Neutrophil-Activating Protein Mediates Adhesion of Helicobacter pylori to Sulfated Carbohydrates on High-Molecular-Weight Salivary Mucin

Author:

Namavar Ferry1,Sparrius Marion1,Veerman Enno C. I.2,Appelmelk Ben J.1,Vandenbroucke-Grauls Christina M. J. E.1

Affiliation:

1. Departments of Medical Microbiology1 and

2. Oral Biochemistry,2 Medical School, Vrije Universiteit, 1081 BT Amsterdam, The Netherlands

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

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