Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin

Yasunori Saitoh, Hiroshi Suzuki, Kazutoshi Tani, Kouki Nishikawa, Katsumasa Irie, Yuki Ogura, Atsushi Tamura, Sachiko Tsukita, Yoshinori Fujiyoshi

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92 Citations (Scopus)

Abstract

The C-terminal region of Clostridium perfringens enterotoxin (C-CPE) can bind to specific claudins, resulting in the disintegration of tight junctions (TJs) and an increase in the paracellular permeability across epithelial cell sheets. Here we present the structure of mammalian claudin-19 in complex with C-CPE at 3.7 Å resolution. The structure shows that C-CPE forms extensive hydrophobic and hydrophilic interactions with the two extracellular segments of claudin-19. The claudin-19/C-CPE complex shows no density of a short extracellular helix that is critical for claudins to assemble into TJ strands. The helix displacement may thus underlie C-CPE-mediated disassembly of TJs.

Original languageEnglish
Pages (from-to)775-778
Number of pages4
JournalScience
Volume347
Issue number6223
DOIs
Publication statusPublished - Feb 13 2015
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Saitoh, Y., Suzuki, H., Tani, K., Nishikawa, K., Irie, K., Ogura, Y., Tamura, A., Tsukita, S., & Fujiyoshi, Y. (2015). Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin. Science, 347(6223), 775-778. https://doi.org/10.1126/science.1261833