The amino-terminal domain of the P-pilus adhesin determines receptor specificity.

Haslam, D B; Borén, T; Falk, P; Ilver, D; Chou, A; Xu, Z; Normark, S

Haslam, D B; Borén, T; Falk, P; Ilver, D; Chou, A; Xu, Z; Normark, S.

Afiliación

Haslam DB; Department of Molecular Microbiology, Washington University School of Medicine St. Louis, Missouri 63110.

Mol Microbiol ; 14(3): 399-409, 1994 Nov.

Article en En | MEDLINE | ID: mdl-7885225

RESUMEN

Pyelonephritic isolates of Escherichia coli commonly express P-pili, which mediate bacterial attachment to glycolipids on epithelial cell surfaces. Three classes of P-pili have been defined, based on varying specificity for galabiose-containing glycolipids. Variation in adhesive capacity is correlated with a shift in preferred host, suggesting that host tropism depends largely on detailed specificity for the globoseries glycolipids. In this study we examined the importance of the PapG adhesin in determining receptor specificity. Translational fusions were constructed between the amino-terminus of the PapG adhesin from each of the three pilus classes and a reporter protein. The binding specificity of the purified fusion proteins in vitro was identical to that seen with whole bacteria. Adherence of intact bacteria to cultured kidney cells was markedly reduced by a monoclonal antibody specific for the Class III adhesin (previously denoted PrsG), confirming the importance of the amino-terminus of PapG in mediating attachment to a receptor when presented on the eukaryotic cell surface. These results suggest that the detailed receptor specificity resides solely within the amino-terminus of the PapG adhesin and is independent of the complex pilus architecture.

Asunto(s)

Adhesinas de Escherichia coli/genética; Adhesinas de Escherichia coli/metabolismo; Moléculas de Adhesión Celular/genética; Proteínas Fimbrias; Receptores Inmunológicos/metabolismo; Secuencia de Aminoácidos; Animales; Anticuerpos Monoclonales; Secuencia de Carbohidratos; Moléculas de Adhesión Celular/metabolismo; Cartilla de ADN/genética; ADN Bacteriano/genética; Escherichia coli/genética; Escherichia coli/metabolismo; Escherichia coli/patogenicidad; Glucolípidos/química; Glucolípidos/metabolismo; Humanos; Ratones; Datos de Secuencia Molecular; Pielonefritis/microbiología; Proteínas Recombinantes de Fusión/genética; Proteínas Recombinantes de Fusión/metabolismo

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Inmunológicos / Moléculas de Adhesión Celular / Adhesinas de Escherichia coli / Proteínas Fimbrias Límite: Animals / Humans Idioma: En Revista: Mol Microbiol Asunto de la revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Año: 1994 Tipo del documento: Article Pais de publicación: Reino Unido

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