Alexander H, Johnson D A, Rosen J, Jerabek L, Green N, Weissman I L, Lerner R A
Nature. 1983;306(5944):697-9. doi: 10.1038/306697a0.
Recent studies have shown that short chemically synthesized peptides very often induce antibodies which react with the cognate sequence in the intact folded protein. Since such antibodies react with known regions of proteins, they are of predetermined specificity and offer a precision not previously possible with immunological probes. A basic concept emerging from the use of such antibodies in viral systems is that the differential immunogenicity of closely related proteins can be mimicked by short peptides which span the regions of sequence variation. To generalize this concept, we have studied the two Thy-1 proteins which vary by only a single amino acid. Chemically synthesized peptides differing in only one out of 19 amino acids were able to induce allospecific antisera. Thus, single amino acid changes have similar effects on the immunogenicity of proteins and small peptides, even though the latter are free from constraints provided by neighbouring structures in the tertiary configuration of the intact folded proteins.
最近的研究表明,短的化学合成肽常常能诱导产生与完整折叠蛋白中的同源序列发生反应的抗体。由于这类抗体与蛋白质的已知区域发生反应,它们具有预先确定的特异性,并提供了以前免疫探针所无法达到的精确性。在病毒系统中使用这类抗体所产生的一个基本概念是,密切相关蛋白质的差异免疫原性可以被跨越序列变异区域的短肽所模拟。为了推广这一概念,我们研究了仅相差一个氨基酸的两种Thy-1蛋白。仅19个氨基酸中有一个不同的化学合成肽能够诱导产生同种特异性抗血清。因此,单个氨基酸的变化对蛋白质和小肽的免疫原性具有相似的影响,尽管后者不受完整折叠蛋白三级结构中相邻结构所提供的限制。