Sveen K, Grov A
Acta Pathol Microbiol Scand B. 1978 Dec;86B(6):369-73. doi: 10.1111/j.1699-0463.1978.tb00058.x.
The mechanism of the leukochemotactic activity of staphylococcal protein A (pA) has been studied by in vitro and in vivo experiments. Protein A alone or mixed with heat-inactivated serum induced no migration of polymorphonuclear leukocytes, demonstrating that pA is not a cytotaxin, but a cytotaxigen. Protein A, activating both pathways of the C system, induced chemotaxis in a C4 deficient serum, but not in a C5 deficient serum. This shows that the chemotactic mediator elaborated is a split product of C5, i.e. C5a. The chemotactic activity of pA observed in the presence of normal sera (in vitro) and in wound chambers (in vivo) was exclusively caused by C activation via reaction with Fc.
已通过体外和体内实验研究了葡萄球菌蛋白A(pA)的白细胞趋化活性机制。单独的蛋白A或与热灭活血清混合时,均未诱导多形核白细胞迁移,这表明pA不是细胞趋化素,而是细胞趋化原。蛋白A激活补体系统的两条途径,在C4缺陷血清中可诱导趋化作用,但在C5缺陷血清中则不能。这表明所产生的趋化介质是C5的裂解产物,即C5a。在正常血清存在下(体外)和伤口小室中(体内)观察到的pA趋化活性完全是由与Fc反应激活补体所致。