title: Sulfated glycans on oral mucin as receptors for Helicobacter pylori.
abstract: Helicobacter pylori is able to colonize gastric epithelia, causing chronic active gastritis, gastric and duodenal ulcers and presumably gastric malignancies. Attempts to identify the natural reservoir for this microorganism other than the stomach have been unsuccessful. It is suspected that H. pylori can be transmitted orally, since the microorganism has been detected at various sites of the oral cavity. The aim of the present study was to determine whether H. pylori can bind to salivary mucins, which in vivo coat the oral epithelia, and characterize further the interaction. Binding of salivary mucins and of synthetic oligosaccharides was studied in ELISA and immunoblotting, using specific mono- and polyclonal antibodies, and synthetic neoglycoconjugates. H. pylori bound most avidly to a highly sulfated subpopulation of high molecular weight salivary mucins, secreted from the palatine salivary glands, and with less avidity to mucin species secreted by the sublingual and submandibular salivary glands, which are less sulfated. Binding was strongly enhanced upon decreasing pH from 6.0 to 5.0. Using synthetic polyacrylamide coupled oligosaccharides it was found that SO3-3-Gal and the SO3-3-Lewis(a) blood group antigen bound to H. pylori. In contrast, binding of sialylated Lewis(a) and Lewis(b) antigens was much weaker. This study indicates that sulfated oligosaccharides on salivary mucins may provide receptor structures for adhesion of H. pylori to oral surfaces.
authors.affiliation: Department of Oral Biochemistry, Academic Centre for Dentistry, Amsterdam (ACTA), The Netherlands.
authors.forename: E C
authors.initials: EC
authors.lastname: Veerman
authors.forename: C M
authors.initials: CM
authors.lastname: Bank
authors.forename: F
authors.initials: F
authors.lastname: Namavar
authors.forename: B J
authors.initials: BJ
authors.lastname: Appelmelk
authors.forename: J G
authors.initials: JG
authors.lastname: Bolscher
authors.forename: A V
authors.initials: AV
authors.lastname: Nieuw Amerongen
mesh_terms: D001422:Bacterial Adhesion; D004797:Enzyme-Linked Immunosorbent Assay; D016480:Helicobacter pylori / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D006801:Humans; D006863:Hydrogen-Ion Concentration; D016253:Microscopy, Immunoelectron; D009077:Mucins / Q000737:chemistry / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012471:Salivary Proteins and Peptides / Q000737:chemistry / Q000378:metabolism*; D013464:Sulfuric Acids / Q000737:chemistry
chemical_list: D009077:Mucins; D011134:Polysaccharides; D012471:Salivary Proteins and Peptides; D013464:Sulfuric Acids