Brígido M de M, Sabbaga J, Brentani R R
Ludwig Institute for Cancer Research, São Paulo Branch, Brazil.
Immunol Lett. 1990 Jun;24(3):191-7. doi: 10.1016/0165-2478(90)90047-t.
Present-day methods for the definition of antibody binding sites on antigenic polypeptides show a strong bias toward identification of sequential epitopes. We have employed anti-sequence monoclonal antibodies raised against short synthetic peptides to screen a random-primed cDNA library constructed in an expression vector. Sequence data analysis performed on three clones thus isolated showed that the clones did not cross-hybridize and that the antigenic peptide sequence was found in none of them. Our findings suggest therefore that sequential epitopes may be preferentially identified because of an inherent bias in commonly used epitope mapping protocols which masks available conformational determinants.
目前用于定义抗原多肽上抗体结合位点的方法，在识别连续表位方面存在强烈偏向性。我们利用针对短合成肽产生的抗序列单克隆抗体，筛选在表达载体中构建的随机引物cDNA文库。对由此分离出的三个克隆进行的序列数据分析表明，这些克隆没有交叉杂交，并且在其中任何一个克隆中都未发现抗原肽序列。因此，我们的研究结果表明，由于常用表位作图方案中存在固有偏向性，掩盖了可用的构象决定簇，连续表位可能被优先识别。
