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Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2.
Han, Pengcheng; Li, Linjie; Liu, Sheng; Wang, Qisheng; Zhang, Di; Xu, Zepeng; Han, Pu; Li, Xiaomei; Peng, Qi; Su, Chao; Huang, Baihan; Li, Dedong; Zhang, Rong; Tian, Mingxiong; Fu, Lutang; Gao, Yuanzhu; Zhao, Xin; Liu, Kefang; Qi, Jianxun; Gao, George F; Wang, Peiyi.
  • Han P; 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.
  • Li L; 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.
  • Liu S; Cryo-EM Center, Department of Biology, Southern University of Science and Technology, Shenzhen 518055, China.
  • Wang Q; Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201204, China.
  • Zhang D; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Faculty of Health Sciences, University of Macau, Macau 999078, China.
  • Xu Z; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Faculty of Health Sciences, University of Macau, Macau 999078, China.
  • Han P; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Li X; Cryo-EM Center, Shanxi Academy of Advanced Research and Innovation, Taiyuan 030032, China.
  • Peng Q; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Su C; Department of Biomedical Sciences, City University of Hong Kong, Hong Kong 999077, China.
  • Huang B; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Li D; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Zhang R; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Tian M; College of life Science, Shanxi University, Taiyuan 03006, China.
  • Fu L; Cryo-EM Center, Department of Biology, Southern University of Science and Technology, Shenzhen 518055, China.
  • Gao Y; Cryo-EM Center, Department of Biology, Southern University of Science and Technology, Shenzhen 518055, China.
  • Zhao X; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Liu K; CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
  • Qi J; 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. Electronic address: jxqi@im.ac.cn.
  • Gao GF; 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. Electronic address: gaof@im.ac.cn.
  • Wang P; Cryo-EM Center, Department of Biology, Southern University of Science and Technology, Shenzhen 518055, China. Electronic address: wangpy@sustech.edu.cn.
Cell ; 185(4): 630-640.e10, 2022 02 17.
Article in English | MEDLINE | ID: covidwho-1611650
ABSTRACT
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Receptors, Virus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 Type of study: Randomized controlled trials Topics: Variants Limits: Humans Language: English Journal: Cell Year: 2022 Document Type: Article Affiliation country: J.cell.2022.01.001

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Receptors, Virus / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 Type of study: Randomized controlled trials Topics: Variants Limits: Humans Language: English Journal: Cell Year: 2022 Document Type: Article Affiliation country: J.cell.2022.01.001