Lantz M S, Switalski L M, Kornman K S, Höök M
J Bacteriol. 1985 Aug;163(2):623-8. doi: 10.1128/jb.163.2.623-628.1985.
The binding of Bacteroides intermedius VPI 8944 to human fibrinogen has been characterized. The binding is time dependent, at least partially reversible, saturable, and specific. On an average, a maximum of 3,500 fibrinogen molecules bind per bacterial cell, with a dissociation constant of 1.7 X 10(-11) M. These bacteria also exhibit a fibrinogenolytic activity which can be partially inhibited by protease inhibitors. Bacteria release fibrinogenolytic activity into the surrounding medium without loss of binding activity, but more pronounced fibrinogen breakdown occurs when 125I-labeled fibrinogen is associated with the bacteria, suggesting that fibrinogen is degraded at the cell surface. Fibrinogen binding by B. intermedius might represent a mechanism of bacterial tissue adherence.
中间拟杆菌VPI 8944与人纤维蛋白原的结合特性已得到表征。这种结合具有时间依赖性,至少部分可逆、可饱和且具有特异性。平均而言,每个细菌细胞最多结合3500个纤维蛋白原分子,解离常数为1.7×10⁻¹¹ M。这些细菌还表现出纤维蛋白原溶解活性,蛋白酶抑制剂可部分抑制该活性。细菌将纤维蛋白原溶解活性释放到周围培养基中,而结合活性不会丧失,但当¹²⁵I标记的纤维蛋白原与细菌结合时,会发生更明显的纤维蛋白原降解,这表明纤维蛋白原在细胞表面被降解。中间拟杆菌与纤维蛋白原的结合可能代表了细菌组织黏附的一种机制。