Receptor affinity purification of a lipid-binding adhesin from Helicobacter pylori.
Our previous work has shown that Helicobacter pylori specifically recognizes gangliotetraosylceramide, gangliotriaosylceramide, and phosphatidylethanolamine in vitro. This binding specificity is shared by exoenzyme S from Pseudomonas aeruginosa, and monoclonal antibodies against this adhesin prevent the attachment of H. pylori to its lipid receptors. We now report the use of a novel, versatile affinity matrix to purify a 63-kDa exoenzyme S-like adhesin from H. pylori which is responsible for the lipid-binding specificity of this organism.
Department of Microbiology, Hospital for Sick Children, Toronto, Ontario, Canada.
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D018829:Adhesins, Bacterial; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D006017:Glycolipids / Q000378:metabolism; D016480:Helicobacter pylori / Q000737:chemistry*; D008969:Molecular Sequence Data; D010714:Phosphatidylethanolamines / Q000378:metabolism
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D006017:Glycolipids; D010714:Phosphatidylethanolamines; C073899:adhesin, helicobacter