The major virulence factor of C. perfringens is the CPE enterotoxin, which is secreted upon invasion of the host gut, and contributes to food poisoning and other gastrointestinal illnesses.[3] It has a molecular weight of 35.3 kDa, and is responsible for the disintegration of tight junctions between epithelial cells in the gut.[6] This mechanism is mediated by host
claudin-3 and
claudin-4 receptors, situated at the
tight junctions.[7]
Clostridium enterotoxin is a nine-stranded
beta sheet sandwich in shape. It has been determined that it is very similar to other spore-forming
bacteria.[1] The binding site is between beta sheets eight and nine. This allows the human
claudin-3,4,6,7,8 and 14 to bind but not 1,2,5, and 10. The way the
protein work is it destroys the
cell membrane structure of animals by binding to claudin family proteins. These are components of tight junctions of the epithelial cell membrane.[1]