Stannard L M, Hardie D R
Department of Medical Microbiology, University of Cape Town Medical School, Observatory, South Africa.
J Virol. 1991 Jun;65(6):3411-5. doi: 10.1128/JVI.65.6.3411-3415.1991.
Immunogold electron microscopy has demonstrated that human immunoglobulin G (IgG) can bind to the tegument of human cytomegalovirus virions by the Fc portion of the molecule. This binding was inhibited by preincubation of the Fc probes with protein A. Treatment of AD169 virions with Triton X-100 allowed release of the Fc-binding proteins, which were precipitated and characterized by polyacrylamide gel electrophoresis (PAGE). Polypeptides of approximately 69 and 33 kDa were recovered and shown by immunoblotting to retain their capacity to bind Fc-gold after separation under both reducing and nonreducing conditions. The combined results of blocking experiments, PAGE of precipitates, and Western blots (immunoblots) indicate that the tegument proteins which bind IgG-Fc are identical to those which bind beta 2 microglobulin.
免疫金电子显微镜技术已证实，人免疫球蛋白G（IgG）可通过分子的Fc部分与人巨细胞病毒病毒粒子的包膜结合。Fc探针与蛋白A预孵育可抑制这种结合。用 Triton X-100处理AD169病毒粒子可释放出Fc结合蛋白，这些蛋白经沉淀后通过聚丙烯酰胺凝胶电泳（PAGE）进行鉴定。回收了约69 kDa和33 kDa的多肽，免疫印迹显示在还原和非还原条件下分离后，它们仍保留结合Fc金的能力。阻断实验、沉淀物的PAGE以及Western印迹（免疫印迹）的综合结果表明，结合IgG-Fc的包膜蛋白与结合β2微球蛋白的包膜蛋白相同。
