J Med Microbiol 57 (2008), 151-158; DOI: 10.1099/jmm.0.47616-0
© 2008 Society for General Microbiology
ISSN 1473-5644
Helicobacter pylori protein response to human bile stress
Chunhong Shao1,
,
Qunye Zhang2,
,
Yundong Sun1,
Zhifang Liu3,
Jiping Zeng3,
Yabin Zhou1,2,
Xiuping Yu1,2 and
Jihui Jia1,2
1 Department of Microbiology, School of Medicine, Shandong University, 44 Wenhuaxi Road, Jinan, Shandong 250012, PR China
2 Key Lab for Experimental Teratology of Chinese Ministry of Education, School of Medicine, Shandong University, Jinan, Shandong 250012, PR China
3 Department of Biochemistry, School of Medicine, Shandong University, Jinan, Shandong 250012, PR China
Correspondence
Jihui Jia
jiajihui{at}sdu.edu.cn
Received 6 September 2007
Accepted 25 October 2007
The ability of Helicobacter pylori to tolerate bile is likely to be important for its colonization and survival in the gastrointestinal tract of humans. As bile can be acidified after reflux into the low pH of the human stomach, the inhibitory effect of fresh human bile with normal appearance on H. pylori before and after acidification was tested first. The results showed that acidification of bile attenuated its inhibitory activity towards H. pylori. Next, the protein profiles of H. pylori under human bile and acidified bile stress were obtained by two-dimensional electrophoresis. Protein spots with differential expression were identified using tandem matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The results showed that the changes in proteomic profiles under bile and acidified bile stress were similar when compared with that of normal H. pylori. Expression of 28 proteins was found to be modulated, with the majority being induced during bile or acidified bile exposure. These proteins included molecular chaperones, proteins involved in iron storage, chemotaxis protein, enzymes related to energy metabolism and flagellar protein. These results indicate that H. pylori responds to bile and acidified bile stress through multiple mechanisms involving many signalling pathways.
Abbreviations: 2-DE, two-dimensional electrophoresis; IPG, immobilized pH gradient; MALDI-TOF/TOF, tandem matrix-assisted laser desorption/ionization time-of-flight; MS, mass spectrometry.
These authors contributed equally to this work.
Copyright © 2008 Society for General Microbiology.