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KMID : 0921620120420030211
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Journal of Bacteriology and Virology
2012 Volume.42 No. 3 p.211 ~ p.223
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Proteomic Analysis of Thiol-active Proteins of Helicobacter pylori 26695
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Park Jeong-Won
Song Jae-Young
Hwang Hyang-Ran
Park Hee-Jin
Youn Hee-Shang
Seo Ji-Hyun
Kang Hyung-Lyun
Lee Kon-Ho
Baik Seung-Chul
Lee Woo-Kon
Cho Myung-Je
Rhee Kwang-Ho
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Abstract
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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.
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KEYWORD
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Helicobacter pylori, Thiol-active proteins, Proteome
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