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Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Helicobacter pylori Strain 26695

Seung-Chul Baik,^1,2, Kyung-Mi Kim,^1, Su-Min Song,¹ Do-Su Kim,¹ Jin-Su Jun,¹ Seung-Gyu Lee,¹ Jae-Young Song,¹ Jeong-Uck Park,^1,2 Hyung-Lyun Kang,^1,2 Woo-Kon Lee,^1,2 Myung-Je Cho,^1,2 Hee-Shang Youn,³ Gyung-Hyuck Ko,⁴ and Kwang-Ho Rhee^1,2*

Department of Microbiology,¹ Pathology,⁴ Pediatrics,³ Gyeongsang Institute of Health Science, Gyeongsang National University College of Medicine, Jinju, Gyeongsangnam-do 660-751, Republic of Korea²

Received 23 July 2003/ Accepted 5 November 2003

Helicobacter pylori causes gastroduodenal disease, which is mediated in part by its outer membrane proteins (OMPs). To identify OMPs of H. pylori strain 26695, we performed a proteomic analysis. A sarcosine-insoluble outer membrane fraction was resolved by two-dimensional electrophoresis with immobilized pH gradient strips. Most of the protein spots, with molecular masses of 10 to 100 kDa, were visible on the gel in the alkaline pI regions (6.0 to 10.0). The proteome of the OMPs was analyzed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. Of the 80 protein spots processed, 62 spots were identified; they represented 35 genes, including 16 kinds of OMP. Moreover, we identified 9 immunoreactive proteins by immunoblot analysis. This study contributes to the characterization of the H. pylori strain 26695 proteome and may help to further elucidate the biological function of H. pylori OMPs and the pathogenesis of H. pylori infection.

S.-C.B. and K.-M.K. contributed equally to this study.

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