Cianfriglia M, Romagnoli G, Tombesi M, Poloni F, Falasca G, Di Modugno F, Castagna M, Chersi A
Laboratorio di Immunologia, Istituto Superiore di Sanità, Rome, Italy.
Int J Cancer. 1995 Mar 29;61(1):142-7. doi: 10.1002/ijc.2910610124.
A new murine monoclonal antibody (MAb), MM6.15, to human MDR1 P-glycoprotein was found to be reactive in ELISA with synthetic peptides selected from the predicted sequences of the first, fourth and sixth extracellular loop of MDR1-P-glycoprotein. In order to precisely define the MM6.15-binding site, a peptide library of overlapping 5- to 9-mer residues covering the entire sixth extracellular loop of both human and rodent class-1 P-glycoproteins was synthesized on polyethylene pins and tested for MAb binding. The results of this ELISA demonstrated that the MAb MM6.15 reacts only with human synthetic peptides and that the critical component of the MAb recognition is made up of the amino-acid sequence LVAHKL (residues 963-968 of the MDR1-P-glycoprotein) with histidine (H), lysine (K) and possibly leucine (L), key residues of this immunogenic domain.
一种针对人多药耐药蛋白1（MDR1）P - 糖蛋白的新型鼠单克隆抗体（MAb）MM6.15，在酶联免疫吸附测定（ELISA）中被发现可与从MDR1 - P - 糖蛋白第一、第四和第六个细胞外环的预测序列中选出的合成肽发生反应。为了精确定义MM6.15的结合位点，在聚乙烯针上合成了覆盖人和啮齿类1类P - 糖蛋白整个第六个细胞外环的重叠5至9聚体残基的肽库，并测试其与单克隆抗体的结合。该ELISA结果表明，单克隆抗体MM6.15仅与人合成肽发生反应，且单克隆抗体识别的关键成分由氨基酸序列LVAHKL（MDR1 - P - 糖蛋白的963 - 968位残基）组成，其中组氨酸（H）、赖氨酸（K）以及可能的亮氨酸（L）是该免疫原性结构域的关键残基。
