Runehagen A, Schönbeck C, Hedner U, Hessel B, Kronvall G
Acta Pathol Microbiol Scand B. 1981 Apr;89(2):49-55. doi: 10.1111/j.1699-0463.1981.tb00151_89b.x.
Binding of fibrinogen degradation products was measured to Gram-positive cocci known to carry receptors for human fibrinogen. Forty-one strains of S. aureus and group A, C and G streptococci were studied. The largest plasmin produced fragment (X-fragment, HMWDP) showed higher binding levels to the bacterial receptors in all four species as compared to intact fibrinogens. The enzymatically produced C-terminal fragment D was strongly reactive, whereas the N-terminal fragment E was non-reactive. Inhibition experiments showed that reactive fragments were bound to the same receptors as fibrinogen. Three chemically-produced and well-characterized fragments from the terminal and the middle portions of the fibrinogen molecule were all negative in binding assays. The binding patterns for fibrinogen and the fragments tested were identical in the four bacterial species tested, S. aureus and group A, C and G streptococci. The results confirm and extend earlier data on similarities between fibrinogen receptors on these Gram-positive bacterial species.
对已知携带人纤维蛋白原受体的革兰氏阳性球菌进行纤维蛋白原降解产物结合检测。研究了41株金黄色葡萄球菌以及A、C、G组链球菌。与完整纤维蛋白原相比，最大的纤溶酶产生片段（X片段，高分子量降解产物）在所有这四个菌种中对细菌受体的结合水平更高。酶促产生的C端片段D具有强烈反应性，而N端片段E无反应性。抑制实验表明，反应性片段与纤维蛋白原结合到相同的受体上。来自纤维蛋白原分子末端和中间部分的三个化学合成且特性明确的片段在结合试验中均呈阴性。在测试的四种细菌菌种（金黄色葡萄球菌以及A、C、G组链球菌）中，纤维蛋白原和测试片段的结合模式相同。这些结果证实并扩展了关于这些革兰氏阳性细菌菌种上纤维蛋白原受体之间相似性的早期数据。
