人血管紧张素转化酶 2 与奥密克戎和德尔塔 SARS-CoV-2 刺突 RBD 的受体结合和复合物结构。
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2.
机构信息
CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; School of Medicine, Zhongda Hospital, Southeast University, NanJing 210009, China.
CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
出版信息
Cell. 2022 Feb 17;185(4):630-640.e10. doi: 10.1016/j.cell.2022.01.001. Epub 2022 Jan 6.
The coronavirus disease 2019 (COVID-19) pandemic continues worldwide with many variants arising, some of which are variants of concern (VOCs). A recent VOC, omicron (B.1.1.529), which obtains a large number of mutations in the receptor-binding domain (RBD) of the spike protein, has risen to intense scientific and public attention. Here, we studied the binding properties between the human receptor ACE2 (hACE2) and the VOC RBDs and resolved the crystal and cryoelectron microscopy structures of the omicron RBD-hACE2 complex as well as the crystal structure of the delta RBD-hACE2 complex. We found that, unlike alpha, beta, and gamma, omicron RBD binds to hACE2 at a similar affinity to that of the prototype RBD, which might be due to compensation of multiple mutations for both immune escape and transmissibility. The complex structures of omicron RBD-hACE2 and delta RBD-hACE2 reveal the structural basis of how RBD-specific mutations bind to hACE2.
新型冠状病毒病 2019（COVID-19）大流行在世界范围内继续，出现了许多变体，其中一些是令人关注的变体（VOC）。最近的一个 VOC，奥密克戎（B.1.1.529），在 Spike 蛋白的受体结合域（RBD）中获得了大量突变，引起了科学界和公众的强烈关注。在这里，我们研究了人类受体 ACE2（hACE2）和 VOC RBD 之间的结合特性，并解析了奥密克戎 RBD-hACE2 复合物的晶体和 cryo-EM 结构以及 delta RBD-hACE2 复合物的晶体结构。我们发现，与 alpha、beta 和 gamma 不同，奥密克戎 RBD 与 hACE2 的结合亲和力与原型 RBD 相似，这可能是由于多个突变同时发生，既能免疫逃逸又能提高传染性。奥密克戎 RBD-hACE2 和 delta RBD-hACE2 的复合物结构揭示了 RBD 特异性突变与 hACE2 结合的结构基础。
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