Your browser does not fully support modern features. Please upgrade for a smoother experience.
Submitted Successfully!
Thank you for your contribution! You can also upload a video entry or images related to this topic. For video creation, please contact our Academic Video Service.
Version Summary Created by Modification Content Size Created at Operation
1 Luigi De Masi + 5577 word(s) 5577 2022-01-10 02:33:56 |
2 corrected the format Dean Liu -5 word(s) 5572 2022-01-12 01:43:43 | |
3 Remove the content except Introduction and Description. Dean Liu -3514 word(s) 2058 2022-04-13 11:44:49 |

Video Upload Options

We provide professional Academic Video Service to translate complex research into visually appealing presentations. Would you like to try it?
No, upload directly Yes
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
De Masi, L.; Facchiano, A. Molecular Aspects of Spike–ACE2 Interaction. Encyclopedia. Available online: https://encyclopedia.pub/entry/17945 (accessed on 11 September 2026).
De Masi L, Facchiano A. Molecular Aspects of Spike–ACE2 Interaction. Encyclopedia. Available at: https://encyclopedia.pub/entry/17945. Accessed September 11, 2026.
De Masi, Luigi, Angelo Facchiano. "Molecular Aspects of Spike–ACE2 Interaction" Encyclopedia, https://encyclopedia.pub/entry/17945 (accessed September 11, 2026).
De Masi, L., & Facchiano, A. (2022, January 10). Molecular Aspects of Spike–ACE2 Interaction. In Encyclopedia. https://encyclopedia.pub/entry/17945
De Masi, Luigi and Angelo Facchiano. "Molecular Aspects of Spike–ACE2 Interaction." Encyclopedia. Web. 10 January, 2022.
Peer Reviewed
Molecular Aspects of Spike–ACE2 Interaction
This is a peer-reviewed entry published in Encyclopedia Journal, full entry can be found at 10.3390/encyclopedia2010007

A new betacoronavirus (CoV-2) is responsible for the pandemic of severe acute respiratory syndrome (SARS) that began in China at the end of 2019, today known as COronaVIrus Disease 2019 (COVID-19). Subsequent studies confirmed the human angiotensin-converting enzyme 2 (hACE2) as the main cell receptor of spike trimeric glycoprotein, located on the viral envelope, mediating the CoV-2 invasion into the host cells through the receptor-binding domain (RBD) of the spike. Computational analysis of the known experimental 3D structures of spike–ACE2 complexes evidenced distinguishing features in the molecular interactions at the RBD-cell receptor binding interface between CoV-2 and previous CoV-1. The spike represents a key target for drug design as well as an optimal antigen for RNA/viral vector vaccines and monoclonal antibodies in order to maximize prevention and therapy of COVID-19.

COVID-19 SARS coronavirus CoV-1 CoV-2 viral spike protein receptor-binding domain (RBD) human ACE2 binding interface

