Glaser S M, Vásquez M, Payne P W, Schneider W P
Protein Design Labs, Inc., Mountain View, CA 94043.
J Immunol. 1992 Oct 15;149(8):2607-14.
The genetically engineered "humanized" anti-Tac antibody (HAT) has been shown to bind the p55 chain of the human IL-2R with an affinity close to that of the murine anti-Tac. Although the HAT molecule contains all six mouse CDR, it was not known which, and to what extent, each of the CDR contributes to Ag binding. These questions were addressed by constructing a series of variant HAT antibodies, each substituting a single HAT CDR with a heterologous CDR. The association constants of the variant HAT antibodies to p55 were determined by competitive binding analysis. We find that CDR 1 and 3 of the H chain and CDR 3 of the L chain are essential for maintaining binding. The remaining three CDR appear to be involved to a lesser degree.
基因工程“人源化”抗 Tac 抗体（HAT）已被证明能以接近鼠抗 Tac 的亲和力与人白细胞介素 -2 受体（IL -2R）的 p55 链结合。尽管 HAT 分子包含所有六个小鼠互补决定区（CDR），但尚不清楚每个 CDR 对抗原结合的贡献程度以及具体是哪些 CDR 起作用。通过构建一系列变体 HAT 抗体来解决这些问题，每个变体 HAT 抗体用一个异源 CDR 替换单个 HAT CDR。通过竞争性结合分析确定变体 HAT 抗体与 p55 的结合常数。我们发现重链的 CDR1 和 CDR3 以及轻链的 CDR3 对于维持结合至关重要。其余三个 CDR 的参与程度似乎较小。
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