Weisbart R H, Noritake D T, Colburn K K, Saxton R E
Department of Medicine, Veterans Administration Medical Centers, Sepulveda, CA 91343.
J Immunol. 1987 Nov 1;139(9):2925-8.
A cloned lymphoblast cell line, hRF-1, that secreted human monoclonal IgG4 rheumatoid factor autoantibody was produced by Epstein-Barr virus transformation of lymphocytes from rheumatoid arthritis synovium. The binding of hRF-1 rheumatoid factor to IgG globulins of different mammalian species was similar to the binding specificity of Staphylococcus aureus protein A (SpA) and to antibodies found in the sera from patients with rheumatoid arthritis. hRF-1 also had the same binding pattern to human IgG subclasses as SpA. Direct competition was observed between SpA and hRF-1 in binding IgG Fc. These results provide evidence for structural homology between a bacterial Fc receptor protein (SpA) and the monoclonal IgG rheumatoid factor.
通过爱泼斯坦-巴尔病毒转化类风湿性关节炎滑膜淋巴细胞产生了一种克隆的淋巴母细胞系hRF-1，它能分泌人单克隆IgG4类风湿因子自身抗体。hRF-1类风湿因子与不同哺乳动物物种的IgG球蛋白的结合类似于金黄色葡萄球菌蛋白A（SpA）的结合特异性，也类似于类风湿性关节炎患者血清中发现的抗体。hRF-1与SpA对人IgG亚类的结合模式也相同。在结合IgG Fc方面，观察到SpA和hRF-1之间存在直接竞争。这些结果为细菌Fc受体蛋白（SpA）与单克隆IgG类风湿因子之间的结构同源性提供了证据。
