Structural Biology of the Food Poisoning <i>Clostridium Perfringens</i> Enterotoxin

  • KITADOKORO Kengo
    Graduate School of Science and Technology, Department of Biomolecular Engineering, Kyoto Institute of Technology
  • NISHIMURA Kousuke
    Graduate School of Science and Technology, Department of Biomolecular Engineering, Kyoto Institute of Technology
  • KAMITANI Shigeki
    Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University
  • HORIGUCHI Yasuhiko
    Department of Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University

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  • 食中毒を引き起こすウェルシュ菌エンテロトキシンCPEの構造生物学的研究
  • ショクチュウドク オ ヒキオコス ウェルシュキン エンテロトキシン CPE ノ コウゾウ セイブツガクテキ ケンキュウ
  • Structural Biology of the Food Poisoning Clostridium Perfringens Enterotoxin

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Description

Clostridium perfringens enterotoxin(CPE)is a cause of food poisoning and is considered a pore-forming toxin which damages target cells by disrupting the selective permeability of the plasma membrane. We determined the crystal structure of the full-length CPE at 2.0 Å. The overall structure of CPE displays an elongated shape, composed of three distinct domains, D1, D2, and D3. In this structure, the pore-forming domain(Val81〜Ile106)of CPE has alternating pattern of polar and hydrophobic residues and forms α-helix. This characteristic sequence is frequently observed in β pore-forming toxin families as typified by α-hemolysin. These results indicate that CPE behaves as β pore-forming toxins.

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