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Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus
Open accessAbstract
The recent emergence of Wuhan coronavirus (2019-nCoV) puts the world on alert. 2019-nCoV is reminiscent of the SARS-CoV outbreak in 2002 to 2003. Our decade-long structural studies on the receptor recognition by SARS-CoV have identified key interactions between SARS-CoV spike protein and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of SARS-CoV. One of the goals of SARS-CoV research was to build an atomic-level iterative framework of virus-receptor interactions to facilitate epidemic surveillance, predict species-specific receptor usage, and identify potential animal hosts and animal models of viruses. Based on the sequence of 2019-nCoV spike protein, we apply this predictive framework to provide novel insights into the receptor usage and likely host range of 2019-nCoV. This study provides a robust test of this reiterative framework, providing the basic, translational, and public health research communities with predictive insights that may help study and battle this novel 2019-nCoV.
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“RBD contains a core structure and a variable receptor-binding motif (RBM; 437–508 a.a.) which interacts and attaches with the host cell ACE-2 receptor (Fig. 2) [7].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [7]
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“RBD contains a core structure and a variable receptor-binding motif (RBM; 437–508 a.a.) which interacts and attaches with the host cell ACE-2 receptor (Fig. 2) [7].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [7]
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Neutralizing monoclonal antibodies for treatment of COVID-19
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“A number of naturally selected mutations in the RBM have been shown to affect infectivity, human-to-human transmission, pathogenesis and immune escape [2].”
BackgroundOrigin, transmission, diagnosis and management of coronavirus disease 2019 (COVID-19)
Umakanthan, S., Sahu, P. K., Ranade, A. V., Bukelo, M. M., Rao, J. S., Abrahão‐Machado, L. F., Dahal, S., Kumar, H. D. V., & Kv, D. (2020) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2020-138234 · Cited by 791
Seah, I. Y. J., & Agrawal, R. V. (2020) · Ocular Immunology and Inflammation · doi:10.1080/09273948.2020.1738501 · Cited by 698
SARS-CoV-2 Omicron virus causes attenuated disease in mice and hamsters
Halfmann, P., Iida, S., Iwatsuki‐Horimoto, K., Maemura, T., Kiso, M., Scheaffer, S. M., Darling, T. L., Joshi, A., Loeber, S. J., Singh, G., et al. (2022) · Nature · doi:10.1038/s41586-022-04441-6 · Cited by 664
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The epidemiology and clinical information about COVID-19
Ge, H., Wang, X., Yuan, X., Xiao, G., Wang, C., Deng, T., Yuan, Q., & Xiao, X. (2020) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-020-03874-z · Cited by 701
Deng, Y., Liu, W., Liu, K., Fang, Y.-Y., Shang, J., Zhou, L., Wang, K., Leng, F., Wei, S., Chen, L., et al. (2020) · Chinese Medical Journal · doi:10.1097/cm9.0000000000000824 · Cited by 657
Self-citationNeurological manifestations of COVID-19 and other coronavirus infections: A systematic review
Montalván, V., Lee, J., Bueso, T., Toledo, J. D., & Rivas, K. M. R. (2020) · Clinical Neurology and Neurosurgery · doi:10.1016/j.clineuro.2020.105921 · Cited by 670
“The increased expression of ACE2 in the epithelial cells in the lower respiratory tract facilitates viral entry by fusion with the cell membrane [12,13].”
COVID-19: A promising cure for the global panic
Vellingiri, B., Jayaramayya, K., Iyer, M., Narayanasamy, A., Govindasamy, V., Giridharan, B., Ganesan, S., Venugopal, A., Venkatesan, D., Ganesan, H., et al. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.138277 · Cited by 650
“The distinguishing factor is probably the nucleotide changes in the spike (S) protein and its receptor-binding domain (RBD) (Kannan et al., 2020; Coutard et al., 2020;Wan et al., 2020).”
BackgroundEngineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2
Chan, K. K., Dorosky, D. E., Sharma, P. A., Abbasi, S. A., Dye, J. M., Kranz, D. M., Herbert, A. S., & Procko, E. (2020) · Science · doi:10.1126/science.abc0870 · Cited by 623
Damas, J., Hughes, G. M., Keough, K. C., Painter, C. A., Persky, N. S., Corbo, M., Hiller, M., Koepfli, K.-P., Pfenning, A. R., Zhao, H., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010146117 · Cited by 633
“When ACE2 from species in our study were compared with results of other studies there were many consistencies, such as the low risk for rodents, but some predictions differ, such as the relatively high risk predicted by others for SARS-CoV-2 S binding in pangolin and horse (39), civet (40), Chinese rufous horseshoe ba…”
Wu, J., Liu, J., Zhao, X., Liu, C., Wang, W., Wang, D., Xu, W., Zhang, C., Yu, J., Jiang, B., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa199 · Cited by 633
The Natural History, Pathobiology, and Clinical Manifestations of SARS-CoV-2 Infections
Machhi, J., Herskovitz, J., Senan, A. M., Dutta, D., Nath, B., Oleynikov, M. D., Blomberg, W. R., Meigs, D. D., Hasan, M., Patel, M., et al. (2020) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-020-09944-5 · Cited by 642
“The virus was quickly identified as a coronavirus sharing genomic homology with SARS-CoV-1 (Lu et al. 2020a; Wan et al. 2020).”