References

  1. She, J.; Jiang, J.; Ye, L.; Hu, L.; Bai, C.; Song, Y. 2019 novel coronavirus of pneumonia in Wuhan, China: Emerging attack and management strategies. Clin. Transl. Med. 2020, 9, 19.
  2. Wu, F.; Zhao, S.; Yu, B.; Chen, Y.M.; Wang, W.; Song, Z.G.; Hu, Y.; Tao, Z.W.; Tian, J.H.; Zhang, Y.Z.; et al. A new coronavirus associated with human respiratory disease in China. Nature 2020, 579, 265–269.
  3. Zhu, N.; Zhang, D.; Wang, W.; Li, X.; Yang, B.; Song, J.; Zhao, X.; Huang, B.; Shi, W.; Lu, R.; et al. A Novel Coronavirus from Patients with Pneumonia in China, 2019. N. Engl. J. Med. 2020, 382, 727–733.
  4. International Committee on Taxonomy of Viruses (ICTV). Available online: https://talk.ictvonline.org (accessed on 22 July 2021).
  5. Chan, J.F.-W.; Kok, K.H.; Zhu, Z.; Chu, H.; To, K.K.-W.; Yuan, S.; Yuen, K.-Y. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerg. Microbes Infect. 2020, 9, 221–236.
  6. He, J.; Tao, H.; Yan, Y.; Huang, S.Y.; Xiao, Y. Molecular Mechanism of Evolution and Human Infection with SARS-CoV-2. Viruses 2020, 12, 428.
  7. Xu, X.; Chen, P.; Wang, J.; Feng, J.; Zhou, H.; Li, X.; Zhong, W.; Hao, P. Evolution of the novel coronavirus from the ongoing Wuhan outbreak and modeling of its spike protein for risk of human transmission. Sci. China Life Sci. 2020, 63, 457–460.
  8. Zhong, N.S.; Zheng, B.J.; Li, Y.M.; Poon, L.L.M.; Xie, Z.H.; Chan, K.H.; Li, P.H.; Tan, S.Y.; Chang, Q.; Xie, J.P.; et al. Epidemiology and cause of severe acute respiratory syndrome (SARS) in Guangdong, People’s Republic of China, in February, 2003. Lancet 2003, 362, 1353–1358.
  9. Li, W.; Zhang, C.; Sui, J.; Kuhn, J.H.; Moore, M.J.; Luo, S.; Wong, S.K.; Huang, I.C.; Xu, K.; Vasilieva, N.; et al. Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. EMBO J. 2005, 24, 1634–1643.
  10. Rabi, F.A.; Al Zoubi, M.S.; Kasasbeh, G.A.; Salameh, D.M.; Al-Nasser, A.D. SARS-CoV-2 and Coronavirus Disease 2019: What We Know So Far. Pathogens 2020, 9, 231.
  11. Facchiano, A.; Facchiano, F.; Facchiano, A. An investigation into the molecular basis of cancer comorbidities in coronavirus infection. FEBS Open Bio 2020, 10, 2363–2374.
  12. Hatmal, M.M.; Alshaer, W.; Al-Hatamleh, M.A.I.; Hatmal, M.; Smadi, O.; Taha, M.O.; Oweida, A.J.; Boer, J.C.; Mohamud, R.; Plebanski, M. Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and Their Interactions with ACE2. Cells 2020, 9, 2638.
  13. Hoffmann, M.; Kleine-Weber, H.; Schroeder, S.; Krüger, N.; Herrler, T.; Erichsen, S.; Schiergens, T.S.; Herrler, G.; Wu, N.H.; Nitsche, A.; et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell 2020, 181, 271–280.
  14. Li, W.; Moore, M.J.; Vasilieva, N.; Sui, J.; Wong, S.K.; Berne, M.A.; Somasundaran, M.; Sullivan, J.L.; Luzuriaga, K.; Greenough, T.C.; et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 2003, 426, 450–454.
  15. Li, F.; Li, W.; Farzan, M.; Harrison, S.C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 2005, 309, 1864–1868.
  16. 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. 2018, 14, e1007236.
  17. Othman, H.; Bouslama, Z.; Brandenburg, J.T.; da Rocha, J.; Hamdi, Y.; Ghedira, K.; Srairi-Abid, N.; Hazelhurst, S. Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS-CoV, hot-spot analysis and effect of the receptor polymorphism. Biochem. Biophys. Res. Commun. 2020, 527, 702–708.
  18. Wan, Y.; Shang, J.; Graham, R.; Baric, R.S.; Li, F. Receptor Recognition by the Novel Coronavirus from Wuhan: An Analysis Based on Decade-Long Structural Studies of SARS Coronavirus. J. Virol. 2020, 94, e00127-20.
  19. Wang, Q.; Zhang, Y.; Wu, L.; Niu, S.; Song, C.; Zhang, Z.; Lu, G.; Qiao, C.; Hu, Y.; Yuen, K.Y.; et al. Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2. Cell 2020, 181, 894–904.
  20. Wrapp, D.; Wang, N.; Corbett, K.S.; Goldsmith, J.A.; Hsieh, C.-L.; Abiona, O.; Graham, B.S.; McLellan, J.S. Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation. Science 2020, 367, 1260–1263.
  21. Yan, R.; Zhang, Y.; Li, Y.; Xia, L.; Guo, Y.; Zhou, Q. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science 2020, 367, 1444–1448.
