Comparative proteome analysis of Helicobacter pylori clinical strains by two-dimensional gel electrophoresis

被引:8
|
作者
Zhang, Ya-nan [2 ]
Ding, Shi-gang [1 ]
Huang, Liu-huan [3 ]
Zhang, Jing [1 ]
Shi, Yan-yan [1 ]
Zhong, Li-jun [4 ]
机构
[1] Peking Univ, Dept Gastroenterol, Hosp 3, Beijing 100191, Peoples R China
[2] Capital Med Univ, Dept Lab, Beijing Tiantan Hosp, Beijing 100050, Peoples R China
[3] Beijing Shi Jing Shan Hosp, Dept Thorac & Cardiovasc Surg, Beijing 100043, Peoples R China
[4] Peking Univ, Hlth Sci Ctr, Beijing 100091, Peoples R China
来源
基金
中国国家自然科学基金;
关键词
Helicobacter pylori; Proteome; Gastric cancer; Gastritis; Two-dimensional gel electrophoresis; GENETIC DIVERSITY; ESCHERICHIA-COLI; INCREASED RISK; RNA-BINDING; CAGA; NUSA; INFECTION; PROTEINS; SEQUENCE; ICEA;
D O I
10.1631/jzus.B1000445
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Objective: To investigate the pathogenic properties of Helicobacter pylori by comparing the proteome map of H. pylori clinical strains. Methods: Two wild-type H. pylori strains, YN8 (isolated from biopsy tissue of a gastric cancer patient) and YN14 (isolated from biopsy tissue of a gastritis and duodenal ulcer patient), were used. Proteomic analysis, using a pH range of 3-10 and 5-8, was performed. The individual proteins were identified by quadrupole time-of-flight (Q-TOF) mass spectrometer and protein database search. Results: Variation in spot patterns directed towards differential protein expression levels was observed between the strains. The gel revealed prominent proteins with several protein "families". The comparison of protein expressions of the two strains reveals a high variability. Differentially present or absent spots were observed. Nine differentially expressed protein spots identified by Q-TOF included adenosine triphosphate (ATP)-binding protein, disulfide oxidoreductase B (DsbB)-like protein, N utilization substance A (NusA), ATP-dependent protease binding subunit/heat shock protein, hydantoin utilization protein A, seryl-tRNA synthetase, molybdenum ABC transporter ModD, and hypothetical proteins. Conclusions: This study suggests that H. pylori strains express/repress protein variation, not only in terms of the virulence proteins, but also in terms of physiological proteins, when they infect a human host. The difference of protein expression levels between H. pylori strains isolated from gastric cancer and gastritis may be the initiator of inflammation, and result in the different clinical presentation. In this preliminary study, we report seven differential proteins between strains, with molecule weights from approximately 10 kDa to approximately 40 kDa. Further studies are needed to investigate those proteins and their function associated with H. pylori colonization and adaptation to host environment stress.
引用
收藏
页码:820 / 827
页数:8
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