IDENTIFICATION OF GLYCOLIPID RECEPTORS FOR HELICOBACTER-PYLORI BY TLC-IMMUNOSTAINING

Helicobacter pylori has been identified as a causative agent in active chronic gastritis. The receptor for this bacteria, however, is not known. It is likely that the receptor molecules may be glycosphingolipids* as shown in the cases of other bacteria. We explored this possibility by a thin-layer chromatography (TLC)-immunostaining method. Among glycosphingolipids extracted from human gastric mucosa, intact Helicobacter pylori specifically bound to I3SO3-GalCer and II3NeuAc-LacCer, whereas no specific binding to neutral glycosphingolipids, which share the same ceramide moiety with I3SO3-GalCer or II3NeuAc-LacCer, was demonstrated. Sonicated bacteria could still bind to II3NeuAc-LacCer with comparable affinity. In contrast, the binding of bacteria to I3SO3-GalCer was greatly diminished upon sonication. These results suggest that each of the oligosaccharide moieties of II3NeuAc-LacCer and I3SO3-GalCer may be specifically recognized by different ligand molecules of Helicobacter pylori.