  22. Kirchdoerfer, R.N.; Wang, N.; Pallesen, J.; Wrapp, D.; Turner, H.L.; Cottrell, C.A.; Corbett, K.S.; Graham, B.S.; McLellan, J.S.; Ward, A.B. Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis. Sci. Rep. 2018, 8, 15701.
  23. Lan, J.; Ge, J.; Yu, J.; Shan, S.; Zhou, H.; Fan, S.; Zhang, Q.; Shi, X.; Wang, Q.; Zhang, L.; et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 2020, 581, 215–220.
  24. Fang, L.; Karakiulakis, G.; Roth, M. Are patients with hypertension and diabetes mellitus at increased risk for COVID-19 infection? Lancet Respir. Med. 2020, 8, e21.
  25. Xu, J.; Zhao, S.; Teng, T.; Abdalla, A.E.; Zhu, W.; Xie, L.; Wang, Y.; Guo, X. Systematic Comparison of Two Animal-to-Human Transmitted Human Coronaviruses: SARS-CoV-2 and SARS-CoV. Viruses 2020, 12, 244.
  26. Ahmed, S.F.; Quadeer, A.A.; McKay, M.R. Preliminary Identification of Potential Vaccine Targets for the COVID-19 Coronavirus (SARS-CoV-2) Based on SARS-CoV Immunological Studies. Viruses 2020, 12, 254.
  27. Graham, R.L.; Baric, R.S. Recombination, reservoirs, and the modular spike: Mechanisms of coronavirus cross-species transmission. J. Virol. 2010, 84, 3134–3146.
  28. Shirato, K.; Kawase, M.; Matsuyama, S. Wild-type human coronaviruses prefer cell-surface TMPRSS2 to endosomal cathepsins for cell entry. Virology 2018, 517, 9–15.
  29. Cantuti-Castelvetri, L.; Ojha, R.; Pedro, L.D.; Djannatian, M.; Franz, J.; Kuivanen, S.; van der Meer, F.; Kallio, K.; Kaya, T.; Anastasina, M.; et al. Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity. Science 2020, 370, 856–860.
  30. Daly, J.L.; Simonetti, B.; Klein, K.; Chen, K.E.; Williamson, M.K.; Antón-Plágaro, C.; Shoemark, D.K.; Simón-Gracia, L.; Bauer, M.; Hollandi, R.; et al. Neuropilin-1 is a host factor for SARS-CoV-2 infection. Science 2020, 370, 861–865.
  31. Mayi, B.S.; Leibowitz, J.A.; Woods, A.T.; Ammon, K.A.; Liu, A.E.; Raja, A. The role of Neuropilin-1 in COVID-19. PLoS Pathog. 2021, 17, e1009153.
  32. Raj, V.S.; Mou, H.; Smits, S.L.; Dekkers, D.H.; Müller, M.A.; Dijkman, R.; Muth, D.; Demmers, J.A.A.; Zaki, A.; Fouchier, R.A.M.; et al. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 2013, 495, 251–254.
  33. Zumla, A.; Chan, J.; Azhar, E.I.; Hui, D.S.; Yuen, K.Y. Coronaviruses—Drug discovery and therapeutic options. Nat. Rev. Drug Discov. 2016, 15, 327–347.
  34. Li, H.; Tang, N.L.; Chan, P.K.; Wang, C.Y.; Hui, D.S.; Luk, C.; Kwok, R.; Huang, W.; Sung, J.J.-Y.; Kong, Q.-P.; et al. Polymorphisms in the C-type lectin genes cluster in chromosome 19 and predisposition to severe acute respiratory syndrome coronavirus (SARS-CoV) infection. J. Med. Genet. 2008, 45, 752–758.
  35. Sun, X.L. The Role of Cell Surface Sialic Acids for SARS-CoV-2 Infection. Glycobiology 2021, 31, 1245–1253.
  36. Protein Data Bank (PDB). Available online: https://www.rcsb.org (accessed on 22 July 2021).
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license; additional terms may apply. By using this site, you agree to the Terms and Conditions and Privacy Policy.
Upload a video for this entry
Information
Subjects: Cell Biology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register : Luigi De Masi , Angelo Facchiano
View Times: 3.8K
Reprint: Encyclopedia of COVID-19
Online Date: 10 Jan 2022
Table of Contents
    Notice
    You are not a member of the advisory board for this topic. If you want to update advisory board member profile, please contact office@encyclopedia.pub.
    OK
    Confirm
    Only members of the Encyclopedia advisory board for this topic are allowed to note entries. Would you like to become an advisory board member of the Encyclopedia?
    Yes
    No
    ${ textCharacter }/${ maxCharacter }
    Submit
    Cancel
    There is no comment~
    ${ textCharacter }/${ maxCharacter }
    Submit
    Cancel
    ${ selectedItem.replyTextCharacter }/${ selectedItem.replyMaxCharacter }
    Submit
    Cancel
    Confirm
    Are you sure to Delete?
    Yes No
    Academic Video Service
    Feedback