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

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 oligosacc...

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Bibliographic Details
Published in:Infection and immunity 1998-02, Vol.66 (2), p.444-447
Main Authors: NAMAVAR, F, SPARRIUS, M, VEERMAN, E. C. I, APPELMELK, B. J, VANDENBROUCKE-GRAULS, C. M. J. E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Adhesion
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
CD18 Antigens - physiology
Fundamental and applied biological sciences. Psychology
Helicobacter pylori - physiology
Humans
Lewis Blood Group Antigens - metabolism
Microbiology
Molecular and Cellular Pathogenesis
Molecular Sequence Data
Molecular Weight
Mucins - metabolism
Oligosaccharides - metabolism
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Saliva - microbiology
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Summary: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.
ISSN:0019-9567
1098-5522
DOI:10.1128/iai.66.2.444-447.1998