Structure of a C. perfringens enterotoxin mutant in complex with a modified Claudin-2 extracellular loop 2.

ABSTRACT: CPE (Clostridium perfringens enterotoxin) is the major virulence determinant for C. perfringens type-A food poisoning, the second most common bacterial food-borne illness in the UK and USA. After binding to its receptors, which include particular human claudins, the toxin forms pores in the cell membrane. The mature pore apparently contains a hexamer of CPE, claudin and, possibly, occludin. The combination of high binding specificity with cytotoxicity has resulted in CPE being investigated, with some success, as a targeted cytotoxic agent for oncotherapy. In this paper, we present the X-ray crystallographic structure of CPE in complex with a peptide derived from extracellular loop 2 of a modified, CPE-binding Claudin-2, together with high-resolution native and pore-formation mutant structu

SUBMITTER: Yelland TS 

PROVIDER: S-EPMC10921947 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature