C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability.

ABSTRACT: The pore-forming Clostridium perfringens enterotoxin (CPE), a common cause of foodborne diseases, facilitates Ca²⁺ influx in enterocytes, leading to cell damage. Upon binding to certain claudins (e.g., claudin-4), CPE forms oligomeric pores in the cell membrane. While the mechanism of CPE-claudin interaction is well understood, the structure and assembly of the pore complex remain elusive. Here, we used AlphaFold2 complex prediction, structure alignment, and molecular dynamics simulations to generate models of prepore and pore states of the CPE/claudin-4 complex. We sequentially addressed CPE-claudin, CPE-CPE, and claudin-claudin interactions, along with CPE conformational changes. The CPE pore is a hexameric variant of the typical heptameric pore stem and cap architectur

SUBMITTER: Nagarajan SK 

PROVIDER: S-EPMC11774686 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature