Characterization of protective antigen CbpB as an adhesin and a plasminogen-binding protein of Erysipelothrix rhusiopathiae
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Updated: Jan 25, 2026

Determining Binding Affinity KD of Radiolabeled Antibodies to Immobilized Antigens
Published on: June 23, 2022
Weifeng Zhu1, Chengzhi Cai2, Jingtao Li3
1Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing, China; College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Abstract:
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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