Bhat N K, Romano-Spica V, Georgiou P, Chen S L, Kui P G, Suzuki H
Laboratory of Molecular Oncology, National Cancer Institute, Frederick, MD 21702-1201.
Hybridoma. 1994 Feb;13(1):1-8. doi: 10.1089/hyb.1994.13.1.
The epitope for E44 monoclonal antibody (mAb) was mapped using mutated ETS1 proteins lacking different carboxy-terminal regions and by the employment of synthetic oligopeptides spanning the epitope region. This epitope lies around Arg211 of the human ETS1 protein since substitution of Arg211 by Gln211 in the epitope region results in the loss of recognition of the mouse ETS1 protein by E44 mAb. Substitution of Leu214 by valine214 in the epitope region (as is found in the chicken ETS1 and viral Ets proteins) does not alter the capacity of the E44 mAb to recognize this antigen. Taken together, these results suggest that a specific ionic interaction is able to play a pivotal role in the recognition of the ETS1 protein by the E44 mAb.
使用缺乏不同羧基末端区域的突变型ETS1蛋白，并通过使用跨越表位区域的合成寡肽，对E44单克隆抗体（mAb）的表位进行了定位。该表位位于人ETS1蛋白的Arg211附近，因为表位区域中Arg211被Gln211取代会导致E44 mAb对小鼠ETS1蛋白的识别丧失。表位区域中Leu214被valine214取代（如在鸡ETS1和病毒Ets蛋白中发现的那样）不会改变E44 mAb识别该抗原的能力。综上所述，这些结果表明特定的离子相互作用在E44 mAb识别ETS1蛋白中起关键作用。
