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Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2.
Cell. 2022 02 17; 185(4):630-640.e10.Cell

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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Authors+Show Affiliations

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.

MeSH

Amino Acid SequenceAngiotensin-Converting Enzyme 2Cryoelectron MicroscopyHumansModels, MolecularMutationPhylogenyProtein BindingProtein DomainsReceptors, VirusSARS-CoV-2Spike Glycoprotein, CoronavirusStatic ElectricityStructural Homology, Protein

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

35093192

Citation

Han, Pengcheng, et al. "Receptor Binding and Complex Structures of Human ACE2 to Spike RBD From Omicron and Delta SARS-CoV-2." Cell, vol. 185, no. 4, 2022, pp. 630-640.e10.
Han P, Li L, Liu S, et al. Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2. Cell. 2022;185(4):630-640.e10.
Han, P., Li, L., Liu, S., Wang, Q., Zhang, D., Xu, Z., Han, P., Li, X., Peng, Q., Su, C., Huang, B., Li, D., Zhang, R., Tian, M., Fu, L., Gao, Y., Zhao, X., Liu, K., Qi, J., ... Wang, P. (2022). Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2. Cell, 185(4), 630-e10. https://doi.org/10.1016/j.cell.2022.01.001
Han P, et al. Receptor Binding and Complex Structures of Human ACE2 to Spike RBD From Omicron and Delta SARS-CoV-2. Cell. 2022 02 17;185(4):630-640.e10. PubMed PMID: 35093192.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2. AU - Han,Pengcheng, AU - Li,Linjie, AU - Liu,Sheng, AU - Wang,Qisheng, AU - Zhang,Di, AU - Xu,Zepeng, AU - Han,Pu, AU - Li,Xiaomei, AU - Peng,Qi, AU - Su,Chao, AU - Huang,Baihan, AU - Li,Dedong, AU - Zhang,Rong, AU - Tian,Mingxiong, AU - Fu,Lutang, AU - Gao,Yuanzhu, AU - Zhao,Xin, AU - Liu,Kefang, AU - Qi,Jianxun, AU - Gao,George F, AU - Wang,Peiyi, Y1 - 2022/01/06/ PY - 2021/12/17/received PY - 2021/12/26/revised PY - 2021/12/31/accepted PY - 2022/1/31/pubmed PY - 2022/3/3/medline PY - 2022/1/30/entrez KW - RBD KW - VOCs KW - delta KW - hACE2 KW - omicron KW - receptor-binding domain KW - structure KW - variants of concern SP - 630 EP - 640.e10 JF - Cell JO - Cell VL - 185 IS - 4 N2 - 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. SN - 1097-4172 UR - https://www.unboundmedicine.com/medline/citation/35093192/Receptor_binding_and_complex_structures_of_human_ACE2_to_spike_RBD_from_omicron_and_delta_SARS_CoV_2_ DB - PRIME DP - Unbound Medicine ER -