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Infection by Staphylococcus epidermidis, anopportunistic pathogen, has become a major problem due to the increased use ofimplanted medical devices and the growing number of patients who aretherapeutically or infectiously immunosuppressed. These infections appear toproceed via modulation of the coagulation and complement systems. In thiscommunication we describe the purification and characterization of a novelextracellular proteinase from an oral strain of S. epidermidis that can degradefibrinogen, complement protein C5, and several other proteins. This proteinasehas a strong preference for cleavage after glutamic acid residues, but notafter aspartic acid. The S. epidermidis enzyme may be a multifunctional proteinwhich not only provides this organism with both the ability to evade thecomplement defense system and to dysregulate the coagulation cascade, but alsosupplies nutrients for its growth through the degradation of Glurichproteins.

Isolation and Characterization of a Highly Specific Serine Endopeptidase from an Oral Strain of Staphylococcus epidermidis