Moravec T, Cerovská N, Pavlícek A
Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Acta Virol. 1998 Nov;42(5):341-5.
Six monoclonal antibodies (MoAbs) against potato virus A (PVA) were prepared and used in enzyme-linked immunosorbent assay (ELISA), immunoblot analysis and electron microscopic study of the virus. Four MoAbs, 151, 290, 328 and 634, reacted with purified virus preparation in dot blot test and showed strong reaction also with virus coat protein (CP) denatured by sodium dodecyl sulphate (SDS), while two MoAbs, 534 and 187, gave significantly weaker reaction with denatured CP than with purified virus. On electron micrographs, MoAb 534 effected binding only on few separate locations of the virus surface after prolonged storage. We presume that this MoAb recognized a conformation-dependent epitope.
制备了六种抗马铃薯A病毒(PVA)的单克隆抗体(MoAbs),并将其用于该病毒的酶联免疫吸附测定(ELISA)、免疫印迹分析和电子显微镜研究。四种单克隆抗体151、290、328和634在斑点印迹试验中与纯化的病毒制剂发生反应,并且与经十二烷基硫酸钠(SDS)变性的病毒衣壳蛋白(CP)也表现出强烈反应,而两种单克隆抗体534和187与变性CP的反应明显弱于与纯化病毒的反应。在电子显微镜照片上,单克隆抗体534在长时间保存后仅在病毒表面的少数几个分散位置产生结合。我们推测这种单克隆抗体识别的是一种构象依赖性表位。