Journal
PROTEOMICS
Volume 9, Issue 6, Pages 1582-1592Publisher
WILEY
DOI: 10.1002/pmic.200700808
Keywords
Adhesins; Helicobacter pylori; Proteome map; Saliva
Funding
- Institute of Medical Microbiology, University of Regensburg
- Deutsche Forschungsgemeinschaft [SFB 585]
- German Society of Dental, Oral, and Craniomandibular Sciences
- Ministry of innovation, Science, Research and Technology of Nordrhein-Westfalen
- Vetenskapsradet/VRM
- Cancerfonden
- Umea University Biotechnology Fund
- Kempestiftelserna
Ask authors/readers for more resources
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
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available