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

doi:10.1126/science.1261833

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

Research output: Contribution to journal › Article › peer-review

159 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 language	English
Pages (from-to)	775-778
Number of pages	4
Journal	Science
Volume	347
Issue number	6223
DOIs	https://doi.org/10.1126/science.1261833
Publication status	Published - Feb 13 2015
Externally published	Yes

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title = "Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin",

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 {\AA} 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.",

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T1 - Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin

AU - Saitoh, Yasunori

AU - Suzuki, Hiroshi

AU - Tani, Kazutoshi

AU - Nishikawa, Kouki

AU - Irie, Katsumasa

AU - Ogura, Yuki

AU - Tamura, Atsushi

AU - Tsukita, Sachiko

AU - Fujiyoshi, Yoshinori

PY - 2015/2/13

Y1 - 2015/2/13

N2 - 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.

AB - 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.

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Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin

Abstract

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