specificity of interaction between clostridium perfringens enterotoxin and claudin-family tight junction proteins相互作用的特异性perfringens梭状芽胞杆菌肠毒素和claudin-family紧密连接蛋白.pdf

Toxins 2010, 2, 1595-1611; doi:10.3390/toxins2071595 OPEN ACCESS toxins ISSN 2072-6651 /journal/toxins Review Specificity of Interaction between Clostridium perfringens Enterotoxin and Claudin-Family Tight Junction Proteins Leslie A. Mitchell 1 and Michael Koval 1,2,* 1 Division 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; E-Mail: leslie.mitchell@ 2 Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA * Author to whom correspondence should be addressed; E-Mail: mhkoval@; Tel.: +1-404-712-2976; Fax: +1-404-712-2974. Received: 18 May 2010; in revised form: 7 June 2010 / Accepted: 23 June 2010 / Published: 24 June 2010 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 a