Visualization of the externalized VP2N termini of infectious human parvovirus B19
Visualization of the externalized VP2N termini of infectious human parvovirus B19
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DOI：
10.1128/jvi.00512-08
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发表时间：
2008-08-01
影响因子：
5.4
通讯作者：
Rossmann, Michael G.
中科院分区：
文献类型：
--
作者：
Kaufmann, Baerbel;Chipman, Paul R.;Rossmann, Michael G.
假设二十面体对称，通过冷冻电子显微镜（cryoEM）分别以7.5埃和11.3埃分辨率测定感染性人细小病毒B19和空野生型颗粒的结构。这两种，DNA填充的和空的，野生型颗粒含有少量拷贝的次要衣壳蛋白VP 1。野生型B19与仅由主要衣壳蛋白VP 2组成的重组B19颗粒的晶体结构和cryoEM重建的比较显示在二十面体五重轴附近的结构差异。虽然在二十面体平均图谱中无法观察到VP 1的独特N-末端区域，但显示VP 2的N-末端暴露在邻近五倍β-圆柱体的病毒表面上。保守的富含甘氨酸的区域位于两个相邻的五倍对称相关VP亚基之间，而不是在其他细小病毒中观察到的五倍通道中。
The structures of infectious human parvovirus B19 and empty wild-type particles were determined by cryoelectron microscopy (cryoEM) to 7.5-angstrom and 11.3 angstrom resolution, respectively, assuming icosahedral symmetry. Both of these, DNA filled and empty, wild-type particles contain a few copies of the minor capsid protein VP1 Comparison of wild-type B19 with the crystal structure and cryoEM reconstruction of recombinant B19 particles consisting of only the major capsid protein VP2 showed structural differences in the vicinity of the icosahedral fivefold axes. Although the unique N-terminal region of VP1 could not be visualized in the icosahedrally averaged maps, the N terminus of VP2 was shown to be exposed on the viral surface adjacent to the fivefold beta-cylinder. The conserved glycine-rich region is positioned between two neighboring, fivefold-symmetrically related VP subunits and not in the fivefold channel as observed for other parvoviruses.