Analysis of the interaction of Clostridium perfringens enterotoxin with claudin

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Clostridium perfringens enterotoxin (CPE), a causative agent of food poisoning, is a pore-forming toxin. Claudin, a component of tight junctions, is a tetratransmembrane protein and constitutes a large family of more than 20 members, not all of which serve as the receptor for CPE. The mechanism by which the toxin distinguishes the sensitive claudins is unknown. In this study, we localized the region of claudin responsible for interaction with CPE to the C-terminal 12 amino acids of the second extracellular loop and found that an electrostatic attraction between the basic claudin region and the acidic CPE cleft is involved in their interaction. Furthermore, we present the structure of CPE determined by X-ray crystallography at 2.0 Å. These structural features imply that CPE is a β pore-forming toxin.