title: Inhibition of Helicobacter pylori and Helicobacter mustelae binding to lipid receptors by bovine colostrum.
abstract: Helicobacter pylori, the etiologic agent of chronic-active gastritis and duodenal ulcers in humans, and Helicobacter mustelae, a gastric pathogen in ferrets, bind to phosphatidylethanolamine (PE), a constituent of host gastric mucosal cells, and to gangliotetraosylceramide (Gg4) and gangliotriaosylceramide (Gg3). The effect of a bovine colostrum concentrate (BCC) on the interaction of H. pylori and H. mustelae to their lipid receptors was examined. BCC blocked attachment of both species to Gg4, Gg3, and PE. Partial inhibition of binding was observed with native bovine and human colostra. BCC lacked detectable antibodies (by immunoblotting) to H. pylori surface proteins (adhesins). However, colostral lipid extracts contained PE and lyso-PE that bound H. pylori in vitro. These results indicate that colostrum can block the binding of Helicobacter species to select lipids and that binding inhibition is conferred, in part, by colostral PE or PE derivatives. Colostral lipids may modulate the interaction of H. pylori and other adhesin-expressing pathogens with their target tissues.
authors.affiliation: Department of Clinical Pathology, Hospital for Sick Children, University of Toronto, Ontario, Canada. m.bitzan@utoronto.ca
authors.forename: M M
authors.initials: MM
authors.lastname: Bitzan
authors.forename: B D
authors.initials: BD
authors.lastname: Gold
authors.forename: D J
authors.initials: DJ
authors.lastname: Philpott
authors.forename: M
authors.initials: M
authors.lastname: Huesca
authors.forename: P M
authors.initials: PM
authors.lastname: Sherman
authors.forename: H
authors.initials: H
authors.lastname: Karch
authors.forename: R
authors.initials: R
authors.lastname: Lissner
authors.forename: C A
authors.initials: CA
authors.lastname: Lingwood
authors.forename: M A
authors.initials: MA
authors.lastname: Karmali
mesh_terms: D018829:Adhesins, Bacterial / Q000276:immunology / Q000378:metabolism; D000818:Animals; D000907:Antibodies, Bacterial / Q000032:analysis / Q000276:immunology; D001422:Bacterial Adhesion / Q000276:immunology; D002417:Cattle; D002855:Chromatography, Thin Layer; D003126:Colostrum / Q000737:chemistry / Q000276:immunology*; D005260:Female; D005678:G(M2) Ganglioside / Q000031:analogs & derivatives* / Q000276:immunology / Q000378:metabolism; D005732:Gangliosides; D006028:Glycosphingolipids / Q000276:immunology / Q000378:metabolism*; D016998:Helicobacter / Q000276:immunology / Q000378:metabolism*; D016480:Helicobacter pylori / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D050356:Lipid Metabolism; D008055:Lipids / Q000032:analysis; D010714:Phosphatidylethanolamines / Q000276:immunology / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000276:immunology / Q000378:metabolism
chemical_list: D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial; C011258:G(A1) ganglioside; D005732:Gangliosides; D006028:Glycosphingolipids; D008055:Lipids; D010714:Phosphatidylethanolamines; D011956:Receptors, Cell Surface; D005678:G(M2) Ganglioside; C046458:gangliotriaosylceramide 3'-sulfate