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 |
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Authors: | Anke Walz Stefan Odenbreit Kai Stühler Andreas Wattenberg Helmut E Meyer Jafar Mahdavi Thomas Borén Stefan Ruhl |
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Institution: | 1. Department of Operative Dentistry and Periodontology, Dental School, University of Regensburg, Regensburg, Germany;2. Max von Pettenkofer Institute, University of Munich, Munich, Germany;3. Medical Proteom Center, Ruhr Universit?t, Bochum, Germany;4. Protagen AG, Dortmund, Germany;5. Division of Microbiology and Infectious Diseases, Queen's Medical Centre, Nottingham, UK;6. Department of Medical Biochemistry and Biophysics, Ume? University, Ume?, Sweden;7. Department of Oral Biology, State University of New York at Buffalo, Buffalo, NY, USA |
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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‐α2‐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. |
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Keywords: | Adhesins Helicobacter pylori Proteome map Saliva |
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