超抗原
融合蛋白
分子生物学
生物
重组DNA
抗原
抗体
主要组织相容性复合体
融合基因
T细胞
免疫系统
免疫学
基因
生物化学
作者
Aruto Ueno,Fumiko Arakawa,Hironori Abe,H Matsumoto,Tetsuichi Kudo,Ryutaro Asano,Kouhei Tsumoto,Izumi Kumagai,Masahide Kuroki,Masahide Kuroki
出处
期刊:PubMed
日期:2002-05-17
卷期号:22 (2A): 769-76
被引量:11
摘要
The bacterial superantigen staphylococcal enterotoxin A (SEA) is an extremely potent activator of T lymphocytes when presented on major histocompatibility complex (MHC) class II molecules. To develop a tumor-specific superantigen for cancer therapy, we constructed a recombinant fusion protein of SEA and the single-chain variable fragment (scFv) of the FU-MK-1 antibody, which recognizes a glycoprotein antigen (termed MK-1 antigen) present on most carcinomas.We employed recombinant DNA techniques to fuse recombinant mutant SEA to an scFv antibody derived from FU-MK-1 and the resulting fusion protein (SEA/FUscFv) was produced by a bacterial expression system, purified with a metal-affinity column, and characterized for its MK-1-binding specificity and its antitumor activity.The SEA/FUscFv fusion protein retained the reactivity with MK-1-expressing tumor cells, introduced a specific cytotoxicity of lymphokine-activated killer T-cells to the tumor cells, and consequently suppressed the tumor growth in a SCID mouse xenograft model.This genetically engineered SEA/FUscFv fusion protein may serve as a potentially useful immunotherapeutic reagent for human MK-1-expressing tumors.
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