Hajeer A H, Worthington J, Morgan K, Bernstein R M
Department of Rheumatology, University of Manchester Medical School, UK.
Clin Exp Immunol. 1992 Jul;89(1):115-9. doi: 10.1111/j.1365-2249.1992.tb06888.x.
The binding sites for MoAbs to the 65-kD heat-shock protein (hsp65) of mycobacteria have been investigated by epitope scanning. Five hundred and twenty-six 8-mer peptides representing the complete sequence of Mycobacterium tuberculosis hsp65 were synthesised in duplicate using the Epitope Scanning Kit (CRB Ltd.). The epitopes of six MoAbs raised to the hsp65 of M. tuberculosis or M. leprae were investigated. We have identified the epitope of a new MoAb (DC16); this epitope is continuous, hydrophilic in nature and 11 amino acids long. We have also confirmed the location of the epitopes of three MoAbs (IIH9, ML30 and IIC8). Thus the epitope scanning technique has proved suitable for the detection of continuous epitopes of hsp65.
通过表位扫描研究了单克隆抗体（MoAbs）与分枝杆菌65-kD热休克蛋白（hsp65）的结合位点。使用表位扫描试剂盒（CRB有限公司）一式两份合成了代表结核分枝杆菌hsp65完整序列的526个8聚体肽。研究了针对结核分枝杆菌或麻风分枝杆菌hsp65产生的六种单克隆抗体的表位。我们确定了一种新的单克隆抗体（DC16）的表位；该表位是连续的，本质上是亲水性的，长度为11个氨基酸。我们还证实了三种单克隆抗体（IIH9、ML30和IIC8）表位的位置。因此，表位扫描技术已被证明适用于检测hsp65的连续表位。
