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通过冷电子断层扫描可视化的酸结合后的virion相关流感血素集群

Qiuyu J Huang, Ryan Kim, Kangkang Song

bioRxiv : the preprint server for biology

|October 28, 2024

概括

在与酸受体结合后,流感病毒的血凝素 (HA) 三分体聚集在一起. 这种使用冷电子断层扫描可视化的结构重组,揭示了病毒葡萄糖蛋白组织的新动态.

科学领域:

病毒学病毒学
结构生物学结构生物学
分子生物物理学分子生物物理学

背景情况:

流感病毒具有表面糖蛋白,主要是血素 (HA),对于宿主细胞进入至关重要.
之前的HA结构研究集中在体外分离的蛋白质上,不清楚体内病毒组织.

研究的目的:

在受体结合时对完整的病毒体上研究流感血质素 (HA) trimers的结构组织和动态.
阐明酸受体相互作用对HA在病毒表面的空间布局的影响.

主要方法:

低温电子断层扫描 (cryoET) 用于绘制与酸受体模拟器相互作用的流感病毒的图像.
使用子图平均和精细化技术,实现病毒表面糖蛋白的高分辨率 (8-10 Å) 重建.

主要成果:

受体结合并没有显著改变整体病毒形态,但诱导了HA三元体组织的重组.
未结合的HA剪切器表现出均的间距,而受体结合的剪切器显示出集群和形成不同的剪切器的剪切器安排.
在高分辨率下确定了特定的三元体间接触和调解这种聚类的分子特征.

结论:

酸受体结合会触发HA三元体在流感病毒上聚合,这表明病毒葡萄糖蛋白组织具有显著的可塑性.
这一发现揭示了先前未被描述的HA动态层,这对于病毒功能和宿主相互作用至关重要.

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