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硫化物稳定揭示了SARS-CoV-1和SARS-CoV-2尖峰之间保存的动态特征

Xixi Zhang¹, Zimu Li¹, Yanjun Zhang²

¹State Key Laboratory of Respiratory Disease, CAS Key Laboratory of Regenerative Biology, Guangdong Provincial Key Laboratory of Stem Cell and Regenerative Medicine, Guangdong Provincial Key Laboratory of Biocomputing, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, China.

Life science alliance

|July 4, 2023

概括

研究人员使用二硫化键稳定了SARS-CoV-1尖端蛋白 (S) 的罕见,锁定形状. 这种结构稳定允许详细的成像和分析以前未被描述的S蛋白状态.

科学领域:

结构生物学是结构生物学.
病毒学病毒学
低温电子显微镜的使用方法

背景情况:

在SARS-CoV-1的尖端蛋白 (S) 呈现出动态的结构变化.
预流形状包括锁定,关闭和开放状态,而锁定状态是暂时的,对SARS-CoV-1的特征不佳.

研究的目的:

为了表征SARS-CoV-1 S蛋白的罕见,锁定前注射形状.
研究二硫化物键在稳定这些形状中的作用.

主要方法:

在SARS-CoV-1 S蛋白中引入特定的二硫化物键 (x1,x2,x3).
电子显微镜 (cryo-EM) 用于图像稳定形状.
与其他与SARS相关的冠状病毒尖峰结构进行比较分析.

主要成果:

成功稳定和成像SARS-CoV-1 S.的各种锁定和罕见形状.
识别了与锁定SARS-CoV-1 S形状相关的绑定辅因子和结构特征.
与其他与SARS相关的CoV尖峰结构的详细比较揭示了保存的特征.

结论:

二硫化物键可以稳定SARS-CoV-1 S蛋白的短暂,锁定形状.
这项研究为SARS-CoV-1 S动态和SARS相关的CoVs中保存的特征提供了新的结构洞察力.

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