Diversity in the CDR3 region of VH is sufficient for most antibody specificities
Diversity in the CDR3 region of VH is sufficient for most antibody specificities
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DOI：
10.1016/s1074-7613(00)00006-6
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发表时间：
2000-07-01
期刊：
影响因子：
32.4
通讯作者：
Davis, MM
中科院分区：
文献类型：
--
作者：
Xu, JL;Davis, MM
所有重排抗原受体基因在通常形成配体结合表面的六个互补决定区（CDR）中具有一个或两个高度多样的互补决定区（CDR）。我们在这里报告，在抗体的情况下，在这些区域之一，V-H结构域的CDR 3的多样性，是足以允许其他相同的IgM分子，以区分各种半抗原和蛋白质抗原。此外，我们发现，体细胞突变可以允许这样的抗体实现令人惊讶的高亲和力。这些结果与其中高度多样的CDR 3环是T细胞受体（TCR）和抗体中抗原识别特异性的关键决定因素的模型一致，而种系编码的CDR 1和CDR 2序列具有更强的交叉反应性。
All rearranging antigen receptor genes have one or two highly diverse complementarity determining regions (CDRs) among the six that typically form the ligand binding surface. We report here that, in the case of antibodies, diversity at one of these regions, CDR3 of the V-H domain, is sufficient to permit otherwise identical IgM molecules to distinguish between a variety of hapten and protein antigens. Furthermore, we find that somatic mutation can allow such antibodies to achieve surprisingly high affinities. These results are consistent with a model in which the highly diverse CDR3 loops are the key determinant of specificity in antigen recognition in both T cell receptors (TCR) and antibodies, whereas the germline-encoded CDR1 and CDR2 sequences are much more cross-reactive.