Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

Nature

Volumn 581, Issue 7807, 2020, Pages 215-220

  Lan, Jun ^a   Ge, Jiwan ^a   Yu, Jinfang ^a   Shan, Sisi ^b   Zhou, Huan ^c   Fan, Shilong ^a   Zhang, Qi ^b   Shi, Xuanling ^b   Wang, Qisheng ^c   Zhang, Linqi ^b   Wang, Xinquan ^a  

^a TSINGHUA UNIVERSITY   (China)

^b Tsinghua University   (China)

^c SHANGHAI ADVANCED RESEARCH INSTITUTE   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN CONVERTING ENZYME 2; ANGIOTENSIN CONVERTING ENZYME 2 RECEPTOR; CELL RECEPTOR; CORONAVIRUS SPIKE GLYCOPROTEIN; EPITOPE; UNCLASSIFIED DRUG; VIRUS ANTIBODY; DIPEPTIDYL CARBOXYPEPTIDASE; INORGANIC SALT; NEUTRALIZING ANTIBODY; PROTEIN BINDING; SPIKE PROTEIN, SARS-COV-2; VIRUS RECEPTOR; WATER;

ANTIBODY; CHEMICAL BINDING; CONVERGENT EVOLUTION; ULTRASTRUCTURE; VIRUS;

ARTICLE; CROSS REACTION; CRYSTAL STRUCTURE; HUMAN; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; RECEPTOR BINDING; SARS CORONAVIRUS; SARS-RELATED CORONAVIRUS; SEQUENCE HOMOLOGY; SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS 2; STRUCTURAL HOMOLOGY; VIRUS ENTRY; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; BETACORONAVIRUS; BINDING SITE; CHEMISTRY; COMPARATIVE STUDY; CONSERVED SEQUENCE; IMMUNOLOGY; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR MODEL; SEQUENCE ALIGNMENT;

CHINA; HUBEI; WUHAN;

CORONAVIRUS; SARS CORONAVIRUS;

AMINO ACID SEQUENCE; ANTIBODIES, NEUTRALIZING; BETACORONAVIRUS; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; EPITOPES; EVOLUTION, MOLECULAR; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; PEPTIDYL-DIPEPTIDASE A; PROTEIN BINDING; PROTEIN DOMAINS; RECEPTORS, VIRUS; SALTS; SARS VIRUS; SEQUENCE ALIGNMENT; SPIKE GLYCOPROTEIN, CORONAVIRUS; WATER;

EID: 85083295918     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/s41586-020-2180-5     Document Type: Article

References (29)

1. Zhou, P. et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 579, 270–273 (2020).
2. Wu, F. et al. A new coronavirus associated with human respiratory disease in China. Nature 579, 265–269 (2020).
3. Zhu, N. et al. A novel coronavirus from patients with pneumonia in China, 2019. N. Engl. J. Med. 382, 727–733 (2020).
4. Li, F., Li, W., Farzan, M. & Harrison, S. C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 309, 1864–1868 (2005).
5. Lu, R. et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet 395, 565–574 (2020).
6. Huang, C. et al. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. Lancet 395, 497–506 (2020).
7. Liu, K. et al. Clinical characteristics of novel coronavirus cases in tertiary hospitals in Hubei Province. Chin. Med. J. (Engl.) 10.1097/CM9.0000000000000744 (2020).
8. Wang, D. et al. Clinical characteristics of 138 hospitalized patients with 2019 novel coronavirus-infected pneumonia in Wuhan, China. J. Am. Med. Assoc. 323, 1061–1069 (2020).
9. Gui, M. et al. Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. Cell Res. 27, 119–129 (2017).
10. Song, W., Gui, M., Wang, X. & Xiang, Y. Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. PLoS Pathog. 14, e1007236 (2018).
11. Kirchdoerfer, R. N. et al. Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis. Sci. Rep. 8, 15701 (2018).
12. Yuan, Y. et al. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. Nat. Commun. 8, 15092 (2017).
13. Walls, A. C. et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 10.1016/j.cell.2020.02.058 (2020).
14. Letko, M., Marzi, A. & Munster, V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat. Microbiol. 5, 562–569 (2020).
15. Hoffmann, M. et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 10.1016/j.cell.2020.02.052 (2020).
16. Tian, X. et al. Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody. Emerg. Microbes Infect. 9, 382–385 (2020).
17. Wrapp, D. et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science 367, 1260–1263 (2020).
18. Wan, Y., Shang, J., Graham, R., Baric, R. S. & Li, F. Receptor recognition by novel coronavirus from Wuhan: an analysis based on decade-long structural studies of SARS. J. Virol. 94, e00127-20 (2020).
19. Li, W. et al. Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. EMBO J. 24, 1634–1643 (2005).
20. Prabakaran, P. et al. Structure of severe acute respiratory syndrome coronavirus receptor-binding domain complexed with neutralizing antibody. J. Biol. Chem. 281, 15829–15836 (2006).
21. Hwang, W. C. et al. Structural basis of neutralization by a human anti-severe acute respiratory syndrome spike protein antibody, 80R. J. Biol. Chem. 281, 34610–34616 (2006).
22. Walls, A. C. et al. Unexpected receptor functional mimicry elucidates activation of coronavirus fusion. Cell 176, 1026–1039 (2019).
23. van den Brink, E. N. et al. Molecular and biological characterization of human monoclonal antibodies binding to the spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus. J. Virol. 79, 1635–1644 (2005).
24. Yu, F. et al. Aquarium: an automatic data-processing and experiment information management system for biological macromolecular crystallography beamlines. J. Appl. Crystallogr. 52, 472–477 (2019).
25. McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007).
26. Cohen, S. X. et al. ARP/wARP and molecular replacement: the next generation. Acta Crystallogr. D 64, 49–60 (2008).
27. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004).
28. Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948–1954 (2002).
29. Janson, G., Zhang, C., Prado, M. G. & Paiardini, A. PyMod 2.0: improvements in protein sequence-structure analysis and homology modeling within PyMOL. Bioinformatics 33, 444–446 (2017).