Goodman-Snitkoff G, Mannino R J, McSharry J J
J Exp Med. 1981 Jun 1;153(6):1489-502. doi: 10.1084/jem.153.6.1489.
The glycoprotein (G protein) of VSV was purified from the intact virion by Triton X-100 extraction. The isolated G protein has been shown to be a T cell-independent, B lymphocyte mitogen and polyclonal activator. Neither G protein nor the intact virion are stimulatory for murine T lymphocytes. The greater the density of G protein in lipid vesicles or the degree of aggregation of isolated G protein, the more highly stimulatory it is for murine splenocytes. As G protein is spread out in artificial vesicles, it becomes less mitogenic. It is probable that other viral components are also stimulatory since the Triton-insoluble pellet and VSV from which the G protein has been enzymatically removed retain mitogenic activity. To out knowledge, this is the first time a purified viral component has been demonstrated to be lymphocyte mitogen.
水泡性口炎病毒（VSV）的糖蛋白（G蛋白）通过Triton X-100抽提从完整病毒粒子中纯化出来。已证明分离出的G蛋白是一种不依赖T细胞的B淋巴细胞有丝分裂原和多克隆激活剂。G蛋白和完整病毒粒子对小鼠T淋巴细胞均无刺激作用。脂质囊泡中G蛋白的密度越高或分离出的G蛋白的聚集程度越高，其对小鼠脾细胞的刺激作用就越强。当G蛋白分散在人工囊泡中时，其促有丝分裂作用就会减弱。由于已通过酶法去除G蛋白的Triton不溶性沉淀和VSV仍保留有丝分裂活性，所以很可能其他病毒成分也具有刺激作用。据我们所知，这是首次证明一种纯化的病毒成分是淋巴细胞有丝分裂原。
