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© The Rockefeller University Press, 0021-9525/1999//195 $5.00
The Journal of Cell Biology, Volume 147, Number 1, , 1999 195-204

Original Article

Clostridium perfringens Enterotoxin Fragment Removes Specific Claudins from Tight Junction Strands

: Evidence for Direct Involvement of Claudins in Tight Junction Barrier



Noriyuki Sonodaa, Mikio Furusea, Hiroyuki Sasakic,d, Shigenobu Yonemuraa, Jun Katahirab, Yasuhiko Horiguchib, and Shoichiro Tsukitaa

a Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan
b Project Research for Molecular Bacteriology, Research Institute for Microbial Diseases, Osaka University 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan
c Laboratory of Cell Biology, KAN Research Institute Inc., Kyoto Research Park, Chudoji, Shimogyo-ku, Kyoto 600-8317, Japan
d Department of Molecular Cell Biology, Institute of DNA Medicine, The Jikei University School of Medicine, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461, Japan
Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.81-75-753-466081-75-753-4372

htsukita{at}mfour.med.kyoto-u.ac.jp

Claudins, comprising a multigene family, constitute tight junction (TJ) strands. Clostridium perfringens enterotoxin (CPE), a single ~35-kD polypeptide, was reported to specifically bind to claudin-3/RVP1 and claudin-4/CPE-R at its COOH-terminal half. We examined the effects of the COOH-terminal half fragment of CPE (C-CPE) on TJs in L transfectants expressing claudin-1 to -4 (C1L to C4L, respectively), and in MDCK I cells expressing claudin-1 and -4. C-CPE bound to claudin-3 and -4 with high affinity, but not to claudin-1 or -2. In the presence of C-CPE, reconstituted TJ strands in C3L cells gradually disintegrated and disappeared from their cell surface. In MDCK I cells incubated with C-CPE, claudin-4 was selectively removed from TJs with its concomitant degradation. At 4 h after incubation with C-CPE, TJ strands were disintegrated, and the number of TJ strands and the complexity of their network were markedly decreased. In good agreement with the time course of these morphological changes, the TJ barrier (TER and paracellular flux) of MDCK I cells was downregulated by C-CPE in a dose-dependent manner. These findings provided evidence for the direct involvement of claudins in the barrier functions of TJs.

Key Words: Clostridium perfringens enterotoxin • tight junction • claudin • epithelial barrier • freeze-fracture

© 1999 The Rockefeller University Press

1.used in this paper: C-CPE, COOH-terminal half fragment of Clostridium perfringens enterotoxin; CPE, Clostridium perfringens enterotoxin; CPE-R, Clostridium perfringens enterotoxin receptor; pAb, polyclonal antibody; TER, transepithelial electrical resistance; TJ, tight junction


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