| Title |
Identification of S-Nitrosylation of Proteins of Helicobacter pylori in Response to Nitric Oxide Stress |
| Author |
Wei Qu1,2, Yabin Zhou1, Yundong Sun1, Ming Fang1, Han Yu1, Wenjuan Li1, Zhifang Liu1, Jiping Zeng1, Chunyan Chen3, Chengjiang Gao1*, and Jihui Jia1* |
| Address |
1Department of Microbiology and Immunology, Key Laboratory for Experimental Teratology of Chinese Ministry of Education, School of Medicine, Shandong University, Jinan, Shandong 250012, P. R. China, 2Department of Radiation Oncology, Key Laboratory of Radiation Oncology of Shandong Province, Shandong Cancer Hospital and Institute, Jinan, Shandong, 250117, P. R. China, 3Department of Hematology, Qilu Hospital, Shandong University, Jinan, Shandong 250012, P. R. China |
| Bibliography |
Journal of Microbiology, 49(2),251-256, 2011,
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| DOI |
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| Key Words |
Helicobacter pylori, S-nitrosylation, nitric oxide, biotin switch |
| Abstract |
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 nitroprusside 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 (MALDITOF-
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. |
