title: Comparative proteome analysis of Helicobacter pylori clinical strains by two-dimensional gel electrophoresis.
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.
authors.affiliation: Department of Laboratory, Beijing Tiantan Hospital affiliated to Capital Medical University, Beijing, China.
authors.forename: Ya-nan
authors.initials: YN
authors.lastname: Zhang
authors.forename: Shi-gang
authors.initials: SG
authors.lastname: Ding
authors.forename: Liu-huan
authors.initials: LH
authors.lastname: Huang
authors.forename: Jing
authors.initials: J
authors.lastname: Zhang
authors.forename: Yan-yan
authors.initials: YY
authors.lastname: Shi
authors.forename: Li-jun
authors.initials: LJ
authors.lastname: Zhong
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D016480:Helicobacter pylori / Q000737:chemistry*; D006801:Humans; D020543:Proteome / Q000032:analysis*
chemical_list: D001426:Bacterial Proteins; D020543:Proteome