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J Med Microbiol 46 (1997), 541-546; DOI: 10.1099/00222615-46-7-541
© 1997 Society for General Microbiology
ISSN 0022-2615
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Identification of heparan sulphate binding surface proteins of Helicobacter pylori: inhibition of heparan sulphate binding with sulphated carbohydrate polymers

M. UTT*,{dagger} and T. WADSTRÖM*

* University of Lund, Institute of Medical Microbiology, SÖlvegatan 23, S-223 62 Lund, Sweden

{dagger}Bional Ltd, Riia 185, EE2400 Tartu, Estonia

Corresponding author: Professor T. WadstrÖm.

Received October 27, 1995 Revision received March 18, 1996.
Accepted March 18, 1996

Heparan sulphate binding to cells of the gastric pathogen Helicobacter pylori at pH 4-6 is common. Binding was inhibited by various unlabelled sulphated polysaccharides and at high ionic strength and pH, but not by carboxylated or non-sulphated compounds. The inhibition by various sulphated compounds such as dextran sulphate and carrageenans was related to the sulphate content and not to the carbohydrate polymer backbone. The IC50 values for heparin and dextran sulphate for H. pylori strain 25 were calculated as 3.55 x 10-7 M and 5.01 x 10-6 M respectively. Heparin-binding proteins of H. pylori are exposed on the cell surface, as shown by biotinylation of cell-surface proteins before separation of outer membranes and by an indirect immunofluorescence assay. The strongest biotin-heparin binding by H. pylori was observed with a polypeptide in the 55-60 kDa region.

Publication was delayed from Oct. 1996 at the request of the authors.




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