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Autor | Fabrino, Daniela Leite | |
Autor | Bleck, Christopher K. E. | |
Autor | Anes, Elsa | |
Autor | Hasilik, Andrej | |
Autor | Melo, Rossana C. N. | |
Autor | Niederweis, Michael | |
Autor | Griffiths, Gareth | |
Autor | Gutierrez, Maximiliano Gabriel | |
Fecha de acceso | 2019-01-02T13:31:38Z | |
Fecha de disponibilización | 2019-01-02T13:31:38Z | |
Fecha de publicación | 2009 | |
Referencia | FABRINO, Daniela Leite; et al. Porins faciitate nitric oxide-mediated killing of mycobacteria. Microbes and Infection, v.11, p.868-875, 2009. | pt_BR |
ISSN | 1286-4579 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/30821 | |
Idioma | eng | pt_BR |
Editor | Elsevier | pt_BR |
Derechos de autor | restricted access | pt_BR |
Palabras clave en Portugués | Fagossomos | pt_BR |
Palabras clave en Portugués | Mycobacterium | pt_BR |
Palabras clave en Portugués | Porinas | pt_BR |
Título | Porins facilitate nitric oxide-mediated killing of mycobacteria | pt_BR |
Tipo del documento | Article | pt_BR |
DOI | 10.1016/j.micinf.2009.05.007 | |
Resumen en Inglés | Non-pathogenic mycobacteria such us Mycobacterium smegmatis reside in macrophages within phagosomes that fuse with late endocytic/lysosomal compartments. This sequential fusion process is required for the killing of non-pathogenic mycobacteria by macrophages. Porins are proteins that allow the influx of hydrophilic molecules across the mycobacterial outer membrane. Deletion of the porins MspA, MspC and MspD significantly increased survival of M. smegmatis in J774 macrophages. However, the mechanism underlying this observation is unknown. Internalization of wild-type M. smegmatis (SMR5) and the porin triple mutant (ML16) by macrophages was identical indicating that the viability of the porin mutant in vivo was enhanced. This was not due to effects on phagosome trafficking since fusion of phagosomes containing the mutant with late endocytic compartments was unaffected. Moreover, in ML16-infected macrophages, the generation of nitric oxide (NO) was similar to the wild type-infected cells. However, ML16 was significantly more resistant to the effects of NO in vitro compared to SMR5. Our data provide evidence that porins render mycobacteria vulnerable to killing by reactive nitrogen intermediates within phagosomes probably by facilitating uptake of NO across the mycobacterial outer membrane. | pt_BR |
Afiliación | European Molecular Biology Laboratory. Heidelberg, Germany / Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Imunologia. Laboratório de Bioquímica de Tripanossomatídeos. Rio de Janeiro, RJ, Brasil. | pt_BR |
Afiliación | European Molecular Biology Laboratory. Heidelberg, Germany, | pt_BR |
Afiliación | University of Lisbon. Faculty of Pharmacy. URIA-Centro de Patogénese Molecular. Lisbon, Portugal. | pt_BR |
Afiliación | Philipps-University Marburg. Institute of Physiological Chemistry. Marburg, Germany. | pt_BR |
Afiliación | Universidade Federal de Juiz de Fora. Departamento de Biologia. Laboratório de Biologia Celular. Juiz de Fora, MG, Brasil. | pt_BR |
Afiliación | University of Alabama at Birmingham. Department of Microbiology. Birmingham, AL, USA. | pt_BR |
Afiliación | European Molecular Biology Laboratory. Heidelberg, Germany, | pt_BR |
Afiliación | European Molecular Biology Laboratory. Heidelberg, Germany, | pt_BR |
Palavras clave en Inglês | Mycobacterium | pt_BR |
Palavras clave en Inglês | Phagosome | pt_BR |
Palavras clave en Inglês | Porins | pt_BR |
DeCS | Porinas | pt_BR |
Fecha de embargo | 2030-01-01 |
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