Briggs, David C. and Naylor, Claire E. and Smedley, J.G. and Lukoyanova, Natalya and Robertson, S. and Moss, David S. and McClane, B.A. and Basak, Ajit K. (2011) Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins. Journal of Molecular Biology 413 (1), pp. 138-149. ISSN 0022-2836.Full text not available from this repository.
Clostridium perfringens enterotoxin (CPE) is a major cause of food poisoning and antibiotic-associated diarrhoea. Upon its release from C. perfringens spores, CPE binds to its receptor, claudin, at the tight junctions between the epithelial cells of the gut wall, and subsequently forms pores in the cell membranes. A number of different complexes between CPE and claudin have been observed and the process of pore-formation has not been fully elucidated. We have determined the 3D-structure of the soluble form of CPE in two crystal forms by X-ray crystallography, to a resolution of 2.7 and 4.0 Å respectively, and found that the N-terminal domain shows structural homology with the aerolysin-like β-pore-forming family of proteins. We show that CPE forms a trimer in both crystal forms and that this trimer is likely to be biologically relevant but is not the active pore form. We use this data to discuss models of pore formation.
|Keyword(s) / Subject(s):||Antibiotic associated diarrhoea, spores, claudin, intestine, tight-junction, trime|
|School or Research Centre:||Birkbeck Schools and Research Centres > School of Science > Biological Sciences|
|Date Deposited:||08 Aug 2011 08:47|
|Last Modified:||11 Oct 2016 12:01|
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