BackgroundThe signal pathways and treatment of cytokine storm in COVID-19
Yang, L., Xie, X., Tu, Z., Fu, J., Xu, D., & Zhou, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00679-0 · Cited by 618
Immunity, endothelial injury and complement-induced coagulopathy in COVID-19
Perico, L., Benigni, A., Casiraghi, F., Ng, L. F. P., Rénia, L., & Remuzzi, G. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-00357-4 · Cited by 616
Ashour, H. M., Elkhatib, W. F., Rahman, M. M., & Elshabrawy, H. A. (2020) · Pathogens · doi:10.3390/pathogens9030186 · Cited by 619
Catanzaro, M., Fagiani, F., Racchi, M., Corsini, E., Govoni, S. M., & Lanni, C. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0191-1 · Cited by 618
“Moreover, the entry of SARS-CoV-2 into human host cells has been found to rely on the same receptor as SARS-CoV: the surface angiotensin-converting enzyme 2 (ACE2), which is expressed in the type II surfactant-secreting alveolar cells of the lungs.(8,9) Consistently, despite amino acid variations at specific key resid…”
BackgroundAn Update on Current Therapeutic Drugs Treating COVID-19
Wu, R., Wang, L., Kuo, H. D., Shannar, A., Peter, R. M., Chou, P. J., Li, S. N., Hudlikar, R. R., Liu, X., Liu, Z., et al. (2020) · Current Pharmacology Reports · doi:10.1007/s40495-020-00216-7 · Cited by 600
“It is speculated that SARS-CoVand SARS-CoV-2 bind to human cells via interaction with ACE2 receptors [118, 119] .”
BackgroundDiarrhea During COVID-19 Infection: Pathogenesis, Epidemiology, Prevention, and Management
D’Amico, F., Baumgart, D. C., Danese, S., & Peyrin‐Biroulet, L. (2020) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2020.04.001 · Cited by 614
“Structural studies 17 showed that the new SARS-CoV-2 not only binds ACE2, but its binding affinity for human ACE2 is significantly stronger (10-20 times more) 18 than its 2003 SARS-CoV predecessor.”
The Effects of Type 2 Diabetes Mellitus on Organ Metabolism and the Immune System
Daryabor, G., Atashzar, M. R., Kabelitz, D., Meri, S., & Kalantar, K. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01582 · Cited by 617
Acute SARS-CoV-2 Infection Impairs Dendritic Cell and T Cell Responses
Zhou, R., To, K. K.-W., Wong, Y.-C., Liu, L., Zhou, B., Li, X., Huang, H., Mo, Y., Luk, T.-Y., Lau, T. T.-K., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.026 · Cited by 531
“…and SARS-CoV use the same cellular entry receptor angiotensinconverting enzyme 2 (ACE2) to initiate infection, despite that only 40% amino acids are identical in the receptor binding domain (RBD) external subdomain (Chan et al., 2020; Lan et al., 2020; Wan et al., 2020; Zhou et al., 2020).”
The N501Y spike substitution enhances SARS-CoV-2 infection and transmission
Liu, Y., Liu, J., Plante, K. S., Plante, J. A., Xie, X., Zhang, X., Ku, Z., An, Z., Scharton, D., Schindewolf, C., et al. (2021) · Nature · doi:10.1038/s41586-021-04245-0 · Cited by 575
Bat-borne virus diversity, spillover and emergence
Letko, M. C., Seifert, S. N., Olival, K. J., Plowright, R. K., & Munster, V. J. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0394-z · Cited by 583
mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · Science · doi:10.1126/science.abg9175 · Cited by 557
Self-citationThe laboratory tests and host immunity of COVID-19 patients with different severity of illness
Wang, F., Hou, H., Luo, Y., Tang, G., Wu, S., Huang, M., Liu, W., Zhu, Y., Lin, Q., Mao, L., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.137799 · Cited by 560
“The current studies focus on the genome sequences (1, 8), epidemiology and outbreak investigation (9, 10), detection methods (11, 12), receptor recognition (13), and drug treatment of SARS-CoV-2 (14).”
