McKeating J A, Griffiths P D, Grundy J E
J Gen Virol. 1987 Mar;68 ( Pt 3):785-92. doi: 10.1099/0022-1317-68-3-785.
We have previously reported that human cytomegalovirus (CMV) from urine specimens cannot be captured onto a solid phase by CMV-specific monoclonal antibodies that can capture CMV grown in vitro. We report here that CMV exists in vivo in body fluids such as urine as beta 2 microglobulin (beta 2 m)-coated particles. We have demonstrated the presence of beta 2m on CMV purified directly from urine by Western blotting and have shown that the beta 2m was associated with the viral envelope. Urinary CMV could be specifically bound by an affinity column comprising a monoclonal antibody specific for beta 2m bound to Sepharose. The beta 2m-coated urinary CMV could not be neutralized by hyperimmune globulin, human immune sera or murine monoclonal antibodies that could neutralize CMV grown in cell culture. We conclude that the binding of beta 2m by CMV masks the important antigenic sites necessary for neutralization which are recognized by man's immune response. We propose that CMV has evolved this mechanism of coating itself in a host protein as a mechanism of evading the host immune response and facilitating transmission between individuals.
我们之前曾报道,尿液标本中的人巨细胞病毒(CMV)无法被能捕获体外培养的CMV的CMV特异性单克隆抗体捕获到固相上。我们在此报告,CMV以β2微球蛋白(β2m)包被的颗粒形式存在于尿液等体液的体内。我们通过蛋白质印迹法证明了直接从尿液中纯化的CMV上存在β2m,并表明β2m与病毒包膜相关。尿液中的CMV可被包含与琼脂糖结合的针对β2m的单克隆抗体的亲和柱特异性结合。β2m包被的尿液CMV不能被能中和细胞培养中生长的CMV的高效价免疫球蛋白、人免疫血清或鼠单克隆抗体中和。我们得出结论,CMV与β2m的结合掩盖了中和所需的重要抗原位点,而这些位点是人类免疫反应所识别的。我们提出,CMV进化出这种用宿主蛋白包被自身的机制,作为逃避宿主免疫反应和促进个体间传播的一种机制。