Onodera S, Ohori H, Yamaki M, Ishida N
J Med Virol. 1982;10(2):147-55. doi: 10.1002/jmv.1890100209.
The ultrastructure of the nucleocapsid component of human hepatitis B virus (core particle) was studied by negative staining-carbon film technique. Using this method an improved image of core particles was obtained in respect of resolution and contrast. Two-dimensional crystalline arrays of core particles were formed in vitro. Under these arrays the distance between the particle centers was 28.3 nm, corresponding to the capsid diameter, when analyzed through optical diffraction patterns. Positively stained images of these arrays revealed that core particles contain an electron-dense center of nucleoid-like area about 21 nm in diameter. The capsid surface rarely exhibited small capsomeres, ie, small spheres or ring-like structures measuring 4.0-4.2 nm. From the dimension of these structures and the analysis by Markham's rotational technique, it was suggested that each of these capsomeres is an individual subunit (monomer) and 180 of these subunits build up the core particle capsid according to the icosahedral symmetry (T = 3), but not clustering into distinct morphological features.
采用负染色-碳膜技术研究了人类乙型肝炎病毒核衣壳成分(核心颗粒)的超微结构。运用该方法,在分辨率和对比度方面获得了核心颗粒的改进图像。核心颗粒在体外形成二维晶体阵列。通过光学衍射图样分析,这些阵列中颗粒中心之间的距离为28.3nm,与衣壳直径相对应。这些阵列的阳性染色图像显示,核心颗粒含有一个直径约21nm的类似核仁区域的电子致密中心。衣壳表面很少出现小的壳粒,即直径为4.0 - 4.2nm的小球体或环状结构。根据这些结构的尺寸以及马尔卡姆旋转技术的分析,提示这些壳粒中的每一个都是单个亚基(单体),并且180个这样的亚基根据二十面体对称性(T = 3)构建核心颗粒衣壳,而非聚集成明显的形态特征。