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Toxins (Basel). 2010 Jul;2(7):1595-611. doi: 10.3390/toxins2071595. Epub 2010 Jun 24.

Specificity of interaction between clostridium perfringens enterotoxin and claudin-family tight junction proteins.

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  • 1Division of Pulmonary, Allergy and Critical Care Medicine, Department of Medicine, 205 Whitehead Bldg, 615 Michael St. Emory University School of Medicine, Atlanta, GA 30322, USA. leslie.mitchell@emory.edu

Abstract

Clostridium perfringens enterotoxin (CPE), a major cause of food poisoning, forms physical pores in the plasma membrane of intestinal epithelial cells. The ability of CPE to recognize the epithelium is due to the C-terminal binding domain, which binds to a specific motif on the second extracellular loop of tight junction proteins known as claudins. The interaction between claudins and CPE plays a key role in mediating CPE toxicity by facilitating pore formation and by promoting tight junction disassembly. Recently, the ability of CPE to distinguish between specific claudins has been used to develop tools for studying roles for claudins in epithelial barrier function. Moreover, the high affinity of CPE to selected claudins makes CPE a useful platform for targeted drug delivery to tumors expressing these claudins.

KEYWORDS:

Clostridium perfringens; acute lung injury; cancer therapeutics; claudin; intestinal epithelium; tight junction

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