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Staphylococcus epidermidis , a Gram-positive, coagulase-negative bacterium is a predominant inhabitant of human skin and mucous membranes. Recently, however, it has become one of the most important agents of hospital-acquired bacteriemia, as it has been found to be responsible for surgical wound infections developed in individuals with indwelling catheters or prosthetic devices, as well as in immunosupressed or neutropenic patients. Despite their medical significance, little is known about proteolytic enzymes of  S. epidermidis  and their possible contribution to the bacteriums pathogenicity; however, it is likely that they function as virulence factors in a manner similar to that proposed for the proteases of  Staphylococcus aureus . Here we describe the purification of a cell wall-associated cysteine protease from  S. epidermidis , its biochemical properties and specificity. A homology search using N-terminal sequence data revealed similarity to staphopain A (ScpA) and staphopain B (SspB), cysteine proteases from  S. aureus . Moreover, the gene encoding  S. epidermidis  cysteine protease (Ecp) and a downstream gene coding for a putative inhibitor of the protease form an operon structure which resembles that of staphopain A in  S. aureus . The active cysteine protease was detected on the bacterial cell surface as well as in the culture media and is apparently produced in a growth phase-dependent manner, with initial expression occurring in the midlogarithmic phase. This enzyme, with elastinolytic properties, as well as the ability to cleave α1PI, fibrinogen and fibronectin, may possibly contribute to the invasiveness and pathogenic potential of  S. epidermidis .

Growth phase-dependent production of a cell wall-associated elastinolytic cysteine proteinase by Staphylococcus epidermidis