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BteA Secreted from the Bordetella bronchiseptica Type III Secetion System Induces Necrosis through an Actin Cytoskeleton Signaling Pathway and Inhibits Phagocytosis by Macrophages.
Kuwae, Asaomi; Momose, Fumitaka; Nagamatsu, Kanna; Suyama, Yasuharu; Abe, Akio.
Afiliación
  • Kuwae A; Laboratory of Bacterial Infection, Graduate School of Infection Control Sciences, Kitasato University, Tokyo 108-8641, Japan.
  • Momose F; Laboratory of Viral Infection II, Graduate School of Infection Control Sciences, Kitasato University, Tokyo 108-8641, Japan.
  • Nagamatsu K; Laboratory of Bacterial Infection, Graduate School of Infection Control Sciences, Kitasato University, Tokyo 108-8641, Japan.
  • Suyama Y; Laboratory of Bacterial Infection, Graduate School of Infection Control Sciences, Kitasato University, Tokyo 108-8641, Japan.
  • Abe A; Laboratory of Bacterial Infection, Graduate School of Infection Control Sciences, Kitasato University, Tokyo 108-8641, Japan.
PLoS One ; 11(2): e0148387, 2016.
Article en En | MEDLINE | ID: mdl-26828590
BteA is one of the effectors secreted from the Bordetella bronchiseptica type III secretion system. It has been reported that BteA induces necrosis in mammalian cells; however, the roles of BteA during the infection process are largely unknown. In order to investigate the BteA functions, morphological changes of the cells infected with the wild-type B. bronchiseptica were examined by time-lapse microscopy. L2 cells, a rat lung epithelial cell line, spread at 1.6 hours after B. bronchiseptica infection. Membrane ruffles were observed at peripheral parts of infected cells during the cell spreading. BteA-dependent cytotoxicity and cell detachment were inhibited by addition of cytochalasin D, an actin polymerization inhibitor. Domain analyses of BteA suggested that two separate amino acid regions, 200-312 and 400-658, were required for the necrosis induction. In order to examine the intra/intermolecular interactions of BteA, the amino- and the carboxyl-terminal moieties were purified as recombinant proteins from Escherichia coli. The amino-terminal moiety of BteA appeared to interact with the carboxyl-terminal moiety in the pull-down assay in vitro. When we measured the amounts of bacteria phagocytosed by J774A.1, a macrophage-like cell line, the phagocytosed amounts of B. bronchiseptica strains that deliver BteA into the host cell cytoplasm were significantly lower than those of strains that lost the ability to translocate BteA into the host cell cytoplasm. These results suggest that B. bronchiseptica induce necrosis by exploiting the actin polymerization signaling pathway and inhibit macrophage phagocytosis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fagocitosis / Citoesqueleto de Actina / Transducción de Señal / Bordetella bronchiseptica / Sistemas de Secreción Bacterianos / Macrófagos Límite: Animals Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2016 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fagocitosis / Citoesqueleto de Actina / Transducción de Señal / Bordetella bronchiseptica / Sistemas de Secreción Bacterianos / Macrófagos Límite: Animals Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2016 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos