Kühnemund O, Havlicek J, Knöll H, Sjöquist J, Köhler W
Acta Pathol Microbiol Immunol Scand B. 1985 Jun;93(3):201-9. doi: 10.1111/j.1699-0463.1985.tb02877.x.
Adsorption chromatography of streptococcal extracts on immobilized fibrinogen allows isolation of components that are linked to the corresponding receptors. In this study it is shown by an indirect bactericidal test that fibrinogen binds the M proteins of the streptococcal strains used. Phage-associated lysin extracts of group A type 1 streptococci precipitated with fibrinogen in a double-diffusion test. Fibrinogen reactive components of other streptococcal types inhibited this precipitation reaction. This suggests that the fibrinogen receptors in different types of group A streptococci have identical activity. The interaction between M protein and fibrinogen does not interfere with the interaction between M protein and the corresponding type specific antibodies. The streptococcal antigen components isolated by immobilized fibrinogen showed mitogenic activity in a lymphocyte transformation test.
将链球菌提取物在固定化纤维蛋白原上进行吸附色谱分析，可分离出与相应受体相连的成分。在本研究中，通过间接杀菌试验表明，纤维蛋白原可结合所用链球菌菌株的M蛋白。A组1型链球菌的噬菌体相关溶素提取物在双向扩散试验中可被纤维蛋白原沉淀。其他链球菌类型的纤维蛋白原反应性成分可抑制这种沉淀反应。这表明不同类型的A组链球菌中的纤维蛋白原受体具有相同的活性。M蛋白与纤维蛋白原之间的相互作用并不干扰M蛋白与相应型特异性抗体之间的相互作用。通过固定化纤维蛋白原分离出的链球菌抗原成分在淋巴细胞转化试验中显示出促有丝分裂活性。
