Identification, Cloning, and Characterization ofStaphylococcus pseudintermediusCoagulase
ABSTRACTCoagulase activation of prothrombin by staphylococcus induces the formation of fibrin deposition that facilitates the establishment of infection byStaphylococcusspecies. Coagulase activity is a key characteristic ofStaphylococcus pseudintermedius; however, no coagulase gene or associated protein has been studied to characterize this activity. We report a recombinant protein sharing 40% similarity toStaphylococcus aureuscoagulase produced from a putativeS. pseudintermediuscoagulase gene. Prothrombin activation by the protein was measured with a chromogenic assay using thrombin tripeptide substrate. Stronger interaction with bovine prothrombin than with human prothrombin was observed. TheS. pseudintermediuscoagulase protein also bound complement C3 and immunoglobulin. Recombinant coagulase facilitated the escape ofS. pseudintermediusfrom phagocytosis, presumably by forming a bridge between opsonizing antibody, complement, and fibrinogen. Evidence from this work suggests thatS. pseudintermediuscoagulase has multifunctional properties that contribute to immune evasion that likely plays an important role in virulence.