J Bacteriol Virol.  2012 Sep;42(3):211-223. 10.4167/jbv.2012.42.3.211.

Proteomic Analysis of Thiol-active Proteins of Helicobacter pylori 26695

Affiliations
  • 1Department of Microbiology, Gyeongsang National University College of Medicine, Jinju, Gyeong-Nam, Korea. mjecho@gnu.kr
  • 2Department of Pediatrics, Gyeongsang National University College of Medicine, Jinju, Gyeong-Nam, Korea.
  • 3Research Institute of Life Science, Gyeongsang National University, Jinju, Gyeong-Nam, Korea.

Abstract

Helicobacter pylori are a capnophilic bacterium, which colonize gastric mucosa and are resistant to acidic and oxidative damage. Thiol-active proteins subserve redox functions in tolerating oxidative stress and environmental toxicants, such as hydrogen peroxide and hypochlorous acid. We analyzed disulfide-containing proteins of H. pylori strain 26695. Active disulfide-containing proteins were separated by thiol-affinity chromatography, displayed with two-dimensional electrophoresis (2-DE), and identified by MALDI-TOF-MS. Thirty-five putative disulfide proteins, including AhpC (HP1563), GroEL (HP0011), and FrdB (HP0191), were identified in this study. In addition, 4 disulfide proteins of HypB, FusA, TufB, and AhpC showed enhanced intensities in the periplasmic space when compared with the pellet, suggesting that these proteins might play roles in the first redox system against environmental oxidative stresses. Disulfide-containing proteins identified in this study will provide the standard landscape for constructing the proteome components responsible for redox regulation of H. pylori.

Keyword

Helicobacter pylori; Thiol-active proteins; Proteome

MeSH Terms

Chromatography
Colon
Electrophoresis
Gastric Mucosa
Helicobacter
Helicobacter pylori
Hydrogen Peroxide
Hypochlorous Acid
Oxidation-Reduction
Oxidative Stress
Periplasm
Proteins
Proteome
Sprains and Strains
Hydrogen Peroxide
Hypochlorous Acid
Proteins
Proteome
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