Specificity of Interaction between Clostridium perfringens Enterotoxin and Claudin-Family Tight Junction Proteins

• Type of Material: Article
• Authors: Leslie A. Mitchell, Emory University; Michael H Koval, Emory University
• Language: English
• Date: 2010-06-24
• Publisher: MDPI
• Publication Version: Final Published Version
• Copyright Statement: © 2010 by the authors; licensee MDPI, Basel, Switzerland.
• License: Creative Commons Attribution 3.0 Unported
• Final Published Version (URL): http://www.mdpi.com/2072-6651/2/7/1595
• Title of Journal or Parent Work: Toxins
• ISSN: 2072-6651
• Volume: 2
• Issue: 7
• Start Page: 1595
• End Page: 1611
• Grant/Funding Information: This work was supported by National Institutes of Health grants HL-083120, AA-013757 (to M.K.) and AA-013528 (to L.A.M.).
• Keywords: cancer therapeutics; tight junction; acute lung injury; claudin; Clostridium perfringens; intestinal epithelium
• Research Categories: Biology, Cell

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.