Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin

Author:

Saitoh Yasunori12,Suzuki Hiroshi1,Tani Kazutoshi1,Nishikawa Kouki1,Irie Katsumasa12,Ogura Yuki3,Tamura Atsushi3,Tsukita Sachiko3,Fujiyoshi Yoshinori12

Affiliation:

1. Cellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan.

2. Department of Basic Medical Science, Graduate School of Pharmaceutical Science, Nagoya University, Chikusa, Nagoya 464-8601, Japan.

3. Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan.

Abstract

How a toxin makes epithelial sheets leaky The entire human body and its many compartments are shielded from their external environments by the barrier function of epithelial cell sheets. The paracellular barrier function of tight junctions (TJs) is critical for maintaining homeostasis in any multicellular organism, especially in the skin and internal organs and at the blood-brain barrier. One of the major components of TJs is a family of adhesive membrane proteins known as claudins. Several members of the claudin family are receptors for the bacterial toxin Clostridium perfringens enterotoxin. This toxin often causes food-borne illness both in humans and animals. Saitoh et al. crystallized a complex between the toxin and a claudin that reveals just how the toxin damages epithelial barriers (see the Perspective by Artursson and Knight). Science , this issue p. 775 ; see also p. 716

Funder

Grants-in-Aid for Scientific Research

Grants-in-Aid for Scientific Research in Innovative Areas

Platform for Drug Discovery, Information

Ministry of Education, Culture, Sports, Science and Technology of Japan

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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