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J. Bacteriol., Jan 1996, 537-541, Vol 178, No. 2
Copyright © 1996, American Society for Microbiology

Ultrastructural organization and regulation of a biomaterial adhesin of Staphylococcus epidermidis

GJ Veenstra, FF Cremers, H van Dijk and A Fleer
Eijkman-Winkler Institute of Clinical and Medical Microbiology, Faculty of Medicine, Utrecht, The Netherlands.

Coagulase-negative staphylococci have emerged as important pathogens in infections associated with intravascular devices. Microbial adherence to biomaterial surfaces is a crucial step in the pathogenesis of these infections. Staphylococcal surface proteins (herein referred to as SSP- 1 and SSP-2) are involved in the attachment of Staphylococcus epidermidis 354 to polystyrene. In the present study we show that the adhesin protrudes from the cell surface as a fimbria-like polymer. Furthermore, in vitro proteolytic cleavage of SSP-1 produces an SSP-2- like protein which coincides with a loss of adhesive function. SSP-1 expression is down-regulated in a phenotypical variant of S. epidermidis 354 whereas SSP-2 expression is not. These results could suggest that proteolytic cleavage is a key to the regulation of the adhesive state of S. epidermidis in vivo.


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