Comparative Proteome Analysis of Cyanidin 3-O-glucoside Treated Helicobacter pylori

Abstract

Some virulence proteins of Helicobacter pylori, such as vacuolating cytotoxic protein A (VacA) and cytotoxin-associated gene protein A (CagA) have been reported to be causative agents of various gastric diseases including chronic gastritis, gastric ulcer or gastric adenocarcinoma. The expression level of these virulence proteins can be regulated when H. pylori is exposed to the antibacterial agent, cyanidin 3-O-glucoside (C3G) as previously reported. In this study, we analyzed the quantitative change of various virulence proteins including CagA and VacA by C3G treatment. We used 2-dimensional electrophoresis (2-DE) to analyze the quantitative change of representative ten proteome components of H. pylori 60190 (VacA+/CagA+; standard strain of Eastern type). After 2-DE analysis, spot intensities were analyzed using ImageMaster™ 2-DE Platinum software then each spot was identified using matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) or peptide sequencing using Finnigan LCQ ion trap mass spectrometer (LC-MS/MS). Next, we selected major virulence proteins of H. pylori among quantitatively meaningful ten spots and confirmed the 2-DE results by Western blot analysis. These results suggest that cyanidin 3-O-glucoside can modulate a variety of H. pylori pathogenic determinants.