Siegall C B, Chaudhary V K, FitzGerald D J, Pastan I
National Institutes of Health, Laboratory of Molecular Biology, Bethesda, MD 20892.
Proc Natl Acad Sci U S A. 1988 Dec;85(24):9738-42. doi: 10.1073/pnas.85.24.9738.
A chimeric toxin composed of human interleukin 6 (IL-6) attached to a portion of Pseudomonas exotoxin (PE) devoid of its own cell recognition domain has been produced in Escherichia coli. The fusion protein (IL-6-PE40) is cytotoxic to a human myeloma cell line expressing IL-6 receptors but has no effect on IL-6 receptor-negative cells. The specificity of IL-6-PE40 cytotoxicity was demonstrated through competition with excess IL-6 and neutralization with an antibody to IL-6. IL-6-PE40 may be useful in the selective elimination of myeloma cells and other cells with high numbers of IL-6 receptors.
一种嵌合毒素已在大肠杆菌中产生,该毒素由连接到绿脓杆菌外毒素(PE)一部分上的人白细胞介素6(IL-6)组成,PE自身的细胞识别域已缺失。融合蛋白(IL-6-PE40)对表达IL-6受体的人骨髓瘤细胞系具有细胞毒性,但对IL-6受体阴性细胞没有影响。通过与过量IL-6竞争以及用抗IL-6抗体中和,证明了IL-6-PE40细胞毒性的特异性。IL-6-PE40可能有助于选择性消除骨髓瘤细胞和其他具有大量IL-6受体的细胞。