Cox J H, Dietzschold B, Schneider L G
Infect Immun. 1977 Jun;16(3):754-9. doi: 10.1128/iai.16.3.754-759.1977.
Purified rabies virus glycoprotein (G) was shown by complement fixation and immunodiffusion tests to be a second distinct antigen of the virus. It it the only structural protein of the virus that induces the formation of virus-neutralizing antibodies and which confers immunity to animals. When the G protein is taken as antigen, the complement fixation test can be used for the assay of virus-neutralizing antibodies. The total protective activity of the virus was recovered in the purified G protein preparation. The protective activity of G protein increased with purification: 9 ng of G protein was required to protect 50% of the mice as compared to 1.63 micrograms of the virus. Selective immunofluorescent membrane staining and immunocytolysis of rabies virus-infected cells were shown to be G protein specific. Due to its purity and potency, the G protein preparation can be considered the ideal human antirabies vaccine.
通过补体结合试验和免疫扩散试验表明，纯化的狂犬病病毒糖蛋白（G）是该病毒的第二种独特抗原。它是病毒唯一能诱导产生病毒中和抗体并赋予动物免疫力的结构蛋白。当以G蛋白作为抗原时，补体结合试验可用于检测病毒中和抗体。纯化的G蛋白制剂恢复了病毒的全部保护活性。G蛋白的保护活性随着纯化而增加：保护50%的小鼠需要9纳克G蛋白，而相比之下，病毒则需要1.63微克。狂犬病病毒感染细胞的选择性免疫荧光膜染色和免疫细胞溶解被证明具有G蛋白特异性。由于其纯度和效力，G蛋白制剂可被视为理想的人用狂犬病疫苗。
