title: Identification of glycoprotein receptors within the human salivary proteome for the lectin-like BabA and SabA adhesins of Helicobacter pylori by fluorescence-based 2-D bacterial overlay.
abstract: Because gastric infection by Helicobacter pylori takes place via the oral route, possible interactions of this bacterium with human salivary proteins could occur. By using modified 1- and 2-D bacterial overlay, binding of H. pylori adhesins BabA and SabA to the whole range of salivary proteins was explored. Bound salivary receptor molecules were identified by MALDI-MS and by comparison to previously established proteome maps of whole and glandular salivas. By use of adhesin-deficient mutants, binding of H. pylori to MUC7 and gp-340 could be linked to the SabA and BabA adhesins, respectively, whereas binding to MUC5B was associated with both adhesins. Binding of H. pylori to the proline-rich glycoprotein was newly detected and assigned to BabA adhesin whereas the SabA adhesin was found to mediate binding to newly detected receptor molecules, including carbonic anhydrase VI, secretory component, heavy chain of secretory IgA1, parotid secretory protein and zinc-alpha(2)-glycoprotein. Some of these salivary glycoproteins are known to act as scavenger molecules or are involved in innate immunity whereas others might come to modify the pathogenetic properties of this organism. In general, this 2-D bacterial overlay technique represents a useful supplement in adhesion studies of bacteria with complex protein mixtures.
authors.affiliation: Department of Operative Dentistry and Periodontology, Dental School, University of Regensburg, Regensburg, Germany.
authors.forename: Anke
authors.initials: A
authors.lastname: Walz
authors.forename: Stefan
authors.initials: S
authors.lastname: Odenbreit
authors.forename: Kai
authors.initials: K
authors.lastname: Stühler
authors.forename: Andreas
authors.initials: A
authors.lastname: Wattenberg
authors.forename: Helmut E
authors.initials: HE
authors.lastname: Meyer
authors.forename: Jafar
authors.initials: J
authors.lastname: Mahdavi
authors.forename: Thomas
authors.initials: T
authors.lastname: Borén
authors.forename: Stefan
authors.initials: S
authors.lastname: Ruhl
mesh_terms: D018829:Adhesins, Bacterial / Q000378:metabolism*; D001422:Bacterial Adhesion; D015153:Blotting, Western; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D016650:Fluorescein-5-isothiocyanate; D005453:Fluorescence; D006023:Glycoproteins / Q000032:analysis* / Q000302:isolation & purification; D016480:Helicobacter pylori / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding; D020543:Proteome / Q000032:analysis*; D011956:Receptors, Cell Surface / Q000032:analysis*; D012463:Saliva / Q000378:metabolism*; D012471:Salivary Proteins and Peptides / Q000302:isolation & purification
chemical_list: D018829:Adhesins, Bacterial; C400429:BabA protein, Helicobacter pylori; D006023:Glycoproteins; D037102:Lectins; D020543:Proteome; D011956:Receptors, Cell Surface; C500808:SabA protein, Helicobacter pylori; D012471:Salivary Proteins and Peptides; D016650:Fluorescein-5-isothiocyanate