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Structural basis for the multitasking nature of the potato virus Y coat protein

机译:马铃薯病毒Y外壳蛋白多任务性质的结构基础

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摘要

Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY’s flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA–coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein’s amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.
机译:马铃薯病毒Y(PVY)是最经济重要的植物病原体之一。使用冷冻电子显微镜,我们确定了PVY弯曲病毒体的近原子结构,揭示了外壳蛋白单元的扩展羧基末端区域与病毒RNA之间先前未知的腔相互作用。 RNA外壳蛋白的相互作用对于病毒体的螺旋构型和稳定性至关重要,正如无RNA的病毒样颗粒独特的近原子结构所揭示的那样。这些结构为外壳蛋白的氨基和羧基末端区域的可塑性提供了第一个证据。连同突变分析和植物实验,我们展示了它们在PVY感染性中的关键作用,并解释了外壳蛋白执行多种生物学任务的能力。此外,PVY病毒样颗粒的高度模块化表明它们作为纳米生物技术应用的新型分子支架的潜力。

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