Characterization of poliovirus conformational alteration mediated by soluble cell receptors.
Characterization of poliovirus conformational alteration mediated by soluble cell receptors.
复制标题
可溶性细胞受体介导的脊髓灰质炎病毒构象改变的表征。
DOI：
10.1006/viro.1993.1621
复制
发表时间：
1993
期刊：
影响因子：
3.7
通讯作者：
Hogle,JM
中科院分区：
文献类型：
--
作者：
GómezYafal,A;Kaplan,G;Racaniello,VR;Hogle,JM
表达脊髓灰质炎病毒受体（PVR）的草地贪夜蛾细胞的可溶性提取物诱导天然脊髓灰质炎病毒（PV）到“A”颗粒构象变化（J.Virol.64，4697-4702）。我们描述了调节这一通道的变量，并研究了增溶PVR的适用性，既可用作anin vitrosystem来表征受体介导的构象改变，又可用于生产大量的改变病毒进行结构分析。PVR似乎以化学计量方式起作用，并且通过电子显微镜观察，产生的A颗粒显示为完整的、染色排除的球形结构，而不管衣壳蛋白VP 1的广泛蛋白水解，其在转化期间发生。所获得的产品，时间过程，以及温度和离子强度依赖性的PV的变化由增溶的PVR是无法区分的改变，导致生产性感染培养的细胞。因此，溶解的PVR可以为进一步表征细胞进入过程提供便利的体外系统。
Soluble extracts ofSpodoptera frugiperdacells expressing the poliovirus receptor (PVR) induce the native poliovirus (PV) to "A" particle conformational change (J. Virol.64, 4697-4702). We describe the variables that regulate this passage and study the suitability of solubilized PVR both for use as anin vitrosystem to characterize the receptor-mediated conformational alteration and for the production of large amounts of altered virus for structural analysis. PVR seems to function in a stoichiometric fashion and the A particles produced appear as intact, stain excluding, spherical structures by electron microscopy, regardless of the extensive proteolysis of the capsid protein VP 1, which takes place during the conversion. The products obtained, time course, and temperature and ionic strength dependence of the alteration of PV by the solubilized PVR are indistinguishable from those of the alteration that leads to productive infection in cultured cells. Therefore, solubilized PVR may provide a convenientin vitrosystem for further characterization of the cell entry process.