SBP2 plays an important role in the virulence changes of different artificial mutants of Streptococcus suis.

Streptococcus suis (SS) is an important bacterial zoonotic pathogen, which can cause infections in pigs and humans. However, the pathogenesis of this bacterium remains unclear, even though some putative virulence factors (VFs) have been reported. Comparative proteomics could be used to identify markers that can distinguish bacterial strains with different virulence; however, the application of this method is restricted by the genome diversities existing in different strains. In this study, two mutants, WT ΔpepT and WT ΔrfeA, which were generated from the same wild-type (WT) strain, ZY05719, and showed opposite virulence tendencies, were constructed. Combining two proteomics assays, two-dimensional difference gel electrophoresis (2D-DIGE) and label-free proteomics, we identified 38 differentially abundant proteins in the mutants compared with their parent, including five known VFs of S. suis and 33 novel elements. One of the novel proteins, a putative pilus protein, named SBP2, was considered as the most promising VF, because SBP2 was not only linked with the known VFs in the virulence interaction network and was proposed to be located on the cell surface, but also showed enriched distribution among highly virulent strains of SS. SBP2 could also bind fibronectin and laminin, two important extracellular matrix proteins of the host, to facilitate the process of adhesion. Thus, spb2 was identified as encoding a promising virulence-associated candidate associated with the pathogenesis of SS, and a comprehensive virulence interaction network of SS was established for the first time.