Kirkham P A, Takamatsu H, Yang H, Parkhouse R M
Department of Immunology, Institute for Animal Health, Pirbright, Surrey, UK.
Immunology. 1996 Apr;87(4):616-23. doi: 10.1046/j.1365-2567.1996.498566.x.
The cloning, characterization and expression of porcine CD3 epsilon and establishment of its role in T-cell activation using an anti-porcine CD3 epsilon monoclonal antibody, as described here, provides a first step towards a greater understanding of the porcine immune response. Porcine CD3 epsilon was cloned from a porcine T-cell cDNA library by polymerase chain reaction and found to have up to 72% identity with other CD3 epsilon chains, retaining all the necessary primary structural motifs for correct functioning of porcine CD3 epsilon. When expressed in COS7 cells porcine CD3 epsilon was an intracellularly localized, monomeric 23,000 MW protein exhibiting no evidence of N-glycosylation. A monoclonal antibody, PPT3, recognized expressed porcine CD3 epsilon and activated porcine T cells as demonstrated by stimulation of calcium mobilization, an increase in protein tyrosine phosphorylation and proliferation. These results further reaffirm and identify CD3 epsilon as an important cell surface protein involved in signal transduction of activation signals in porcine T cells.
本文所述的猪CD3ε的克隆、特性鉴定、表达以及使用抗猪CD3ε单克隆抗体确定其在T细胞激活中的作用，为更深入了解猪免疫反应迈出了第一步。通过聚合酶链反应从猪T细胞cDNA文库中克隆出猪CD3ε，发现其与其他CD3ε链具有高达72%的同一性，保留了猪CD3ε正确发挥功能所需的所有主要结构基序。当在COS7细胞中表达时，猪CD3ε是一种细胞内定位的单体23,000 MW蛋白，未显示出N-糖基化的迹象。一种单克隆抗体PPT3识别表达的猪CD3ε并激活猪T细胞，这通过钙动员的刺激、蛋白质酪氨酸磷酸化的增加和增殖得到证明。这些结果进一步证实并确定CD3ε是参与猪T细胞激活信号转导的重要细胞表面蛋白。
