Abstract
Clostridium perfringens enterotoxin (CPE) is responsible for the diarrheal symptoms of C. perfringens type A food poisoning and antibiotic-associated diarrhea. The CPE protein consists of a single 35 kDa polypeptide with a C-terminal receptor-binding region and an N-terminal toxicity domain. Under appropriate conditions, CPE can interact with structural components of the epithelial tight junctions, including certain claudins and occludin. Those interactions can affect tight junction structure and function, thereby altering paracellular permeability and (possibly) contributing to CPE-induced diarrhea. However, the tight junction effects of CPE require cellular damage as a prerequisite. CPE induces cellular damage via its cytotoxic activity, which results from plasma membrane permeability alterations caused by formation of a ∼155 kDa CPE-containing complex that may correspond to a pore. Thus, CPE appears to be a bifunctional toxin that first induces plasma membrane permeability alterations; using the resultant cell damage, CPE then gains access to tight junction proteins and affects tight junction structure and function.
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