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Background   Leptospira interrogans  is a spirochaete responsible for leptospirosis in mammals. The molecular mechanisms of the  Leptospira  virulence remain mostly unknown. Recently, it has been demonstrated that  L. interrogans  ClpB (ClpB Li ) is essential for bacterial survival under stressful conditions and also during infection. The aim of this study was to provide further insight into the role of ClpB in  L. interrogans  and answer the question whether ClpB Li  as a potential virulence factor may be a target of the humoral immune response during leptospiral infections in mammals.    Results  ClpB Li  consists of 860 amino acid residues with a predicted molecular mass of 96.3 kDa and shows multi-domain organization similar to that of the well-characterized ClpB from  Escherichia coli . The amino acid sequence identity between ClpB Li  and  E. coli  ClpB is 52 %. The coding sequence of the  clpB   Li   gene was cloned and expressed in  E. coli  BL21(DE3) strain. Immunoreactivity of the recombinant ClpB Li  protein was assessed with the sera collected from  Leptospira -infected animals and uninfected healthy controls. Western blotting and ELISA analysis demonstrated that ClpB Li  activates the host immune system, as evidenced by an increased level of antibodies against ClpB Li  in the sera from infected animals, as compared to the control group. Additionally, ClpB Li  was found in kidney tissues of  Leptospira- infected hamsters.    Conclusions  ClpB Li  is both synthesized and immunogenic during the infectious process, further supporting its involvement in the pathogenicity of  Leptospira . In addition, the immunological properties of ClpB Li  point to its potential value as a diagnostic antigen for the detection of leptospirosis.

Immunoreactivity of the AAA+ chaperone ClpB from Leptospira interrogans with sera from Leptospira-infected animals