnimal DiseasesMacrophagesCattleLprGMycobacterium bovis causes tuberculosis in a wide variety of mammals, with strong tropism for cattle and eventually humans. P27, also called LprG, is among the proteins involved in the mechanisms of the virulence and persistence of M. bovis and Mycobacterium tuberculosis. Here, we describe a novel function of P27 in the interaction of M. bovis with its natural host cell, the bovine macrophage. We found that a deletion in the p27-p55 operon impairs the replication of M. bovis in bovine macrophages. Importantly, we show for the first time that M. bovis arrests phagosome maturation in a process that depends on P27. This effect is P27 specific since complementation with wild-type p27 but not p55 fully restored the wild-type phenotype of the mutant strain; this indicates that P55 plays no important role during the early events of M. bovis infection. In addition, we also showed that the presence of P27 from M. smegmatis decreases the association of LAMP-3 with bead phagosomes, indicating that P27 itself blocks phagosome-lysosome fusion by modulating the traffic machinery in the cell host.Instituto de BiotecnologíaFil: Vazquez, Cristina Lourdes. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Bianco, María Veronica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Blanco, Federico Carlos. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Forrellad, Marina Andrea. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Gutierrez, Maximiliano Gabriel. The Francis Crick Institute, Host-Pathogen Interactions in Tuberculosis Laboratory; Reino UnidoFil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina2017-07-04T15:15:21Z2017-07-04T15:15:21Z2017-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/552http://iai.asm.org/content/85/3/e00720-16.full.pdf+htmlhttps://doi.org/10.1128/IAI.00720-16Infection and immunity 85 (3): e00720-16. (2017 Mar.)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-10-23T11:16:18Zoai:localhost:20.500.12123/552instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-23 11:16:18.613INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
title Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
spellingShingle Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
Vazquez, Cristina Lourdes
Mycobacterium Bovis
Enfermedades de los Animales
Tuberculosis
Macrofagos
Ganado Bovino
Animal Diseases
Macrophages
Cattle
LprG
title_short Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
title_full Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
title_fullStr Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
title_full_unstemmed Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
title_sort Mycobacterium bovis requires P27 (LprG) to arrest phagosome maturation and replicate within bovine macrophages
dc.creator.none.fl_str_mv Vazquez, Cristina Lourdes
Bianco, María Veronica
Blanco, Federico Carlos
Forrellad, Marina Andrea
Gutierrez, Maximiliano Gabriel
Bigi, Fabiana
author Vazquez, Cristina Lourdes
author_facet Vazquez, Cristina Lourdes
Bianco, María Veronica
Blanco, Federico Carlos
Forrellad, Marina Andrea
Gutierrez, Maximiliano Gabriel
Bigi, Fabiana
author_role author
author2 Bianco, María Veronica
Blanco, Federico Carlos
Forrellad, Marina Andrea
Gutierrez, Maximiliano Gabriel
Bigi, Fabiana
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Mycobacterium Bovis
Enfermedades de los Animales
Tuberculosis
Macrofagos
Ganado Bovino
Animal Diseases
Macrophages
Cattle
LprG
topic Mycobacterium Bovis
Enfermedades de los Animales
Tuberculosis
Macrofagos
Ganado Bovino
Animal Diseases
Macrophages
Cattle
LprG
dc.description.none.fl_txt_mv Mycobacterium bovis causes tuberculosis in a wide variety of mammals, with strong tropism for cattle and eventually humans. P27, also called LprG, is among the proteins involved in the mechanisms of the virulence and persistence of M. bovis and Mycobacterium tuberculosis. Here, we describe a novel function of P27 in the interaction of M. bovis with its natural host cell, the bovine macrophage. We found that a deletion in the p27-p55 operon impairs the replication of M. bovis in bovine macrophages. Importantly, we show for the first time that M. bovis arrests phagosome maturation in a process that depends on P27. This effect is P27 specific since complementation with wild-type p27 but not p55 fully restored the wild-type phenotype of the mutant strain; this indicates that P55 plays no important role during the early events of M. bovis infection. In addition, we also showed that the presence of P27 from M. smegmatis decreases the association of LAMP-3 with bead phagosomes, indicating that P27 itself blocks phagosome-lysosome fusion by modulating the traffic machinery in the cell host.
Instituto de Biotecnología
Fil: Vazquez, Cristina Lourdes. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Bianco, María Veronica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Blanco, Federico Carlos. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Forrellad, Marina Andrea. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Gutierrez, Maximiliano Gabriel. The Francis Crick Institute, Host-Pathogen Interactions in Tuberculosis Laboratory; Reino Unido
Fil: Bigi, Fabiana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
description Mycobacterium bovis causes tuberculosis in a wide variety of mammals, with strong tropism for cattle and eventually humans. P27, also called LprG, is among the proteins involved in the mechanisms of the virulence and persistence of M. bovis and Mycobacterium tuberculosis. Here, we describe a novel function of P27 in the interaction of M. bovis with its natural host cell, the bovine macrophage. We found that a deletion in the p27-p55 operon impairs the replication of M. bovis in bovine macrophages. Importantly, we show for the first time that M. bovis arrests phagosome maturation in a process that depends on P27. This effect is P27 specific since complementation with wild-type p27 but not p55 fully restored the wild-type phenotype of the mutant strain; this indicates that P55 plays no important role during the early events of M. bovis infection. In addition, we also showed that the presence of P27 from M. smegmatis decreases the association of LAMP-3 with bead phagosomes, indicating that P27 itself blocks phagosome-lysosome fusion by modulating the traffic machinery in the cell host.
publishDate 2017
dc.date.none.fl_str_mv 2017-07-04T15:15:21Z
2017-07-04T15:15:21Z
2017-03
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/20.500.12123/552
http://iai.asm.org/content/85/3/e00720-16.full.pdf+html
https://doi.org/10.1128/IAI.00720-16
url http://hdl.handle.net/20.500.12123/552
http://iai.asm.org/content/85/3/e00720-16.full.pdf+html
https://doi.org/10.1128/IAI.00720-16
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Infection and immunity 85 (3): e00720-16. (2017 Mar.)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.982451

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