The pore structure of Clostridium perfringens epsilon toxin
Savva, C.G. and Clark, A.R and Naylor, Claire E. and Popoff, M.R. and Moss, David and Basak, Ajit K. and Titball, R.W. and Bokori-Brown, M. (2019) The pore structure of Clostridium perfringens epsilon toxin. Nature Communications 10 (1), p. 2641. ISSN 2041-1723.
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Abstract
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.
Metadata
Item Type: | Article |
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School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
Depositing User: | David Moss |
Date Deposited: | 27 Jun 2019 15:53 |
Last Modified: | 02 Aug 2023 17:52 |
URI: | https://eprints.bbk.ac.uk/id/eprint/27946 |
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