DIPHTHERIA-TOXIN RECEPTOR-BINDING DOMAIN SUBSTITUTION WITH INTERLEUKIN-2 - GENETIC CONSTRUCTION AND PROPERTIES OF A DIPHTHERIA TOXIN-RELATED INTERLEUKIN-2 FUSION PROTEIN
DIPHTHERIA-TOXIN RECEPTOR-BINDING DOMAIN SUBSTITUTION WITH INTERLEUKIN-2 - GENETIC CONSTRUCTION AND PROPERTIES OF A DIPHTHERIA TOXIN-RELATED INTERLEUKIN-2 FUSION PROTEIN
复制标题
DOI：
10.1093/protein/1.6.493
复制
发表时间：
1987-12-01
期刊：
影响因子：
--
通讯作者：
MURPHY, JR
中科院分区：
文献类型：
--
作者：
WILLIAMS, DP;PARKER, K;MURPHY, JR
我们已经用编码白细胞介素-2（IL-2）和翻译终止信号的合成基因在遗传上取代了白喉毒素受体结合结构域。白喉毒素相关T细胞生长因子融合基因编码70个586-d多肽，即IL-2-毒素原。IL-2-毒素的成熟形式具有推导的mol. wt为68，086，并显示输出到大肠杆菌（pABI 508）的周质区室，并含有其白喉毒素和IL-2组分固有的免疫决定簇。从重组大肠杆菌的周质提取物中纯化了IL-2毒素。coli（pABI 508）中进行免疫亲和层析。纯化的嵌合毒素显示出选择性抑制携带IL-2受体的靶细胞中的蛋白质合成，而不表达IL-2受体的细胞系对IL-2毒素的作用具有抗性。
We have genetically replaced the diphtheria toxin receptor binding domain with a synthetic gene encoding interleukin-2 (IL-2) and a translational stop signal. The diptheria toxin-related T-cell growth factor fusion gene encodes of 70 586-d polypeptide, pro-IL-2-toxin. The mature form of IL-2- toxin has a deduced mol. wt of 68,086 and is shown to be exported to the periplasmic compartment of Escherichia coli (pABI508), and contain immunologic determinants intrinsic to both its diphtheria toxin and IL-2 components. IL-2-toxin has been purified from periplasmic etracts of recombinant strains of E. coli (pABI508) by immunoaffinity chromatography using immobilized anti-IL-2. The purified chimeric toxin is shown to selectively inhibit protein synthesis in IL-2 receptor bearing targeted cells, whereas cell lines which do not express the IL-2 receptor are resistant to IL-2 toxin action.