Proteomic Analysis of Thiol-active Proteins of Helicobacter pylori 26695.
10.4167/jbv.2012.42.3.211
- Author:
Jeong Won PARK
1
;
Jae Young SONG
;
Hyang Ran HWANG
;
Hee Jin PARK
;
Hee Shang YOUN
;
Ji Hyun SEO
;
Hyung Lyun KANG
;
Kon Ho LEE
;
Seung Chul BAIK
;
Woo Kon LEE
;
Myung Je CHO
;
Kwang Ho RHEE
Author Information
1. Department of Microbiology, Gyeongsang National University College of Medicine, Jinju, Gyeong-Nam, Korea. mjecho@gnu.kr
- Publication Type:Original Article
- Keywords:
Helicobacter pylori;
Thiol-active proteins;
Proteome
- MeSH:
Chromatography;
Colon;
Electrophoresis;
Gastric Mucosa;
Helicobacter;
Helicobacter pylori;
Hydrogen Peroxide;
Hypochlorous Acid;
Oxidation-Reduction;
Oxidative Stress;
Periplasm;
Proteins;
Proteome;
Sprains and Strains
- From:Journal of Bacteriology and Virology
2012;42(3):211-223
- CountryRepublic of Korea
- Language:English
-
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.
