Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins.
Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins.
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DOI：
10.1016/j.jmb.2011.07.066
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发表时间：
2011-10-14
影响因子：
5.6
通讯作者：
Basak AK
中科院分区：
文献类型：
--
作者：
Briggs DC;Naylor CE;Smedley JG 3rd;Lukoyanova N;Robertson S;Moss DS;McClane BA;Basak AK
产气荚膜梭菌肠毒素（CPE）是食物中毒和抗生素相关性腹泻的主要原因。从产气荚膜梭菌孢子中释放出来后，CPE在肠壁上皮细胞之间的紧密连接处与受体claudin结合，随后在细胞膜上形成孔。已经观察到CPE和claudin之间有许多不同的配合物，但孔隙形成的过程尚未完全阐明。我们通过x射线晶体学分别以2.7和4.0 Å的分辨率确定了两种晶体形式的CPE可溶性形式的3d结构，并发现n端结构域与气溶素样β-成孔蛋白家族具有结构同源性。我们发现CPE在两种晶体形式中形成三聚体，并且这种三聚体可能具有生物学相关性，但不是活性孔隙形式。我们使用这些数据来讨论孔隙形成模型。
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.
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DOI：
10.1107/s0907444905036693
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