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© Emmanuel Lemichez
Microscopy image showing the formation of large tunnels in a blood vessel endothelial cell induced by a group of bacterial toxins
Publication : Nature communications

The pore structure of Clostridium perfringens epsilon toxin

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 14 Jun 2019

Savva CG, Clark AR, Naylor CE, Popoff MR, Moss DS, Basak AK, Titball RW, Bokori-Brown M

Link to Pubmed [PMID] – 31201325

Nat Commun 2019 06;10(1):2641

Epsilon toxin (Etx), a potent pore forming toxin (PFT) produced by Clostridium perfringens, is responsible for the pathogenesis of enterotoxaemia of ruminants and has been suggested to play a role in multiple sclerosis in humans. Etx is a member of the aerolysin family of β-PFTs (aβ-PFTs). While the Etx soluble monomer structure was solved in 2004, Etx pore structure has remained elusive due to the difficulty of isolating the pore complex. Here we show the cryo-electron microscopy structure of Etx pore assembled on the membrane of susceptible cells. The pore structure explains important mutant phenotypes and suggests that the double β-barrel, a common feature of the aβ-PFTs, may be an important structural element in driving efficient pore formation. These insights provide the framework for the development of novel therapeutics to prevent human and animal infections, and are relevant for nano-biotechnology applications.

https://www.ncbi.nlm.nih.gov/pubmed/31201325