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Apically exposed, tight junction-associated beta1-integrins allow binding and YopE-mediated perturbation of epithelial barriers by wild-type Yersinia bacteria.
Tafazoli, F; Holmström, A; Forsberg, A; Magnusson, K E.
Afiliación
  • Tafazoli F; Division of Medical Microbiology, Department of Health and Environment, Linköping University, S-581 85 Linköping, Sweden. farta@mme.liu.se
Infect Immun ; 68(9): 5335-43, 2000 Sep.
Article en En | MEDLINE | ID: mdl-10948163
Using polarized epithelial cells, primarily MDCK-1, we assessed the mode of binding and effects on epithelial cell structure and permeability of Yersinia pseudotuberculosis yadA-deficient mutants. Initially, all bacteria except the invasin-deficient (inv) mutant adhered apically to the tight junction areas. These contact points of adjacent cells displayed beta1-integrins together with tight junction-associated ZO-1 and occludin proteins. Indeed, beta1-integrin expression was maximal in the tight junction area and then gradually decreased along the basolateral membranes. Wild-type bacteria also opened gradually the tight junction to paracellular permeation of different-sized markers, viz., 20-, 40-, and 70-kDa dextrans and 45-kDa ovalbumin, as well as to their own translocation between adjacent cells in intimate contact with beta1-integrins. The effects on the epithelial cells and their barrier properties could primarily be attributed to expression of the Yersinia outer membrane protein YopE, as the yopE mutant bound but caused no cytotoxicity. Moreover, the apical structure of filamentous actin (F-actin) was disturbed and tight junction-associated proteins (ZO-1 and occludin) were dispersed along the basolateral membranes. It is concluded that the Yersinia bacteria attach to beta1-integrins at tight junctions. Via this localized injection of YopE, they perturb the F-actin structure and distribution of proteins forming and regulating tight junctions. Thereby they promote paracellular translocation of bacteria and soluble compounds.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de la Membrana Bacteriana Externa / Adhesión Bacteriana / Yersinia pseudotuberculosis / Uniones Estrechas / Integrina beta1 Tipo de estudio: Risk_factors_studies Límite: Animals Idioma: En Revista: Infect Immun Año: 2000 Tipo del documento: Article País de afiliación: Suecia Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de la Membrana Bacteriana Externa / Adhesión Bacteriana / Yersinia pseudotuberculosis / Uniones Estrechas / Integrina beta1 Tipo de estudio: Risk_factors_studies Límite: Animals Idioma: En Revista: Infect Immun Año: 2000 Tipo del documento: Article País de afiliación: Suecia Pais de publicación: Estados Unidos