Ultrastructural organization and regulation of a biomaterial adhesin of Staphylococcus epidermidis.
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.
Veenstra
G J
GJ
Eijkman-Winkler Institute of Clinical and Medical Microbiology, Faculty of Medicine, Utrecht, The Netherlands.
Cremers
F F
FF
van Dijk
H
H
Fleer
A
A
D018829:Adhesins, Bacterial / Q000032:analysis / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D001422:Bacterial Adhesion / Q000502:physiology*; D001672:Biocompatible Materials; D002404:Catheterization; D015536:Down-Regulation; D010861:Fimbriae, Bacterial / Q000737:chemistry; D006801:Humans; D008863:Microspheres; D008970:Molecular Weight; D011137:Polystyrenes; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013212:Staphylococcus epidermidis / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure; D014357:Trypsin / Q000378:metabolism
D018829:Adhesins, Bacterial; D001672:Biocompatible Materials; D011137:Polystyrenes; D012710:Serum Albumin, Bovine; D014357:Trypsin