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Infect Immun, February 1998, p. 444-447, Vol. 66, No. 2
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

Ferry Namavar,1,* Marion Sparrius,1 Enno C. I. Veerman,2 Ben J. Appelmelk,1 and Christina M. J. E. Vandenbroucke-Grauls1

Departments of Medical Microbiology1 and Oral Biochemistry,2 Medical School, Vrije Universiteit, 1081 BT Amsterdam, The Netherlands

Received 18 July 1997/Returned for modification 5 September 1997/Accepted 7 November 1997

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.

* Corresponding author. Mailing address: Department of Medical Microbiology, Medical School, Vrije Universiteit, van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands. Phone: 31 20 4448296. Fax: 31 20 4448318. E-mail: F.Namavar.mm{at}med.vu.nl.




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