Adhesive properties of Clostridium perfringens to extracellular matrix proteins collagens and fibronectin
Adhesive properties of Clostridium perfringens to extracellular matrix proteins collagens and fibronectin
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DOI：
10.1016/j.anaerobe.2013.11.002
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发表时间：
2014-02-01
期刊：
影响因子：
2.3
通讯作者：
Katayama, Seiichi
中科院分区：
文献类型：
--
作者：
Hitsumoto, Yasuo;Morita, Naomi;Katayama, Seiichi
研究了产气荚膜梭菌对胶原、明胶、纤维连接蛋白（Fn）、Fn-预结合胶原和Fn-预结合明胶的粘附特性。C.产气荚膜杆菌可与Fn预结合的II型、III型胶原和明胶结合，但不与明胶或除I型胶原外的其他胶原直接结合。重组C.产气荚膜杆菌rFbpA和rFbpB用于检查Fn介导的细菌对I型胶原的粘附。在rFbps存在下，C.产气荚膜杆菌对Fn预结合的I型胶原蛋白的粘附以剂量依赖性方式被抑制。Fn不因rFbps的存在而从包被的I型胶原蛋白中释放，并且rFbps不与I型胶原蛋白结合。因此，C.产气荚膜杆菌通过rFbps与Fn-预结合的I型胶原蛋白的结合不能用Fn从胶原蛋白中的去除或rFbps与胶原蛋白的竞争性结合来解释。相反，发现两种rFbp都与C结合。产气荚膜杆菌这些结果提示rFbp可能与C.产气荚膜梭菌并竞争性抑制Fn与C.产气荚膜杆菌(C)2013爱思唯尔有限公司保留所有权利。
The adhesive properties of Clostridium perfringens to collagens, gelatin, fibronectin (Fn), Fn-prebound collagens, and Fn-prebound gelatin were investigated. C. perfringens could bind to Fn-prebound collagen type II, type III, and gelatin, but not to gelatin or collagens except for collagen type I directly. Recombinant Fn-binding proteins of C. perfringens, rFbpA and rFbpB, were used to examine Fn-mediated bacterial adherence to collagen type I. In the presence of rFbps, C. perfringens adherence to Fn-prebound collagen type I was inhibited in a dose-dependent manner. Fn was not released from the coated collagen type I by the presence of rFbps, and rFbps did not bind to collagen type I. Thus, the inhibition of C. perfringens binding to Fn-prebound collagen type I by rFbps could not be explained by the removal of Fn from collagen or by the competitive binding of rFbps to collagen. Instead, both rFbps were found to bind to C. perfringens. These results suggest the possibility that rFbps may bind to the putative Fn receptor expressed on C. perfringens and competitively inhibit Fn binding to C. perfringens. (C) 2013 Elsevier Ltd. All rights reserved.