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.