Identification of S-Nitrosylation of Proteins of Helicobacter pylori in Response to Nitric Oxide Stress

Wei Qu; Yabin Zhou; Yundong Sun; Ming Fang; Han Yu; Wenjuan Li; Zhifang Liu; Jiping Zeng; Chunyan Chen; Chengjiang Gao; Jihui Jia

doi:10.1007/s12275-011-0262-7

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Identification of S-Nitrosylation of Proteins of Helicobacter pylori in Response to Nitric Oxide Stress: Wei Qu ^1,2, Yabin Zhou ¹, Yundong Sun ¹, Ming Fang ¹, Han Yu ¹, Wenjuan Li ¹, Zhifang Liu ¹, Jiping Zeng ¹, Chunyan Chen ³, Chengjiang Gao ¹, Jihui Jia ¹; Journal of Microbiology 2011;49(2):251-256.
DOI: https://doi.org/10.1007/s12275-011-0262-7
Published online: May 3, 2011

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

Corresponding author: Chengjiang Gao , Tel: +86-531-8838-2672,
Jihui Jia , Tel: +86-531-8838-2672,

Received: 21 July 2010 • Accepted: 10 November 2010

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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.

Keywords: Helicobacter pylori;S-nitrosylation;nitric oxide;biotin switch

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Identification of S-Nitrosylation of Proteins of Helicobacter pylori in Response to Nitric Oxide Stress

J. Microbiol. 2011;49(2):251-256. Published online May 3, 2011

DOI: https://doi.org/10.1007/s12275-011-0262-7

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