Department of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Graduate School of Biomedicine, Medical Faculty, University of Ljubljana, Vrazov trg 2, 1000 Ljubljana, Slovenia.
Sci Adv. 2019 Jul 17;5(7):eaaw3808. doi: 10.1126/sciadv.aaw3808. eCollection 2019 Jul.
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.
马铃薯 Y 病毒 (PVY) 是最重要的植物病原体之一。我们利用冷冻电镜技术确定了 PVY 弯曲病毒的近原子结构，揭示了衣壳蛋白单元羧基末端延伸区域与病毒 RNA 之间以前未知的内腔相互作用。RNA-衣壳蛋白相互作用对于病毒的螺旋构象和稳定性至关重要，这从无 RNA 的病毒样颗粒的独特近原子结构中得到了揭示。这些结构为衣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。通过突变分析和体内实验，我们证明了它们在 PVY 感染力中的关键作用，并解释了衣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有潜力成为纳米生物技术应用的新型分子支架。
