Richert J R, Robinson E D, Deibler G E, Martenson R E, Dragovic L J, Kies M W
Department of Neurology, Georgetown University Medical Center, Washington, DC 20007.
Ann Neurol. 1989 Sep;26(3):342-6. doi: 10.1002/ana.410260306.
Previous studies with a panel of myelin basic protein (MBP)-specific human T-cell clones suggested a clustering of epitopes in the middle and at the C terminus of the molecule. The current study demonstrates that 19 of 40 clones recognize a synthetic peptide corresponding to residues 152 to 170 of the human MBP molecule and that 9 clones recognize a synthetic peptide corresponding to residues 86 to 105. Myelin basic protein-specific cytotoxic activity was restricted to the clones that recognized peptide 152-170, and this peptide served as a preferential cytotoxic T-cell target when attached to an autologous B-cell line. The specificity of MBP-directed cytotoxic activity appears to be much more restricted than the specificity demonstrated for proliferative activity.
此前针对一组髓鞘碱性蛋白(MBP)特异性人T细胞克隆开展的研究表明,表位在该分子的中部和C端聚集。当前研究表明,40个克隆中有19个识别对应于人MBP分子第152至170位残基的合成肽,9个克隆识别对应于第86至105位残基的合成肽。髓鞘碱性蛋白特异性细胞毒性活性仅限于识别肽152 - 170的克隆,且当该肽连接至自体B细胞系时,可作为优先的细胞毒性T细胞靶点。MBP导向的细胞毒性活性的特异性似乎比增殖活性所显示的特异性受到更多限制。