Tunnacliffe A, Olsson C, de la Hera A
Basel Institute for Immunology, Switzerland.
Int Immunol. 1989;1(5):546-50. doi: 10.1093/intimm/1.5.546.
Transgenic mouse T cells expressing the human CD3 epsilon chain bind the majority (29/36) of monoclonal antibodies (mAbs) specific for human CD3. A proportion of these mAbs are also able to recognize isolated CD3 epsilon in a soluble, recombinant form. Thus, CD3 epsilon can confer most CD3 epitopes on the TCR--CD3 complex, but many determinants may require assembly of the complex for their formation. A number of mAbs did not recognize epsilon-transgenic T cells and probably need other CD3 subunits for binding. CD3-specific mAbs from each of the three groups defined here, as well as mAbs directed against the TCR alpha beta heterodimer, are all able to activate T cells. Therefore mAb attachment at several different sites on the TCR--CD3 complex can give rise to activation signals. This suggests that the cross-linking function of mitogenic antibodies may be their most significant property, rather than the perturbation of a particular 'functional epitope'.
表达人CD3ε链的转基因小鼠T细胞能结合大多数（29/36）针对人CD3的单克隆抗体（mAb）。其中一部分mAb也能够识别可溶性重组形式的分离CD3ε。因此，CD3ε可以在TCR - CD3复合物上赋予大多数CD3表位，但许多决定簇可能需要复合物组装才能形成。一些mAb不能识别ε转基因T细胞，可能需要其他CD3亚基来进行结合。这里定义的三组中的每一组的CD3特异性mAb，以及针对TCRαβ异二聚体的mAb，都能够激活T细胞。因此，mAb在TCR - CD3复合物上的几个不同位点结合可以产生激活信号。这表明促有丝分裂抗体的交联功能可能是其最重要的特性，而不是对特定“功能表位”的干扰。
