Shemiakin I G, Anisimova V A, Mitrofanova G N
Mol Biol (Mosk). 1992 Sep-Oct;26(5):1088-98.
Recombinant fusion proteins consist of the N-terminal 488 or 513 amino acids of diphtheria toxin joined to human interleukin 2. Initially those fusion proteins were expressed in E. coli under the control of the tox promotor. Western blot analyses showed that E. coli strains bearing the hybrid genes produce 68 kDa or 72 kDa fusion proteins that retain the immunological determinants of both the diphtheria toxin component and the interleukin 2 component. The fusion protein with mol. mass 72 kDa was partially purified by affinity chromatography. The expression of the fusion proteins under the control of the strong promotors was increased (100-fold for tac- promotor) compared to that under the control of the tox promotor. DT-IL2 might be a useful cytotoxic agent in the treatment of diseases involving IL2 receptor-positive cells, such as allograft rejection, graft-versus-host disease, multiple sclerosis et al.
重组融合蛋白由白喉毒素的N端488或513个氨基酸与人类白细胞介素2连接而成。最初，这些融合蛋白在大肠杆菌中由tox启动子控制表达。蛋白质免疫印迹分析表明，携带杂交基因的大肠杆菌菌株产生68 kDa或72 kDa的融合蛋白，这些融合蛋白保留了白喉毒素成分和白细胞介素2成分的免疫决定簇。分子量为72 kDa的融合蛋白通过亲和层析进行了部分纯化。与tox启动子控制下的表达相比，在强启动子控制下融合蛋白的表达增加了（tac启动子控制下增加了100倍）。DT-IL2可能是治疗涉及IL2受体阳性细胞的疾病（如同种异体移植排斥、移植物抗宿主病、多发性硬化症等）的一种有用的细胞毒性药物。
