Goldfien R D, Chen P P, Fong S, Carson D A
J Exp Med. 1985 Aug 1;162(2):756-61. doi: 10.1084/jem.162.2.756.
Synthetic peptides corresponding to eight individual heavy chain complementarity-determining regions (CDR) of three human monoclonal IgM anti-IgG (rheumatoid factor [RF]) paraproteins elicited rabbit antibodies with markedly different properties. All antisera recognized the immunizing peptide, and several reacted with the isolated IgM heavy chain on immunoblots. However, only the antisera against peptides representing the third CDR bound consistently and specifically to the intact IgM-RF molecule. These data indicate that the third CDR of human mu chains comprises an immunodominant idiotype, and suggest that the D gene segment may be especially important in creating idiotypic diversity. Synthetic peptides corresponding to the third heavy chain CDR of human paraproteins may be clinically useful for the specific induction of antiidiotypic antibodies.
对应于三种人源单克隆 IgM 抗 IgG(类风湿因子 [RF])副蛋白的八个单独重链互补决定区(CDR)的合成肽引发了具有明显不同特性的兔抗体。所有抗血清都识别免疫肽,并且有几种在免疫印迹上与分离的 IgM 重链发生反应。然而,只有针对代表第三个 CDR 的肽的抗血清始终如一地特异性结合完整的 IgM-RF 分子。这些数据表明人μ链的第三个 CDR 包含一个免疫显性独特型,并表明 D 基因片段在产生独特型多样性方面可能特别重要。对应于人副蛋白第三个重链 CDR 的合成肽在临床上可能有助于特异性诱导抗独特型抗体。