Matthes T, Wolff A, Soubiran P, Gros F, Dighiero G
Unité d'Immunohématologie, Institut Pasteur, Paris, France.
J Immunol. 1988 Nov 1;141(9):3135-41.
Natural and induced antitubulin antibodies were compared for their epitope recognition on alpha- and beta-tubulin subunits by immunoenzymatic assays and Western blot techniques on partially digested tubulin molecules. Our results indicated that natural autoantibodies recognized different epitopes from those recognized by induced antibodies, because: 1) all polyspecific natural autoantibodies tested so far recognized the same or very overlapping epitopes in the central part of both alpha- and beta-subunits (between positions 100 and 300 on the tubulin amino acid sequence) and that this epitope differed from the various epitopes recognized by induced antitubulin antibodies on the amino-terminal or carboxy-terminal parts of the tubulin subunits; 2) one human myeloma protein (monoclonal (m)IgA, kappa) with a monospecific antitubulin activity bound to an epitope around position 310 on both alpha- and beta-subunits and a second human mIg (mIgM, kappa) with a monospecific anti-beta activity bound to an epitope on the carboxy-terminal part of the subunit around amino acid position 350. Both epitopes differed from epitopes recognized by induced antitubulin antibodies. These results thus confirmed our previous findings indicating that natural and induced antitubulin antibodies do not share cross-reactive idiotopes.
通过免疫酶测定法和对部分消化的微管蛋白分子进行蛋白质印迹技术，比较了天然和诱导产生的抗微管蛋白抗体在α-和β-微管蛋白亚基上的表位识别情况。我们的结果表明，天然自身抗体识别的表位与诱导抗体识别的表位不同，原因如下：1）到目前为止测试的所有多特异性天然自身抗体在α-和β-亚基的中央部分（微管蛋白氨基酸序列上第100至300位之间）识别相同或非常重叠的表位，并且该表位与诱导抗微管蛋白抗体在微管蛋白亚基的氨基末端或羧基末端部分识别的各种表位不同；2）一种具有单特异性抗微管蛋白活性的人骨髓瘤蛋白（单克隆（m）IgA，κ）与α-和β-亚基上第310位左右的一个表位结合，另一种具有单特异性抗β活性的人mIg（mIgM，κ）与亚基羧基末端部分氨基酸位置350左右的一个表位结合。这两个表位都与诱导抗微管蛋白抗体识别的表位不同。因此，这些结果证实了我们之前的发现，即天然和诱导产生的抗微管蛋白抗体不共享交叉反应性独特型。
