Identification of glycolipid receptors for Helicobacter pylori by TLC-immunostaining
| Autor: | Hitomi Natomi, Yoshitaka Nagai, Kastuko Okuzumi, Masao Iwamori, Toshihito Saitoh, Kentaro Sugano, Weilu Zhao |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Ceramide
Biophysics Bacterial adhesion In Vitro Techniques Biology Biochemistry chemistry.chemical_compound Glycolipid Structural Biology Genetics Humans Receptor Molecular Biology Glycosphingolipid chemistry.chemical_classification Helicobacter pyroli Helicobacter pylori Cell Biology Oligosaccharide biology.organism_classification Ligand (biochemistry) carbohydrates (lipids) Gastric mucosa chemistry Gastritis lipids (amino acids peptides and proteins) Glycolipids Bacteria |
| Zdroj: | FEBS Letters. (2):385-387 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(91)80519-9 |
| Popis: | 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 PSO 3 -GalCer and II 3 NeuAc-LacCer, whereas no specific binding to neutral glycosphingolipids, which share the same ceramide moiety with PSO 3 -GalCer or II 3 NeuAc-LacCer, was demonstrated. Sonicated bacteria could still bind to II 3 NeuAc-LacCer with comparable affinity. In contrast, the binding of bacteria of PSO 3 -GalCer was greatly diminished upon sonication. These results suggest that each of the oligosaccharide moieties of II 3 NeuAc-LarCer and PSO 3 -GalCer may be specifically recognized by different ligand molecules of Helicobacter pylori . |
| Databáze: | OpenAIRE |
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