BackgroundZhou, H., Chen, X., Hu, T., Li, J., Song, H., Liu, Y., Wang, P., Liu, D., Yang, J., Holmes, E. C., et al. (2020) · Current Biology · doi:10.1016/j.cub.2020.05.023 · Cited by 589
“In contrast, RaTG13 (Figure 2B), pangolin/MP789/2019 (Figure 2C), and pangolin/P5L/2017 (Figure 2D) did not have the deletions, and had similar conformations at their external domains, indicating that they may also use ACE2 as cell receptor, although with the exception of pangolin/MP789/2019 (see below), all exhibited…”
InfluentialCOVID-19: Disease, management, treatment, and social impact
Ali, I., & Alharbi, O. M. L. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.138861 · Cited by 579
“It depends on the age, health and clinical conditions of the patients (Wan et al., 2020).”
BackgroundA systematic review of SARS-CoV-2 vaccine candidates
Dong, Y., Dai, T., Wei, Y., Zhang, L., Zheng, M., & Zhou, F. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00352-y · Cited by 555
Severe Acute Respiratory Syndrome Coronavirus 2 from Patient with Coronavirus Disease, United States
Harcourt, J. L., Tamin, A., Lu, X., Kamili, S., Sakthivel, S. K., Murray, J., Queen, K. J., Tao, Y., Paden, C. R., Zhang, J., et al. (2020) · Emerging infectious diseases · doi:10.3201/eid2606.200516 · Cited by 534
Impaired immune cell cytotoxicity in severe COVID-19 is IL-6 dependent
Mazzoni, A., Salvati, L., Maggi, L., Capone, M., Vanni, A., Spinicci, M., Mencarini, J., Caporale, R., Peruzzi, B., Antonelli, A., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138554 · Cited by 502
“ACE2 is expressed in the respiratory tract, by mucosal epithelial cells, lung alveolar type 2 pneumocytes, and arterial and venous endothelial cells but also in other tissues, including the gastrointestinal tract, accounting for the mild enteritis that sometimes is present in patients with COVID-19 (15, 16).”
BackgroundCOVID-19: The Inflammation Link and the Role of Nutrition in Potential Mitigation
Zabetakis, I., Lordan, R., Norton, C., & Τσούπρας, Α. (2020) · Nutrients · doi:10.3390/nu12051466 · Cited by 553
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The molecular virology of coronaviruses
Hartenian, E., Nandakumar, D., Lari, A., Ly, M., Tucker, J. M., & Glaunsinger, B. A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.013930 · Cited by 544
“Comparing the SARS-CoV-2 S protein sequence with that of closely related SARS-CoV–like viruses revealed that almost all the residues important for ACE2 engagement are not conserved in SARS-CoV-2 (32), although the SARS-CoV-2 S RBD has a 10–20-fold higher binding affinity to ACE2 than SARS-CoV S RBD (33).”
Pruijssers, A. J. P., George, A. S., Schäfer, A., Leist, S. R., Gralinski, L. E., Dinnon, K. H., Yount, B. L., Agostini, M. L., Stevens, L. J., Chappell, J. D., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107940 · Cited by 503
“In addition, SARS-CoV-2 does not readily infect wild-type mice because of incompatibilities between the virus spike and the murine ACE2 ortholog, which serves as the SARS-CoV-2 entry receptor (Wan et al., 2020).”
BackgroundSelf-citationA comprehensive review of COVID-19 characteristics
Esakandari, H., Nabi‐Afjadi, M., Afjadi, J. F., Farahmandian, N., Miresmaeili, S. M., & Bahreini, E. (2020) · Biological Procedures Online · doi:10.1186/s12575-020-00128-2 · Cited by 511
“cluding lung, intestine, kidney, and blood vessels [25].”
Background
Metadata
- Authors
- Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F.
- Affiliations
- University of Minnesota (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Li, Fang
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2020-03-17
- Volume
- 94
- Issue
- 7
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC7081895
- OpenAlex
- W3004348779
- Cited by
- 4,341
- References
- 38
- Citations by year
- 2026: 27 · 2025: 75 · 2024: 170 · 2023: 299 · 2022: 619 · 2021: 1273 · 2020: 1865
- FWCI
- 133.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (R01AI089728, R01AI110700)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Health Sciences › Medicine › Infectious Diseases › Viral Infections and Outbreaks Research
- Keywords
- SARS-CoV-2, SARS-CoV, spike protein, angiotensin-converting enzyme 2, receptor recognition, host range prediction, interspecies transmission, human-to-human transmission, animal models, disease surveillance
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Amino Acid Sequence, Animals, China, Chiroptera, Humans, Peptidyl-Dipeptidase A, Models, Molecular, Phylogeny, Pneumonia, Viral, Receptors, Virus, Sequence Alignment, Coronavirus Infections, Severe acute respiratory syndrome-related coronavirus, Host Specificity, Spike Glycoprotein, Coronavirus
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