Dietzschold B, Wiktor T J, Wunner W H, Varrichio A
Virology. 1983 Jan 30;124(2):330-7. doi: 10.1016/0042-6822(83)90349-5.
Soluble glycoprotein (Gs), purified from virion-depleted, rabies-infected tissue culture fluid, was chemically and immunologically analyzed. A comparison of this antigen with the virion-associated glycoprotein showed that Gs lacks 58 amino acid residues from the carboxy terminus of the virion-associated glycoprotein. Analysis with monoclonal antibodies revealed that all the epitopes of the viral glycoprotein are also present in the soluble glycoprotein. However, when tested for its ability to protect mice against a lethal challenge infection with rabies virus, Gs in contrast to viral glycoprotein, showed no protective activity. These results suggest that the carboxy terminus of the rabies virus glycoprotein is necessary for its full protective activity even though this portion of the glycoprotein molecule does not contain any antigenic determinants.
从去除病毒粒子的狂犬病感染组织培养液中纯化得到的可溶性糖蛋白(Gs),进行了化学和免疫学分析。将该抗原与病毒粒子相关糖蛋白进行比较,结果显示Gs在病毒粒子相关糖蛋白的羧基末端缺少58个氨基酸残基。用单克隆抗体分析表明,病毒糖蛋白的所有表位也存在于可溶性糖蛋白中。然而,当检测其保护小鼠免受狂犬病病毒致死性攻击感染的能力时,与病毒糖蛋白相比,Gs没有显示出保护活性。这些结果表明,狂犬病病毒糖蛋白的羧基末端对于其完全保护活性是必需的,尽管糖蛋白分子的这一部分不包含任何抗原决定簇。