Structure of the Food-Poisoning Clostridium perfringens Enterotoxin Reveals Similarity to the Aerolysin-Like Pore-Forming Toxins

JOURNAL OF MOLECULAR BIOLOGY

卷:413

Article

Briggs, David C.¹  Naylor, Claire E.¹  Smedley, James G., III²  Lukoyanova, Natalya¹  Robertson, Susan²  Moss, David S.¹  McClane, Bruce A.²  Basak, Ajit K.¹ 

[1] Univ London Birkbeck Coll, Inst Struct & Mol Biol, Dept Biol Sci, London WC1E 7HX, England

[2] Univ Pittsburgh, Sch Med, Dept Microbiol & Mol Genet, Pittsburgh, PA 15219 USA

关键词: antibiotic-associated diarrhea;    trimer;    claudin;    intestine;    tight junction;   

DOI  :  10.1016/j.jmb.2011.07.066

来源: Elsevier

【 摘 要 】

Clostridium perfringens enterotoxin (CPE) is a major cause of food poisoning and antibiotic-associated diarrhea. 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 three-dimensional structure of the soluble form of CPE in two crystal forms by X-ray crystallography, to a resolution of 2.7 and 4.0 angstrom, respectively, and found that the N-terminal domain shows structural homology with the aerolysin-like beta-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 these data to discuss models of pore formation. (C) 2011 Published by Elsevier Ltd.

【 授权许可】

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