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KMID : 0880220110490020251
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Journal of Microbiology
2011 Volume.49 No. 2 p.251 ~ p.256
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Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress
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Wei Qu
Yabin Zhou
Yundong Sun
Ming Fang
Han Yu
Wenjuan Li
Zhifang Liu
Jiping Zeng
Chengjiang Gao
Jihui Jia
Chunyan Chen
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Abstract
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Innate and adaptive immune responses are activated in humans when Helicobacter pylori invades the gastric mucosa. Nitric oxide (NO) and reactive nitrogen species are important immune effectors, which can exert their functions through oxidation and S-nitrosylation of proteins. S-nitrosoglutathione and sodium nitroprus-side were used as NO donors and H. pylori cells were incubated with these compounds to analyze the inhibitory effect of NO. The suppressing effect of NO on H. pylori has been shown in vitro. Furthermore, the proteins modified by S-nitrosylation in H. pylori were identified through the biotin switch method in association with matrix-assisted laser desorption ionization/time-of-flight tandem mass spectrometry (MALDI-TOF-MS/MS). Five S-nitrosylated proteins identified were a chaperone and heat-shock protein (GroEL), alkyl hydroperoxide reductase (TsaA), urease alpha subunit (UreA), HP0721, and HP0129. Importantly, S-nitrosylation of TsaA and UreA were confirmed using purified recombinant proteins. Considering the importance of these enzymes in antioxidant defenses, adherence, and colonization, NO may exert its antibacterial actions by targeting enzymes through S-nitrosylation. Identification of protein S-nitrosylation may contribute to an understanding of the antibacterial actions of NO. Our findings provide an insight into potential targets for the development of novel therapeutic agents against H. pylori infection.
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KEYWORD
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Helicobacter pylori, S-nitrosylation, nitric oxide, biotin switc
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