蛋白质亚基的可转换构象:揭示二十面体病毒的组装动力学

Siyu Li, Guillaume Tresset, Roya Zandi
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引用次数: 0

摘要

在许多单链 RNA 病毒的生命周期中,将遗传物质包装在一个称为囊壳的蛋白质外壳中是一个关键步骤。了解数百甚至数千个蛋白质如何围绕基因组组装形成高度对称的结构仍然是一个未解之谜。在本文中,我们设计了新的亚基并建立了一个模型,使我们能够探索二十面体病毒的组装途径和基因组包装机制,这在以前是无法实现的。通过分子动力学(MD)模拟,我们观察到蛋白数量和形态各异的囊膜片段在基因组的不同位置组装。起初,这些片段形成一个无序结构,随后合并形成一个完全对称的噬菌体。该模型在解决围绕病毒组装的众多悬而未决的问题方面显示出非凡的优势。例如,它使我们能够探索噬菌体蛋白包装 RNA 相对于线性聚合物的优势。我们的 MD 模拟与小角 X 射线散射和冷冻透射电子显微镜的实验结果非常吻合,仔细分析了具有不同拓扑结构的 RNA 周围病毒噬菌体蛋白的组装产物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Switchable Conformation in Protein Subunits: Unveiling Assembly Dynamics of Icosahedral Viruses
The packaging of genetic material within a protein shell, called the capsid, marks a pivotal step in the life cycle of numerous single-stranded RNA viruses. Understanding how hundreds, or even thousands, of proteins assemble around the genome to form highly symmetrical structures remains an unresolved puzzle. In this paper, we design novel subunits and develop a model that enables us to explore the assembly pathways and genome packaging mechanism of icosahedral viruses, which were previously inaccessible. Using molecular dynamics (MD) simulations, we observe capsid fragments, varying in protein number and morphology, assembling at different locations along the genome. Initially, these fragments create a disordered structure that later merges to form a perfect symmetric capsid. The model demonstrates remarkable strength in addressing numerous unresolved issues surrounding virus assembly. For instance, it enables us to explore the advantages of RNA packaging by capsid proteins over linear polymers. Our MD simulations are in excellent agreement with our experimental findings from small-angle X-ray scattering and cryo-transmission electron microscopy, carefully analyzing the assembly products of viral capsid proteins around RNAs with distinct topologies.
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