Biochemical and functional characterization of Helicobacter pylori vesicles


Helicobacter pylori can cause peptic ulcer disease and/or gastric cancer. Adhesion of bacteria to the stomach mucosa is an important contributor to the vigour of infection and resulting virulence. H. pylori adheres primarily via binding of BabA adhesins to ABO/Lewis b (Leb) blood group antigens and the binding of SabA adhesins to sialyl-Lewis x/a (sLex/a) antigens. Similar to most Gram-negative bacteria, H. pylori continuously buds off vesicles and vesicles derived from pathogenic bacteria often include virulence-associated factors. Here we biochemically characterized highly purified H. pylori vesicles. Major protein and phospholipid components associated with the vesicles were identified with mass spectroscopy and nuclear magnetic resonance. A subset of virulence factors present was confirmed by immunoblots. Additional functional and biochemical analysis focused on the vesicle BabA and SabA adhesins and their respective interactions to human gastric epithelium. Vesicles exhibit heterogeneity in their protein composition, which were specifically studied in respect to the BabA adhesin. We also demonstrate that the oncoprotein, CagA, is associated with the surface of H. pylori vesicles. Thus, we have explored mechanisms for intimate H. pylori vesicle-host interactions and found that the vesicles carry effector-promoting properties that are important to disease development.

DOI: 10.1111/j.1365-2958.2010.07307.x

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@inproceedings{Olofsson2010BiochemicalAF, title={Biochemical and functional characterization of Helicobacter pylori vesicles}, author={Annelie Olofsson and Anna Vallstr{\"{o}m and Katja Petzold and Nicole Tegtmeyer and J{\"{u}rgen Schleucher and Sven Carlsson and Rainer Haas and Steffen Backert and Sun Nyunt Wai and Gerhard Gr{\"{o}bner and Anna Arnqvist}, booktitle={Molecular microbiology}, year={2010} }