| Title |
The Changes of Proteomes Components of Helicobacter pylori in Response to Acid Stress without Urea |
| Author |
Chunhong Shao1, Qunye Zhang2, Wei Tang1, Wei Qu1, Yabin Zhou1, Yundong Sun1, Han Yu1, and Jihui Jia1,2* |
| Address |
1Department of Microbiology, School of Medicine, Shandong University, Jinan 250012, P. R. China, 2Key Lab for Experimental Teratology of Chinese Ministry of Education, School of Medicine, Shandong University, Jinan 250012, P. R. China |
| Bibliography |
Journal of Microbiology, 46(3),331-337, 2008,
|
| DOI |
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| Key Words |
Helicobacter pylori, acid stress, comparative proteomics |
| Abstract |
Acid stress is the most obvious challenge Helicobacter pylori encounters in human stomach. The urease system is the basic process used to maintain periplasmic and cytoplasmic pH near neutrality when H. pylori is exposed to acidic condition. However, since the urea concentration in gastric juice is approximately 1 mM, considered possibly insufficient to ensure the survival of H. pylori, it is postulated that additional mechanisms of pH homeostasis may contribute to the acid adaptation in H. pylori. In order to identify the acid-related proteins other than the urease system we have compared the proteome profiles of H. pylori strain 26695 exposed to different levels of external pH (7.4, 6.0, 5.0, 4.0, 3.0, and 2.0) for 30 min in the absence of urea using 2-DE. Differentially expressed proteins were identified by MALDI-TOF-TOF-MS analysis, which turned out to be 36 different proteins. The functions of these proteins included ammonia production, molecular chaperones, energy metabolism, cell envelope, response regulator and some proteins with unknown function. SOM analysis indicated that H. pylori responds to acid stress through multi-mechanisms involving many proteins, which depend on the levels of acidity the cells encounter. |
