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针对爱泼斯坦-巴尔核抗原的免疫反应:抗体与合成肽结合的构象和结构特征。

The immune response to Epstein-Barr nuclear antigen: conformational and structural features of antibody binding to synthetic peptides.

作者信息

Rhodes G, Houghten R, Taulane J P, Carson D, Vaughan J

出版信息

Mol Immunol. 1984 Nov;21(11):1047-54. doi: 10.1016/0161-5890(84)90114-7.

Abstract

Naturally developing human antibodies to the Epstein-Barr nuclear antigen recognize synthetic peptides containing sequences from the unusual glycine-alanine region of this protein. We tested antibody binding to a series of peptides of from five to 20 amino acids in length. Peptides as small as seven amino acids could bind but optimal results required chain lengths of 15. Binding was extremely sensitive to small changes in the length and sequence of the peptide, and also to the temp of the reaction. The changes can be ascribed to two factors: (1) deletion of the site of antigen binding and (2) loss of peptide secondary structure.

摘要

针对EB病毒核抗原的天然产生的人类抗体可识别含有该蛋白异常甘氨酸-丙氨酸区域序列的合成肽。我们测试了抗体与一系列长度为5至20个氨基酸的肽的结合情况。短至7个氨基酸的肽就能结合,但最佳结果需要15个氨基酸的链长。结合对肽的长度和序列的微小变化以及反应温度极为敏感。这些变化可归因于两个因素:(1)抗原结合位点的缺失和(2)肽二级结构的丧失。

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