Veenstra G J, Cremers F F, van Dijk H, Fleer A
Eijkman-Winkler Institute of Clinical and Medical Microbiology, Faculty of Medicine, Utrecht, The Netherlands.
J Bacteriol. 1996 Jan;178(2):537-41. doi: 10.1128/jb.178.2.537-541.1996.
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.
凝固酶阴性葡萄球菌已成为与血管内装置相关感染中的重要病原体。微生物对生物材料表面的黏附是这些感染发病机制中的关键步骤。葡萄球菌表面蛋白（在此称为SSP-1和SSP-2）参与表皮葡萄球菌354对聚苯乙烯的黏附。在本研究中，我们表明黏附素以菌毛样聚合物的形式从细胞表面突出。此外，SSP-1的体外蛋白水解切割产生一种与黏附功能丧失一致的SSP-2样蛋白。SSP-1的表达在表皮葡萄球菌354的一个表型变体中下调，而SSP-2的表达则不然。这些结果可能表明蛋白水解切割是体内调节表皮葡萄球菌黏附状态的关键。
