The interaction of Clostridium perfringens enterotoxin with receptor claudins.
The interaction of Clostridium perfringens enterotoxin with receptor claudins.
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DOI：
10.1016/j.anaerobe.2016.04.011
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发表时间：
2016-10
期刊：
影响因子：
2.3
通讯作者：
McClane, Bruce A.
中科院分区：
文献类型：
--
作者：
Shrestha, Archana;Uzal, Francisco A.;McClane, Bruce A.
产气荚膜梭菌肠毒素（Clostridium perfringens enterotoxin，CPE）是一种重要的生物学毒素，可引起多种常见的胃肠道疾病。这种35 kDa的单多肽毒素由两个结构域组成：参与受体结合的C-末端结构域和参与寡聚化、膜插入和孔形成的N-末端结构域。CPE的作用始于其与受体的结合，所述受体包括紧密连接蛋白家族的某些成员;结合的CPE然后形成一系列复合物，其中之一是引起负责宿主细胞死亡的钙内流的孔。最近的研究表明，CPE与claudin受体的结合涉及C-末端CPE结构域与claudin受体的第一和第二胞外环（ECL-1和ECL-2）之间的相互作用。对于这种结合特别重要的是ECL-2对接到存在于毒素的C-末端结构域中的口袋中。CPE与claudin受体相互作用的这种增加的理解现在正在促进CPE介导的胃肠道疾病的受体诱饵治疗剂、癌症治疗/诊断试剂和药物递送增强剂的开发。
Clostridium perfringens enterotoxin (CPE) has significant medical importance due to its involvement in several common human gastrointestinal diseases. This 35 kDa single polypeptide toxin consists of two domains: a C-terminal domain involved in receptor binding and an N-terminal domain involved in oligomerization, membrane insertion and pore formation. The action of CPE starts with its binding to receptors, which include certain members of the claudin tight junction protein family; bound CPE then forms a series of complexes, one of which is a pore that causes the calcium influx responsible for host cell death. Recent studies have revealed that CPE binding to claudin receptors involves interactions between the C-terminal CPE domain and both the 1st and 2nd extracellular loops (ECL-1 and ECL-2) of claudin receptors. Of particular importance for this binding is the docking of ECL-2 into a pocket present in the C-terminal domain of the toxin. This increased understanding of CPE interactions with claudin receptors is now fostering the development of receptor decoy therapeutics for CPE-mediated gastrointestinal disease, reagents for cancer therapy/diagnoses and enhancers of drug delivery.
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