Newkirk M M
Department of Medicine, McGill University, Montreal, Quebec, Canada.
Scand J Immunol. 1992 Jun;35(6):651-8. doi: 10.1111/j.1365-3083.1992.tb02971.x.
The complete amino acid structure of the variable regions of two monoclonal human rheumatoid factors (RF), antibodies that bind to the Fc portion of IgG, is presented. Although these RFs are of different isotypes, IgG (SFL) and IgM (RIV), they are highly related. They probably derive from the same KIII light chain variable region used, but the heavy chains are derived from genes of the VHIII family that are probably evolutionarily related. An analysis of the level of somatic mutation reveals that antigen selection was probably involved in the maturation of these clones. These antibodies, although highly related, are not merely IgM to IgG switch variants which occurred independently in different individuals. Little is currently known about the structure of IgG RFs and this study indicates that the level of somatic mutation of SFL is similar to other autoantibodies or antiviral antibodies of the IgG isotype.
本文展示了两种单克隆人类风湿因子(RF)可变区的完整氨基酸结构,RF是一种能与IgG的Fc部分结合的抗体。尽管这些RF属于不同的同种型,即IgG(SFL)和IgM(RIV),但它们高度相关。它们可能源自相同的KIII轻链可变区,但其重链源自VHIII基因家族中可能具有进化相关性的基因。对体细胞突变水平的分析表明,抗原选择可能参与了这些克隆的成熟过程。这些抗体虽然高度相关,但并非在不同个体中独立发生的IgM到IgG转换变体。目前对IgG RF的结构了解甚少,本研究表明SFL的体细胞突变水平与IgG同种型的其他自身抗体或抗病毒抗体相似。