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首页> 美国卫生研究院文献>Journal of Virology >Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer.
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Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer.

机译：具有完整且氨基末端缺失的VP2的重组轮状病毒样颗粒的三维结构分析：对VP2衣壳层结构的影响。

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摘要

Rotaviruses are the leading cause of severe infantile gastroenteritis worldwide. These viruses are large, complex icosahedral particles consisting of three concentric capsid layers enclosing a genome of eleven segments of double-stranded RNA (dsRNA). The amino terminus of the innermost capsid protein VP2 possesses a nonspecific single-stranded RNA and dsRNA binding activity, and the amino terminus is also essential for the incorporation of the polymerase enzyme VP1 and guanylyltransferase VP3 into the core of the virion. Biochemical and structural studies have suggested that VP2, and especially the amino terminus, appears to act as a scaffold for proper assembly of the components of the viral core. To locate the amino terminus of VP2 within the core, we have used electron cryomicroscopy and image reconstruction to determine the three-dimensional structures of recombinant virus-like particles that contain either full-length or amino-terminal-deleted forms of VP2 coexpressed with the intermediate capsid protein VP6. A comparison of these structures indicates two significant changes along the inner surface of VP2 in the structure lacking the amino terminus: a loss of mass adjacent to the fivefold axes and a redistribution of mass along the fivefold axes. Examination of the VP2 layer suggests that the proteins are arranged as dimers of 120 quasi-equivalent molecules, with each dimer extending between neighboring fivefold axes. Our results indicate that the amino termini of both quasi-equivalent VP2 molecules are located near the icosahedral vertices.
机译：轮状病毒是全世界严重婴儿胃肠炎的主要原因。这些病毒是大型的复杂二十面体颗粒，由三个同心衣壳层组成，这些衣壳层包裹着双链RNA（dsRNA）的11个片段的基因组。最里面的衣壳蛋白VP2的氨基末端具有非特异性的单链RNA和dsRNA结合活性，并且氨基末端对于将聚合酶VP1和鸟苷基转移酶VP3掺入病毒体的核心也是必不可少的。生化和结构研究表明，VP2，尤其是氨基末端，似乎充当了适当组装病毒核心组分的支架。为了在核心内定位VP2的氨基末端，我们使用电子冷冻显微镜和图像重建技术来确定重组病毒样颗粒的三维结构，该颗粒包含全长或氨基末端缺失形式的VP2，与VP2共表达。中间衣壳蛋白VP6。这些结构的比较表明，在缺少氨基末端的结构中，沿VP2内表面的两个显着变化是：邻近五倍轴的质量损失和沿五倍轴的质量重新分布。 VP2层的检查表明蛋白质排列为120个准等价分子的二聚体，每个二聚体在相邻的五倍轴之间延伸。我们的结果表明，两个准当量VP2分子的氨基末端都位于二十面体顶点附近。

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