Helicobacter pylori r-Glutamyl Transpeptidase Plays a Role in Detoxification of Epigallocatechin Gallate
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Abstract
The emergence of antibiotic resistance in Helicobacter pylori, a major cause of dyspepsia and a carcinogenic agent of gastric cancer, has led to the search for new natural antibacterial compounds. It has been reported that epigallocatechin gallate (EGCG), the most potent catechin found in green tea (Camellia sinensis L.), exhibits antibacterial activity against several bacteria, including H. pylori. Recently, the inhibition of the human liver cell -glutamyl transpeptidase (GGT) by EGCG has been demonstrated. However, there have been no reports on the effect of EGCG on H. pylori GGT, which is one of the bacterial virulence factors. Based on the evidence of human GGT inhibition, it is assumed that the EGCG can also inhibit H. pylori GGT through mechanisms that may include a reduction in the bacterial ggt gene expression. To extend our knowledge, the effect of EGCG on the H. pylori ggt mRNA level was examined. The minimal inhibitory concentration (MIC) of EGCG against H. pylori was determined and found to be 250 µg/ml. Subsequently, the ggt gene expression level of the H. pylori grown on a media containing EGCG at sub-MIC (125 µg/ml) and no EGCG was studied using the quantitative RT-PCR with SYBR green fluorescein method. The result showed that the ggt gene expression of H. pylori exposed to EGCG was up-regulated by over 12 fold (p < 0.01). This finding contradicts the expected reduction in gene expression. The observed increase in transcriptional level of the bacterial ggt gene in this study indicates that, besides its role in bacterial colonization, the H. pylori GGT is produced as a respond to EGCG exposure, possibly due to the fact that the enzyme involves the detoxification of toxic substances.
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References
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