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在SARS-CoV-2 BA.2.86和JN.1中尖端受体结合域移动性的结构基础
Hisano Yajima1, Yuki Anraku2, Yu Kaku3
1Laboratory of Medical Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Nature communications
|October 7, 2024
概括
研究人员观察到SARS-CoV-2的尖端蛋白质.
科学领域:
- 病毒学 病毒学
- 结构生物学 结构生物学
- 生物化学 生物化学
背景情况:
- SARS-CoV-2 突变引发了流行病浪潮.
- 尖端蛋白的受体结合域 (RBD) 与ACE2结合是细胞进入的关键.
- RBD构造 (上下) 对ACE2相互作用至关重要.
研究的目的:
- 阐明ACE2与SARS-CoV-2尖端蛋白变体相互作用的结构基础.
- 调查RBD向下构造在ACE2结合和构造变化中的作用.
- 分析BA.2.86和JN.1变种中特定突变的结构影响.
主要方法:
- 进行X射线晶体学以确定与ACE2.2结合的BA.2.86和JN.1尖端蛋白的结构.
- 分析蛋白质-连接体相互作用和形状动态.
- 突变分析以评估特定氨基酸变化的影响 (例如,K356T) 对病毒感染性和抗体逃避.
主要成果:
- 观察到ACE2与SARS-CoV-2尖端蛋白结合的新型结构,包括下方构造中的RBD.
- 确定了下行RBD-ACE2相互作用作为一个中间步骤,促进过渡到RBD上行构造.
- 证明BA.2.86中的K356T突变增强了感染力,并有助于抗体逃避,而与N354相关的甘氨酸则没有.
结论:
- ACE2可以在下降形态中与RBD相互作用,促进向RBD上升状态的转变.
- 对尖峰-ACE2动态的结构洞察力有助于理解SARS-CoV-2感染机制.
- 像K356T这样的特定突变对于SARS-CoV-2变种的传染性和免疫逃避是至关重要的.
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