Identification of heparan sulphate binding surface proteins of Helicobacter pylori: inhibition of heparan sulphate binding with sulphated carbohydrate polymers.

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.