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阿尔法B.1.1.7SARS-CoV-2S蛋白与Fab中和抗体REGN1098787复合体中的结构和动态

Milita V Kocharovskaya¹, Evgeny B Pichkur², Artem D Ivannikov¹

¹Department of Structural Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia; Moscow Center for Advanced Studies, 123592, Moscow, Russia.

Biochemical and biophysical research communications

|March 5, 2025

概括

这项研究揭示了中和抗体 (nAbs) 如何与SARS-CoV-2 Alpha变种尖端蛋白结合. REGN10987抗体结合了受体结合域,阻断了ACE-2相互作用并抑制了病毒的进入.

科学领域:

结构生物学结构生物学
病毒学病毒学
免疫学免疫学免疫学

背景情况:

中和抗体 (nAbs) 对于COVID-19治疗至关重要.
了解nAb对SARS-CoV-2变种的识别有助于药物和疫苗的开发.

研究的目的:

确定与REGN10987 nAb Fab片段复合的SARS-CoV-2阿尔法变异尖端蛋白的冷电子显微镜结构.
阐明 REGN10987 与尖端蛋白的结合机制,并与其他变体进行比较.

主要方法:

低温电子显微镜 (cryo-EM) 在3.1 Å分辨率.
将抗体-RBD相互作用接口改进为3.6 Å分辨率.

主要成果:

该结构显示了两个"上升"状态的受体结合域 (RBD) 和一个"下降"状态的受体结合域,与Delta变种复合体不同.
该REGN10987 Fab与"上"和"下"形状的RBD相同地结合.
抗体结合了受体结合动机 (RBM),阻止了ACE-2结合.
在RBM中的α和delta变异突变不会改变RBD-Fab相互作用模式.

结论:

该REGN10987 nAb通过与RBM结合,有效地中和SARS-CoV-2 Alpha变种.
在抗体结合时,α和delta变体之间的尖端蛋白开放的结构差异可能是由于protomer间接口的突变.
保存的结合模式表明REGN10987对多种SARS-CoV-2变体的潜在疗效.

关键词:

中和抗体的抗体.在RBD中,RBD是RBD.这是一种S-蛋白质.这就是SARS-CoV-2病毒.低温电磁波冷却器 (Cryo-EM) 是一个非常好的方法.

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