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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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.[1]


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