Mukhopadhyay Suchetana, Chipman Paul R, Hong Eunmee M, Kuhn Richard J, Rossmann Michael G
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA.
J Virol. 2002 Nov;76(21):11128-32. doi: 10.1128/jvi.76.21.11128-11132.2002.
In vitro-assembled core-like particles produced from alphavirus capsid protein and nucleic acid were studied by cryoelectron microscopy. These particles were found to have a diameter of 420 A with 240 copies of the capsid protein arranged in a T=4 icosahedral surface lattice, similar to the nucleocapsid core in mature virions. However, when the particles were subjected to gentle purification procedures, they were damaged, preventing generation of reliable structural information. Similarly, purified nucleocapsid cores isolated from virus-infected cells or from mature virus particles were also of poor quality. This suggested that in the absence of membrane and glycoproteins, nucleocapsid core particles are fragile, lacking accurate icosahedral symmetry.
利用冷冻电子显微镜对由甲病毒衣壳蛋白和核酸体外组装而成的核心样颗粒进行了研究。发现这些颗粒直径为420埃,有240个衣壳蛋白拷贝排列成T = 4二十面体表面晶格,类似于成熟病毒粒子中的核衣壳核心。然而,当对这些颗粒进行温和的纯化程序时,它们受到了损伤,从而无法生成可靠的结构信息。同样,从病毒感染细胞或成熟病毒粒子中分离出的纯化核衣壳核心质量也很差。这表明在没有膜和糖蛋白的情况下,核衣壳核心颗粒很脆弱,缺乏精确的二十面体对称性。