Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin.

Namavar, F; Sparrius, M; Veerman, E C; Appelmelk, B J; Vandenbroucke-Grauls, C M

Namavar, F; Sparrius, M; Veerman, E C; Appelmelk, B J; Vandenbroucke-Grauls, C M.

Afiliación

Namavar F; Department of Medical Microbiology, Medical School, Vrije Universiteit, Amsterdam, The Netherlands. F.Namavar.mm@med.vu.nl

Infect Immun ; 66(2): 444-7, 1998 Feb.

Article en En | MEDLINE | ID: mdl-9453593

RESUMEN

The in vitro binding of surface-exposed material and outer membrane proteins of Helicobacter pylori to high-molecular-weight salivary mucin was studied. We identified a 16-kDa surface protein which adhered to high-molecular-weight salivary mucin. This protein binds specifically to sulfated oligosaccharide structures such as sulfo-Lewis a, sulfogalactose and sulfo-N-acetyl-glucosamine on mucin. Sequence analysis of the protein proved that it was identical to the N-terminal amino acid sequence of neutrophil-activating protein. Moreover, this adhesin was able to bind to Lewis x blood group antigen.

Asunto(s)

Adhesión Bacteriana; Proteínas Bacterianas/fisiología; Helicobacter pylori/fisiología; Mucinas/metabolismo; Saliva/microbiología; Secuencia de Aminoácidos; Antígenos CD18/fisiología; Humanos; Antígenos del Grupo Sanguíneo de Lewis/metabolismo; Datos de Secuencia Molecular; Peso Molecular; Oligosacáridos/metabolismo

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saliva / Proteínas Bacterianas / Adhesión Bacteriana / Helicobacter pylori / Mucinas Límite: Humans Idioma: En Revista: Infect Immun Año: 1998 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos

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