RABIES VIRUS GLYCOPROTEIN .2. BIOLOGICAL AND SEROLOGICAL CHARACTERIZATION
RABIES VIRUS GLYCOPROTEIN .2. BIOLOGICAL AND SEROLOGICAL CHARACTERIZATION
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DOI：
10.1128/iai.16.3.754-759.1977
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发表时间：
1977-01-01
影响因子：
3.1
通讯作者：
SCHNEIDER, LG
中科院分区：
文献类型：
--
作者：
COX, JH;DIETZSCHOLD, B;SCHNEIDER, LG
纯化的狂犬病毒糖蛋白(G)经补体固定和免疫扩散试验证实是该病毒的第二种不同抗原。它是该病毒唯一的结构蛋白，能诱导病毒中和抗体的形成，并赋予动物免疫力。当以G蛋白为抗原时，补体固定试验可用于病毒中和抗体的测定。在纯化的G蛋白制备中恢复了病毒的总保护活性。G蛋白的保护活性随着纯化而增强；9 ng G蛋白可以保护50%的小鼠，而1.63 μ G蛋白则可以保护50%的小鼠。病毒的G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是G蛋白特异性的。由于其纯度和效力，G蛋白制剂可以被认为是理想的人抗狂犬病疫苗。
Purified rabies virus glycoprotein (G) was shown by complement fixation and immunodiffusion tests to be a 2nd distinct antigen of the virus. It is 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 .mu.g of the virus. Selective immunofluorescent membrane staining and immunocytolysis of rabies virus-infected cells were G protein specific. Due to its purity and potency, the G protein preparation can be considered the ideal human antirabies vaccine.