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Anaerobe v.51, 2018년, pp.124 - 130   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Expression of glyceraldehyde-3-phosphate dehydrogenase on the surface of Clostridium perfringens cells

Matsunaga, Nozomu (Department of Life Science, Faculty of Science, Okayama University of Science, 1-1 Ridai-cho, Kita-ku, Okayama-shi, Okayama 700-0005, Japan ) ; Shimizu, Haruka (Department of Life Science, Faculty of Science, Okayama University of Science, 1-1 Ridai-cho, Kita-ku, Okayama-shi, Okayama 700-0005, Japan ) ; Fujimoto, Kanako (Department of Life Science, Faculty of Science, Okayama University of Science, 1-1 Ridai-cho, Kita-ku, Okayama-shi, Okayama 700-0005, Japan ) ; Watanabe, Kanako (Department of Life Science, Faculty of Science, Okayama University of Science, 1-1 Ridai-cho, Kita-ku, Okayama-shi, Okayama 700-0005, Japan ) ; Yamasaki, Tsutomu (Pharmaceutical Department, Shujitsu University, 1-6-1 Nishigawara, Naka-ku, Okayaka-shi, Okayama 703-8516, Japan ) ; Hatano, Naoya (The Integrated Center for Mass Spectrometry, Kobe University Graduate School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe-shi, Hyogo 650-0017, Japan ) ; Tamai, Eiji (Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, 4-2 Bunkyo-cho, Matsuyama-shi, Ehime 790-8578, Japan ) ; Katayama, Seiichi (Department of Life ) ; Hitsumoto, Yasuo ;
  • 초록  

    Abstract During research to identify fibronectin (Fn)-binding proteins (Fbps) on the surface of Clostridium perfringens cells, we identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a candidate Fbp. GAPDH is a glycolytic enzyme found in a wide range of prokaryotes and eukaryotes. The Fn-binding activity of recombinant C. perfringens GAPDH (rGAPDH) was investigated using both ligand blotting analysis and enzyme-linked immunosorbent assay (ELISA). rGAPDH strongly bound plasminogen but not laminin or gelatin. Although GAPDH has no signal sequence, it is expressed on the cell surface of many microorganisms. The presence of GAPDH on the surface of C. perfringens cells was analyzed using ELISA and flow cytometry analyses; purified rGAPDH bound to the surface of C. perfringens cells. As autolysin is reportedly involved in the binding of GAPDH to the cell surface, we evaluated the interaction between rGAPDH and the C. perfringens autolysin Acp by both ELISA and ligand blotting assay. These assays revealed that rGAPDH binds to the catalytic domain of Acp but not the cell wall binding domains. These results suggest that autolysin mediates expression of GAPDH on the surface of C. perfringens cells and indicate a possible moonlighting function for GAPDH in binding both Fn and plasminogen. Highlights GAPDH of Clostridium perfringens bound both fibronectin and plasminogen. GAPDH is expressed on the Clostridium perfringens cell surface. GAPDH bound the catalytic domain of the autolysin, Acp, of Clostridium perfringens.


  • 주제어

    Clostridium perfringens .   GAPDH .   Fibronectin .   Fibronectin-binding proteins.  

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