Streptococcus suis is an important zoonotic pathogen worldwide and is responsible for disease in swine and humans. In the present study, we identified and characterised a surface-associated peptidase (abpb, amylase-binding protein B) in Streptococcus suis serotype 2 (S. suis 2) that has high hydrolytic activity towards H-Arg-pNa, with maximum activity at pH 7.0. Stimulation of RAW 264.7 macrophages with purified recombinant abpb protein triggered the release of pro-inflammatory cytokines. An abpb-deficient mutant ΔAbpb was constructed by homologous recombination to determine the role of abpb in S. suis 2. The mutant ΔAbpb showed decreased adherence to Hep-2 cells and attenuated virulence in a mouse model compared to the wild type strains. The results of the infection showed impaired bacterial growth in vivo and poor colonisation of the organs. In a protection assay, the recombinant abpb provided excellent protection against a lethal challenge of S. suis 2. Together, these findings suggest that abpb contributes to the pathogenicity of S. suis 2 and may be another target for S. suis prevention and control.
Keywords: Antigen; Arginine peptidase; Pathogenicity; Streptococcus suis; Streptococcus suis serotype 2.
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