Ohtsuka H, Horigome K, Ochi H, Nishimoto T, Kozuki T, Kato M, Okuda T, Noguchi H
Laboratory of Biotechnology, Takarazuka Research Center, Sumitomo Chemical Co., Ltd., Hyogo, Japan.
Hybridoma. 1991 Apr;10(2):297-307. doi: 10.1089/hyb.1991.10.297.
Human cell lines producing monoclonal antibodies (MAbs) against Pseudomonas aeruginosa exotoxin A were established by EBV transformation followed by cell fusion. Monoclonal antibody FK-001, IgM (mu, kappa), was demonstrated to be specifically reactive with exotoxin A in ELISA and immunoblotting, by recognizing N-terminal 16 amino acid residues of exotoxin A as an epitope. This epitope region belongs to domain I which is required for the binding of exotoxin A to the receptor on target cells. FK-001 showed a partial neutralizing activity for cell toxicity caused by exotoxin A and appeared to be effective against exotoxin A-producing P. aeruginosa infection in mice. A line of evidence suggests that monoclonal antibody FK-001 neutralizes exotoxin A-induced cell toxicity by the interference of accessibility and/or binding of exotoxin A to animal cell receptors.
通过EBV转化继以细胞融合，建立了产生抗铜绿假单胞菌外毒素A单克隆抗体（MAb）的人细胞系。单克隆抗体FK-001，IgM（μ，κ），在ELISA和免疫印迹中被证明与外毒素A具有特异性反应，通过将外毒素A的N端16个氨基酸残基识别为表位。该表位区域属于结构域I，外毒素A与靶细胞上的受体结合需要该结构域。FK-001对外毒素A引起的细胞毒性表现出部分中和活性，并且似乎对小鼠中产生外毒素A的铜绿假单胞菌感染有效。一系列证据表明，单克隆抗体FK-001通过干扰外毒素A与动物细胞受体的可及性和/或结合来中和外毒素A诱导的细胞毒性。
