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Molecular basis of toxicity of Clostridium perfringens epsilon toxin

Bokori-Brown, M. and Savva, Christos G. and Fernandes da Costa, S.P. and Naylor, Claire E. and Basak, Ajit K. and Titball, R.W. (2011) Molecular basis of toxicity of Clostridium perfringens epsilon toxin. FEBS Journal 278 (23), pp. 4589-4601. ISSN 1742-464X.

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Official URL: http://dx.doi.org/10.1111/j.1742-4658.2011.08140.x

Abstract

Clostridium perfringensε-toxin is produced by toxinotypes B and D strains. The toxin is the etiologic agent of dysentery in newborn lambs, but is also associated with enteritis and enterotoxaemia in goats, calves and foals. It is also considered to be a potential biowarfare or bioterrorism agent by the U.S. Government Centres for Disease Control and Prevention. The relatively inactive 32.9 kDa prototoxin is converted to active mature toxin by proteolytic cleavage, either by digestive proteases of the host, such as trypsin and chymotrypsin, or by C. perfringensλ-protease. In vivo, the toxin appears to target the brain and kidneys, but relatively few cell lines are susceptible to the toxin, and most work has been carried out using Madin-Darby Canine Kidney (MDCK) cells. The binding of ε-toxin to MDCK cells and rat synaptosomal membranes is associated with the formation of a stable, high molecular weight complex. The crystal structure of ε-toxin reveals similarity to aerolysin from Aeromonas hydrophila, parasporin-2 from Bacillus thuringiensis, and a lectin from Laetiporus sulphurous. Like these toxins, ε-toxin appears to form heptameric pores in target cell membranes. The exquisite specificity of the toxin for specific cell types suggests that it binds to a receptor found only on these cells.

Item Type: Article
Keyword(s) / Subject(s): Clostridium perfringens, crystal structure, enterotoxaemia, epsilon toxin, pore-forming
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 24 May 2011 09:48
Last Modified: 30 Aug 2013 09:12
URI: http://eprints.bbk.ac.uk/id/eprint/3326

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