Proteomic Analysis of Thiol-active Proteins ofHelicobacter pylori26695 | Zendy

Jeongwon Park | Zendy; Jaeyoung Song | Zendy; H. Hwang | Zendy; Hee-Jin Park | Zendy; HeeShang Youn | Zendy; JiHyun Seo | Zendy; HyungLyun Kang | Zendy; Kon-Ho Lee | Zendy; SeungChul Baik | Zendy; WooKon Lee | Zendy; Myung-Je Cho | Zendy; KwangHo Rhee | Zendy

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Proteomic Analysis of Thiol-active Proteins ofHelicobacter pylori26695

Author(s) -

Jeongwon Park,

Jaeyoung Song,

H. Hwang,

Hee-Jin Park,

HeeShang Youn,

JiHyun Seo,

HyungLyun Kang,

Kon-Ho Lee,

SeungChul Baik,

WooKon Lee,

Myung-Je Cho,

KwangHo Rhee

Publication year - 2012

Publication title -

journal of bacteriology and virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.179

H-Index - 12

eISSN - 2093-0429

pISSN - 1598-2467

DOI - 10.4167/jbv.2012.42.3.211

Subject(s) - proteome , biochemistry , thiol , helicobacter pylori , hypochlorous acid , periplasmic space , peroxiredoxin , oxidative stress , chemistry , proteomics , groel , cysteine , biology , escherichia coli , genetics , peroxidase , gene , enzyme

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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