ANTIGENICITY AND NATIVE STRUCTURE OF GLOBULAR-PROTEINS - LOW-FREQUENCY OF PEPTIDE REACTIVE ANTIBODIES
ANTIGENICITY AND NATIVE STRUCTURE OF GLOBULAR-PROTEINS - LOW-FREQUENCY OF PEPTIDE REACTIVE ANTIBODIES
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DOI：
10.1073/pnas.84.24.9180
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发表时间：
1987-12-01
影响因子：
11.1
通讯作者：
JEMMERSON, R
中科院分区：
文献类型：
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作者：
JEMMERSON, R
最近的报道称肽经常模仿球状蛋白上的表位，这与早期研究表明天然球状蛋白的抗体通常不结合肽的研究不一致。这种差异可能是由于目前抗血清中两种不同抗体群体的混淆造成的：一种与肽和变性蛋白质反应，另一种仅与天然蛋白质反应。为了测试这种可能性，通过 ELISA 检查了数百种针对大鼠细胞色素 c 的单克隆抗体与完整蛋白质和溴化氰切割肽的结合情况。可溶性天然细胞色素 c 的抑制作用确定了哪些抗体对天然蛋白具有特异性。这些抗体中的绝大多数不与肽结合，而大多数对变性抗体具有特异性的抗体却与肽结合。结果与这样的观点一致，即在固相测定中很容易检测到变性抗原的抗体，其中一些抗原分子在附着到微量滴定板上时变性，并表明这些抗体通常是与肽反应的抗体。因此，有必要重新评估表明抗天然球状蛋白抗体结合肽的数据。
Recent reports that peptides can frequently mimic epitopes on globular proteins are inconsistent with early studies demonstrating that antibodies to native globular proteins generally do not bind peptides. This discrepancy could result from current confusion of two different populations of antibodies in antisera: one reacting with peptides and denatured protein and the other reacting only with the native protein. To test this possibility, several hundred monoclonal antobodies to rat cytochrome c were examined by ELISA for binding the intact protein and cyanogen bromide-cleaved peptides. Inhibition by soluble native cytochrome c identified which antibodies were specific for the native protein. The vast majority of these antibodies did not bind the peptides, whereas most of the antibodies specific for denatured froms did bind them. The results are consistent with the idea that antibodies to denatured antigen are readily detected in solid-phase assays, where some antigen molecules denature as they attach to microtiter plates, and show that these antibodies are generally the ones that react with peptides. Thus, reevaluation of data suggesting that anti-native globular protein antibodies bind peptides is warranted.