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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Erysipelothrix rhusiopathiae recruits host plasminogen via the major protective antigen SpaA
Weifeng Zhu1,2, Ya Wang1,2, Chengzhi Cai1,2
1Animal Infectious Disease Unit, National State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Abstract:
Erysipelothrix rhusiopathiae is the causative agent of animal erysipelas and human erysipeloid. Some pathogenic bacteria are able to recruit host plasminogen and then use the plasminogen system for migration across tissue barriers or for nutritional demands during infection. However, there is no study on E. rhusiopathiae recruitment of plasminogen. SpaA has long been known to be a major protective antigen of E. rhusiopathiae, but its roles in virulence have not yet been well clarified. The aim of this study was to detect the activity of E. rhusiopathiae to recruit host plasminogen and evaluate the ability of SpaA to act as a receptor in the recruitment process. It was found that E. rhusiopathiae could recruit host plasminogen. SpaA could specifically bind host plasminogen. Anti-SpaA serum could significantly decrease the activity of E. rhusiopathiae to recruit plasminogen. In addition, this binding activity was lysine dependent. In conclusion, E. rhusiopathiae was able to recruit host plasminogen via SpaA. To our knowledge, this is the first report on E. rhusiopathiae recruitment of host plasminogen and the receptor in the process.
Insights
Erysipelothrix rhusiopathiae recruits host plasminogen, a process mediated by the SpaA protein. This finding reveals a novel virulence mechanism for this bacterium, impacting animal erysipelas and human erysipeloid infections.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Erysipelothrix rhusiopathiae causes animal erysipelas and human erysipeloid.
- Pathogenic bacteria often utilize host plasminogen for virulence, aiding in tissue migration and nutrient acquisition.
- The role of E. rhusiopathiae's major protective antigen, SpaA, in virulence remains unclear.
Purpose of the Study:
- To investigate the ability of E. rhusiopathiae to recruit host plasminogen.
- To determine if SpaA acts as a receptor for plasminogen recruitment.
- To elucidate the mechanism of plasminogen binding.
Main Methods:
- Detection of plasminogen recruitment by E. rhusiopathiae.
- Assessment of SpaA's specific binding to host plasminogen.
- Evaluation of anti-SpaA serum's effect on plasminogen recruitment.
- Analysis of lysine dependency for binding.
Main Results:
- Erysipelothrix rhusiopathiae demonstrated the ability to recruit host plasminogen.
- SpaA was identified as a specific binding protein for host plasminogen.
- Inhibition of SpaA significantly reduced plasminogen recruitment.
- Plasminogen binding was dependent on lysine.
Conclusions:
- Erysipelothrix rhusiopathiae recruits host plasminogen through its SpaA protein.
- This represents the first report of plasminogen recruitment by E. rhusiopathiae and identification of its receptor.
- SpaA plays a role in the virulence of E. rhusiopathiae by facilitating plasminogen binding.
