Clostridium perfringens type A enterotoxin forms mepacrine-sensitive pores in pure phospholipid bilayers in the absence of putative receptor proteins.
Clostridium perfringens enterotoxin (CPE) is an important cause of food poisoning with no significant homology to other enterotoxins and its mechanism of action remains uncertain. Although CPE has recently been shown to complex with tight junction proteins, we have previously demonstrated that CPE increases ionic permeability in single Caco-2 cells using the whole-cell patch-clamp technique, thereby excluding any paracellular permeability. In this paper we demonstrate that CPE forms pores in synthetic phospholipid membranes in the absence of receptor proteins. The properties of the pores are consistent with CPE-induced permeability changes in Caco-2 cells suggesting that CPE has innate pore-forming ability.
Hardy
S P
SP
Department of Pharmacy and Biomolecular Sciences, University of Brighton, Sussex, UK. s.hardy@bton.ac.uk
Ritchie
C
C
Allen
M C
MC
Ashley
R H
RH
Granum
P E
PE
D001427:Bacterial Toxins / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D018938:Caco-2 Cells; D002135:Calcium-Binding Proteins; D003016:Clostridium perfringens / Q000472:pathogenicity*; D004305:Dose-Response Relationship, Drug; D006801:Humans; D007473:Ion Channels / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008564:Membrane Potentials / Q000187:drug effects; D011796:Quinacrine / Q000494:pharmacology; D010738:Type C Phospholipases / Q000037:antagonists & inhibitors / Q000494:pharmacology*
D001427:Bacterial Toxins; D002135:Calcium-Binding Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D010738:Type C Phospholipases; C040649:alpha toxin, Clostridium perfringens; D011796:Quinacrine