Ellis S A, Taylor C, McMichael A
Hum Immunol. 1982 Aug;5(1):49-59. doi: 10.1016/0198-8859(82)90030-1.
A monoclonal antibody that binds specifically to HLA-B27, B7, and B22 is described. Binding to B27 appeared to be slightly stronger than to B7 and stronger than to B22 in an indirect binding assay, but no difference in B7 and B27 binding could be detected by Scatchard analysis. No distinction could be made between B27 on cells from normal and from ankylosing spondylitis patients in any assay system. The antibody, which was not cytotoxic, blocked complement-dependent cytolysis mediated by human HLA typing sera specific for B7 and B27. Competitive binding studies with other monoclonal antibodies showed that ME1 could block the binding of antibodies that recognized different antigenic sites on HLA. ME1 did not bind to Klebsiella pneumoniae. This reagent will be useful in further analysis of the relationship between B27 and ankylosing spondylitis.
本文描述了一种能特异性结合HLA - B27、B7和B22的单克隆抗体。在间接结合试验中，该抗体与B27的结合似乎略强于与B7的结合，且强于与B22的结合，但通过Scatchard分析未检测到B7和B27结合存在差异。在任何检测系统中，均无法区分正常人和强直性脊柱炎患者细胞上的B27。该抗体无细胞毒性，可阻断由针对B7和B27的人HLA分型血清介导的补体依赖性细胞溶解。与其他单克隆抗体的竞争性结合研究表明，ME1可阻断识别HLA上不同抗原位点的抗体的结合。ME1不与肺炎克雷伯菌结合。该试剂将有助于进一步分析B27与强直性脊柱炎之间的关系。
