Eckels K H, Hetrick F M, Russell P K
Infect Immun. 1975 May;11(5):1053-60. doi: 10.1128/iai.11.5.1053-1060.1975.
Japanese encephalitis virions contain a 58 X 10-3-molecular-weight envelope glycoprotein antigen that can be solubilized with sodium lauryl sulfate and separated from other virion structural polypeptides and viral ribonucleic acid by gel filtration chromatography. The 58 X 10-3-molecular-weight envelope protein is the major antigen responsible for cross-reactivity of the virion in complement fixation tests with other closely related arboviruses. A naturally occurring soluble complement-fixing antigen is found in Japanese encephalitis mouse brain preparations after removal of particulate antigens. After partial purification by gel filtration and isoelectric focusing, the 53 X 10-3-molecular weight soluble complement-fixing antigen is more type specific than the Japanese encephalitis envelope antigen in complement fixation tests. Further, the Japanese encephalitis soluble complement-fixing antigen is stable to treatment with sodium lauryl sulfate and 2-mercaptoethanol, whereas virion complement-fixing antigens are unstable after this treatment.
日本脑炎病毒粒子含有一种分子量为58×10⁻³的包膜糖蛋白抗原,该抗原可用十二烷基硫酸钠溶解,并通过凝胶过滤色谱法与其他病毒粒子结构多肽和病毒核糖核酸分离。分子量为58×10⁻³的包膜蛋白是病毒粒子在补体结合试验中与其他密切相关虫媒病毒发生交叉反应的主要抗原。在去除颗粒性抗原后,日本脑炎小鼠脑制备物中发现一种天然存在的可溶性补体结合抗原。经凝胶过滤和等电聚焦部分纯化后,分子量为53×10⁻³的可溶性补体结合抗原在补体结合试验中比日本脑炎包膜抗原更具型特异性。此外,日本脑炎可溶性补体结合抗原对十二烷基硫酸钠和2-巯基乙醇处理稳定,而病毒粒子补体结合抗原经此处理后不稳定。