Isolation and characterization of a fibronectin receptor from Staphylococcus aureus.

摘要: Attachment of bacteria to the host tissue is considered a first step in development many infections. Previous studies have shown that fibronectin, protein mediate substrate adhesion eukaryotic cells, also binds some pathogenic and mediates adherence these prokaryotes. In present communication, we report on isolation characterization fibronectin receptor from Staphylococcus aureus strain Newman. A 210-kDa binding was isolated bacterial lysate by affinity chromatography followed gel chromatography. Additional smaller peptides with properties were obtained. These seem represent degradation products large since former dominated when purification carried out absence protease inhibitors. Furthermore, purified staphylococcal V8 generated number retained activity. This observation suggests contains several sites for analysis 29-kDa amino-terminal fragment adsorbed microtiter wells one molecule can bind six nine molecules.