Details

Autor(en) / Beteiligte

• Savva, Christos G.
• Clark, Alice R.
• Naylor, Claire E.
• Popoff, Michel R.
• Moss, David S.
• Basak, Ajit K.
• Titball, Richard W.
• Bokori-Brown, Monika

Titel

The pore structure of Clostridium perfringens epsilon toxin

Ist Teil von

• Nature communications, 2019-06, Vol.10 (1), p.2641-10, Article 2641

Ort / Verlag

London: Nature Publishing Group UK

Erscheinungsjahr

2019

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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. Epsilon toxin (Etx) is a potent pore forming toxin (PFT) produced by Clostridium perfringens. Here authors show the cryo-EM structure of the Etx pore assembled on the membrane of susceptible cells and shed light on pore formation and mutant phenotypes.