The glycerolipid receptor for Helicobacter pylori (and exoenzyme S) is phosphatidylethanolamine.
We have previously shown that Helicobacter pylori specifically binds to a glycerolipid species preferentially found in the antrum of the human stomach. We now show by high-pressure liquid chromatographic analysis that this species is a form of phosphatidylethanolamine and that H. pylori specifically binds to bona fide phosphatidylethanolamine as detected by a thin-layer chromatogram overlay procedure. Considerable variation in the binding of H. pylori to phosphatidylethanolamine from different sources was observed, however, suggesting the importance of the nature of the long-chain hydrophobic moiety. A similar binding specificity was shown by exoenzyme S from Pseudomonas aeruginosa, consistent with our hypothesis that that an exoenzyme S-like adhesin is responsible for the binding of H. pylori to its lipid receptors.
Lingwood
C A
CA
Department of Microbiology, Hospital for Sick Children, Toronto, Ontario, Canada.
Huesca
M
M
Kuksis
A
A
D036002:ADP Ribose Transferases; D001427:Bacterial Toxins; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D016480:Helicobacter pylori / Q000378:metabolism* / Q000472:pathogenicity; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D010743:Phospholipids / Q000032:analysis / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000472:pathogenicity
D001427:Bacterial Toxins; D010714:Phosphatidylethanolamines; D010743:Phospholipids; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases; C444820:exoenzyme S