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S373P突变稳定了Omicron中尖端蛋白的受体结合域,并促进了结合

Bin Zheng¹, Yuelong Xiao¹, Bei Tong²

¹State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu 210023, China.

|July 28, 2023

概括

新的Omicron突变增强了尖端蛋白的稳定性. 这种增加的机械稳定性和对人类ACE2受体的更强的结合可能会影响SARS-CoV-2传播动态.

科学领域:

病毒学病毒学
生物物理学的生物物理.
结构生物学结构生物学

背景情况:

SARS-CoV-2 尖端蛋白的受体结合域 (RBD) 对于病毒进入至关重要.
在RBD的突变可以改变病毒结合亲和力和稳定性.
呼吸道的动态机械环境可能会影响病毒与宿主之间的相互作用.

研究的目的:

为了研究Omicron变种RBD的机械稳定性.
了解机械稳定性观察到的任何变化的结构基础.
评估Omicron突变对RBD和ACE2之间的解离力的影响.

主要方法:

基于原子力显微镜的单分子力光谱 (AFM-SMFS) 来测量RBD的机械稳定性.
分子动力学 (MD) 模拟用于分析RBD中的结构变化和键.
将Omicron RBD与野生型SARS-CoV-2 RBD进行比较.

主要成果:

与野生类型相比,Omicron RBD的机械稳定性大约提高了20%.
分子动力学模拟显示,与S373P突变相关的Omicron的β核心区域中增加了结.
对于与ACE2相互作用的Omicron RBD观察到更高的展开和解离力.

结论:

S373P突变有助于奥米克朗RBD的机械稳定.
奥米克朗RBD的机械稳定性增加可能会影响病毒结合和传播.
RBD的β核心区域可能是SARS-CoV-2适应的不断变化的目标.

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