NapA has been recognized not only as a virulence AZD0530 manufacturer factor but also as an antioxidant protein that can protect H. pylori from iron-mediated oxidative DNA damage (Wang et al., 2006). Thioredoxin reductase (TrxB) and the associated thioredoxin constitute a thiol-dependent reduction–oxidation system that can catalyze the reduction of specific proteins (e.g. a number of reactive oxygen species detoxification enzymes) by NADPH (Holmgren, 1985). As allitridi downregulated the production of NapA and TrxB, it rendered H. pylori more sensitive to oxidative

stress, which was likely to be harmful to bacterial survival. In this experiment, we also found that the production of several proteins increased, for example alkyl hydroperoxide reductase (AhpC) and co-chaperone (GroES). We supposed that this is the responsive regulation of H. pylori to deal with an unfavorable stress environment. Chuang et al. (2006) have reported that AhpC of H. pylori functions not only as a peroxide reductase but also as a stress-dependent molecular chaperone for the prevention of protein misfolding. GroES is also involved in refolding of stress-denatured proteins (Veinger et al., 1998). It seems that the bacteria attempted to maintain the correct protein conformation by upregulating AhpC and GroES expression

under a stressful selleck kinase inhibitor environment. In the 2-DE maps, we identified that the protein level of CagA was decreased with the administration of 1 μg mL−1 allitridi Chloroambucil compared with control. This result was further confirmed by Western blot analysis (Fig. 3). However, we were more interested in whether allitridi, at subinhibitory concentrations, can still decrease the production of CagA. The examination was carried out using a Western blot. Figure 3 shows that allitridi can effectively suppress the production of CagA at subinhibitory concentrations and in a concentration-dependent manner in the indicated time. The vacuolating cytotoxin (VacA) is another important virulence factor in the process of pathogenicity by H. pylori. The major biological function of VacA is the formation of large cytoplasmic vacuoles in eukaryotic cells by

disrupting the vesicular trafficking machinery (Cover & Blaser, 1992). VacA is a secreted protein and mainly exists in the supernatant, and so we could not identify its change in the 2-DE maps. Whether the production of this toxin is suppressed by allitridi is not clear. Western blot analysis was conducted with the anti-VacA antibody. Our results showed that the production of the secreted VacA protein was decreased by allitridi at MIC and even at subinhibitory concentrations, and this effect was dose-dependent (Fig. 3). The above study shows that allitridi, at subinhibitory concentrations, can potently inhibit the production of CagA and VacA, suggesting that allitridi is of significant clinical value as an anti-H. pylori agent. As virulence factors produced by H.