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Interaction of Leptospira interrogans with Human Proteolytic Systems Enhances Dissemination through Endothelial Cells and Protease Levels
Vieira, ML; Alvarez-Flores, MP; Kirchgatter, K; Romero, EC; Alves, IJ.
Afiliación
  • Vieira, ML; Instituto Butantan. Centro de Biotecnologia. São Paulo. BR
  • Alvarez-Flores, MP; Instituto Butantan. Laboratório de Bioquímica e Biofísica. São Paulo. BR
  • Kirchgatter, K; Superintendência de Controle de Endemias—SUCEN/IMTSP. Núcleo de Estudos em Malária. São Paulo. BR
  • Romero, EC; Instituto Adolfo Lutz. Centro de Bacteriologia. São Paulo. BR
  • Alves, IJ; Instituto Butantan. Centro de Biotecnologia. São Paulo. BR
Infection and Immunity ; 81(5): 1764-1774, Mai, 2013. ilus, graf
Article en En | SES-SP, SESSP-SUCENPROD, SES-SP | ID: biblio-1063430
Biblioteca responsable: BR93.2
Ubicación: BR93.2
ABSTRACT
We have recently reported the ability of Leptospira to capture plasminogen (PLG) and generate plasmin (PLA) bound on the microbial surface in the presence of exogenous activators. In this work, we examined the effects of leptospiral PLG binding for active penetration through the endothelial cell barrier and activation. The results indicate that leptospires with PLG association or PLA activation have enhanced migration activity through human umbilical vein endothelial cell (HUVEC) monolayers compared with untreated bacteria. Leptospira cells coated with PLG were capable of stimulating the expression of PLG activators by HUVECs. Moreover, leptospires endowed with PLG or PLA promoted transcriptional upregulation matrix metalloprotease 9(MMP-9). Serum samples from patients with confirmed leptospirosis showed higher levels of PLG activators and total MMP-9 than serum samples from normal (healthy) subjects. The highest level of PLG activators and total MMP-9 was detected with microscopicagglutination test (MAT)-negative serum samples, suggesting that this proteolytic activity stimulation occurs at the early stage of the disease. Furthermore, a gelatin zymography profile obtained for MMPs with serum samples from patients with leptospirosis appears to be specific to leptospiral infection because serum samples from patients with unrelated infectious diseases produced no similar degradation bands. Altogether, the data suggest that the Leptospira-associated PLG or PLA might represent a mechanism that contributes to bacterial penetration of endothelial cells through an activation cascade of events that enhances the proteolytic capability of the organism. To our knowledge, this is the first proteolytic activity associated with leptospiral pathogenesis described to date...
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Texto completo: 1 Colección: 06-national / BR Base de datos: SES-SP / SESSP-SUCENPROD Asunto principal: Fibrinolisina / Leptospira Límite: Humans Idioma: En Revista: Infection and Immunity Año: 2013 Tipo del documento: Article
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 06-national / BR Base de datos: SES-SP / SESSP-SUCENPROD Asunto principal: Fibrinolisina / Leptospira Límite: Humans Idioma: En Revista: Infection and Immunity Año: 2013 Tipo del documento: Article