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首页> 外文期刊>Journal of Neuroimmunology: Official Bulletin of the Research Committee on Neuroimmunology of the World Federation of Neurology >Epitope specificity of demyelinating monoclonal autoantibodies directed against the human myelin oligodendrocyte glycoprotein (MOG).
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Epitope specificity of demyelinating monoclonal autoantibodies directed against the human myelin oligodendrocyte glycoprotein (MOG).

机译：针对人髓磷脂少突胶质细胞糖蛋白（MOG）的脱髓鞘单克隆自身抗体的表位特异性。

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摘要

We describe the epitope specificity of a panel of ten demyelinating monoclonal antibodies (mAb) that recognise the extracellular immunoglobulin-like domain of human myelin oligodendrocyte glycoprotein (hMOG(lgd)). All the mAbs bind to the surface of MOG-transfected fibroblasts as assessed in vitro by FACS and immunocytochemistry but failed to recognise overlapping 15-mer MOG peptides when assessed by ELISA. However, increasing peptide length to 25 amino acids revealed that four mAbs recognised epitopes within the amino acid sequence 63-100 of human MOG. In contrast, a non-demyelinating MOG-specific mAb recognised MOG by both ELISA and Western blotting but failed to stain MOG transfected fibroblasts. These observations suggest that assays based on the use of MOG-transfected cell lines will differentiate between pathogenic and non-pathogenic MOG-specific antibody responses in experimental models and human diseases of the nervous system.
机译：我们描述了识别人髓磷脂少突胶质细胞糖蛋白（hMOG（lgd））的细胞外免疫球蛋白样域的十个脱髓鞘单克隆抗体（mAb）面板的表位特异性。如通过FACS和免疫细胞化学方法在体外评估，所有mAb均与转染MOG的成纤维细胞表面结合，但通过ELISA评估时，无法识别重叠的15-mer MOG肽。然而，将肽长度增加至25个氨基酸表明，四个mAb识别人MOG的氨基酸序列63-100内的表位。相反，非脱髓鞘的MOG特异性mAb通过ELISA和Western印迹都能识别MOG，但无法染色MOG转染的成纤维细胞。这些观察结果表明，基于使用MOG转染的细胞系的测定将区分实验模型和神经系统人类疾病中的致病性和非致病性MOG特异性抗体反应。

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