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CLC number: R735.2; R378

On-line Access: 2011-10-08

Received: 2010-12-24

Revision Accepted: 2011-08-09

Crosschecked: 2011-08-09

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Journal of Zhejiang University SCIENCE B 2011 Vol.12 No.10 P.820-827

http://doi.org/10.1631/jzus.B1000445


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


Author(s):  Ya-nan Zhang, Shi-gang Ding, Liu-huan Huang, Jing Zhang, Yan-yan Shi, Li-jun Zhong

Affiliation(s):  Department of Laboratory, Beijing Tiantan Hospital Affiliated to Capital Medical University, Beijing 100050, China, Department of Gastroenterology, Peking University Third Hospital, Beijing 100191, China, Department of Thoracic and Cardiovascular Surgery, Beijing Shi Jing Shan Hospital, Beijing 100043, China, Peking University Health Science Center, Beijing 100091, China

Corresponding email(s):   dingshigang222@163.com

Key Words:  Helicobacter pylori, Proteome, Gastric cancer, Gastritis, Two-dimensional gel electrophoresis


Ya-nan Zhang, Shi-gang Ding, Liu-huan Huang, Jing Zhang, Yan-yan Shi, Li-jun Zhong. Comparative proteome analysis of Helicobacter pylori clinical strains by two-dimensional gel electrophoresis[J]. Journal of Zhejiang University Science B, 2011, 12(10): 820-827.

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author="Ya-nan Zhang, Shi-gang Ding, Liu-huan Huang, Jing Zhang, Yan-yan Shi, Li-jun Zhong",
journal="Journal of Zhejiang University Science B",
volume="12",
number="10",
pages="820-827",
year="2011",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1000445"
}

%0 Journal Article
%T Comparative proteome analysis of Helicobacter pylori clinical strains by two-dimensional gel electrophoresis
%A Ya-nan Zhang
%A Shi-gang Ding
%A Liu-huan Huang
%A Jing Zhang
%A Yan-yan Shi
%A Li-jun Zhong
%J Journal of Zhejiang University SCIENCE B
%V 12
%N 10
%P 820-827
%@ 1673-1581
%D 2011
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1000445

TY - JOUR
T1 - Comparative proteome analysis of Helicobacter pylori clinical strains by two-dimensional gel electrophoresis
A1 - Ya-nan Zhang
A1 - Shi-gang Ding
A1 - Liu-huan Huang
A1 - Jing Zhang
A1 - Yan-yan Shi
A1 - Li-jun Zhong
J0 - Journal of Zhejiang University Science B
VL - 12
IS - 10
SP - 820
EP - 827
%@ 1673-1581
Y1 - 2011
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1000445


Abstract: 
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.

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

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