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Characterization of protective antigen CbpB as an adhesin and a plasminogen-binding protein of Erysipelothrix rhusiopathiae

文献类型： 外文期刊

作者： Zhu, Weifeng 1 ; Cai, Chengzhi 2 ; Li, Jingtao 2 ; Zhang, Qiang 4 ; Huang, Jingjing 2 ; Jin, Meilin 2 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Vet Med, Nanjing, Jiangsu, Peoples R China

2.Huazhong Agr Univ, Coll Vet Med, Wuhan, Hubei, Peoples R China

3.Minist Agr, Key Lab Dev Vet Diagnost Prod, Wuhan, Hubei, Peoples R China

4.Cooperat Innovat Ctr Sustainable Pig Prod, Wuhan, Hubei, Peoples R China

5.Huazhong Agr Univ, Coll Life Sci Technol, Wuhan, Hubei, Peoples R China

关键词： Adhesin; CbpB; Endothelial cell; Fibronectin; Plasminogen

期刊名称：RESEARCH IN VETERINARY SCIENCE （ 影响因子：2.534； 五年影响因子：2.382 ）

ISSN： 0034-5288

年卷期： 2019 年 124 卷

页码：

收录情况： SCI

摘要： Erysipelothrix rhusiopathiae is the causative agent of animal erysipelas and human erysipeloid. E. rhusiopathiae CbpB has been reported to be a protective antigen, but its pathogenic roles are not known. The aim of this study was to evaluate the ability of CbpB to act as an adhesin in E. rhusiopathiae adhesion to porcine endothelial cells as well as a host plasminogen- and fibronectin- binding protein. Recombinant CbpB (rCbpB) was successfully obtained, and it was found that E. rhusiopathiae CbpB was located on the cell surface of E. rhusiopathiae. Moreover, CbpB exhibited binding activity to porcine endothelial cells. Recombinant CbpB successfully bound to host plasminogen but was unable to bind to fibronectin. In conclusion, our work suggested that CbpB is a virulence factor of E. rhusiopathiae.

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