Structures of a synthetic antibody selected against and bound to the C-terminal domain of Clostridium perfringens enterotoxin.

ABSTRACT: Clostridium perfringens enterotoxin (CpE) causes cytotoxic gastrointestinal disease in mammalian epithelium by binding membrane protein receptors called claudins. Claudins direct the formation of cell/cell tight junctions through oligomerization and govern the transport of molecules between individual cells. CpE binds claudins through its C-terminal domain (cCpE) and induces cytotoxicity through its N-terminal domain. The non-toxic cCpE is a useful tool to study claudins, tight junctions, and for translational applications, such as increasing the permeability of restrictive tissues like the blood-brain barrier or selective targeting of claudin overexpressing cancers. Conversely, there are no specialized molecular tools to study CpE or cCpE, or to modulate or inhibit their functions. We pre

SUBMITTER: Ogbu CP 

PROVIDER: S-EPMC12432410 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature