Tsai C H, Williams M V, Glaser R
Department of Medical Microbiology and Immunology, Ohio State University College of Medicine, Columbus 43210.
J Virol Methods. 1991 Jun;33(1-2):47-52. doi: 10.1016/0166-0934(91)90006-l.
Five monoclonal antibodies (mAbs) were identified using immunofluorescence that were specific for the Epstein-Barr virus (EBV) encoded 52/50 kDa early antigen (EA-D) protein complex. Evidence to suggest that these mAbs react with the same 52/50 kDa EA-D protein was obtained by Western blotting, immunoprecipitation and ELISA. Two of the mAbs, 90E2 and 214A9, neutralized EBV DNA polymerase activity. The 214A9 mAb also inhibited the activity of bacteriophage T4 DNA polymerase while the 90E2 mAb did not. These data suggest that the 90E2 and 214A9 mAbs recognize two different epitopes on the 52/50 kDa EA-D protein. The high frequency of recovery of hybridomas producing anti 52/50 kDa EA-D mAbs suggest that this protein may have an important role in EBV pathogenesis/replication.
利用免疫荧光法鉴定出五种单克隆抗体（mAb），它们对爱泼斯坦-巴尔病毒（EBV）编码的52/50 kDa早期抗原（EA-D）蛋白复合物具有特异性。通过蛋白质免疫印迹法、免疫沉淀法和酶联免疫吸附测定法获得的证据表明，这些单克隆抗体与相同的52/50 kDa EA-D蛋白发生反应。其中两种单克隆抗体90E2和214A9可中和EBV DNA聚合酶活性。214A9单克隆抗体还可抑制噬菌体T4 DNA聚合酶的活性，而90E2单克隆抗体则不能。这些数据表明，90E2和214A9单克隆抗体识别52/50 kDa EA-D蛋白上的两个不同表位。产生抗52/50 kDa EA-D单克隆抗体的杂交瘤的高回收率表明，该蛋白可能在EBV发病机制/复制中起重要作用。
