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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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“[71] demonstrated that residue 394 (glutamine) in the SARS-CoV-2 receptor-binding domain (RBD) can be recognized by critical lysine 31 on the human ACE2 receptor [72].”
BackgroundGüler, H. İ., Tatar, G., Yıldız, O., Beldüz, A. O., & Kolaylı, S. (2021) · Archives of Microbiology · doi:10.1007/s00203-021-02351-1 · Cited by 98
“Subsequent studies have shown that SARS-CoV-2 has been suggested to recognize human ACE-II more strongly than SARS-CoV, thereby increasing the ability to be transmitted from person to person (Wan et al. 2020).”
BackgroundWeston, S. M., Coleman, C. M., Haupt, R., Logue, J., Matthews, K. L., & Frieman, M. B. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.25.008482 · Cited by 96
Brandão, S. C. S., Ramos, J. D. O. X., Dompieri, L. T., Godoi, E. T. A. M., de Figueiredo, J. L., SARINHO, E. S. C., Chelvanambi, S., & Aikawa, M. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.09.002 · Cited by 93
“and the spike protein binding to the ACE2 [17], other factors may contribute to the infectivity and pathogenesis of SARS-CoV-2 that deserve further investigations [18].”
Trimpert, J., Vladimirova, D., Dietert, K., Abdelgawad, A., Kunec, D., Dökel, S., Voß, A., Gruber, A. D., Bertzbach, L. D., & Osterrieder, N. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108488 · Cited by 89
“However, we failed to identify any difference in any of the amino acids thought to be critically important for virus binding (Figure 5) (Lan et al., 2020; Shang et al., 2020; Wan et al., 2020).”
Molecular evolutionary characteristics of SARS‐CoV‐2 emerging in the United States
Wang, S., Xu, X., Wei, C., Li, S., Zhao, J., Zheng, Y., Liu, X., Zeng, X., Yuan, W., & Peng, S. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27331 · Cited by 87
Highly Conserved Homotrimer Cavity Formed by the SARS-CoV-2 Spike Glycoprotein: A Novel Binding Site
Kalathiya, U., Padariya, M., Mayordomo, M. Y., Lisowska, M. M., Nicholson, J., Singh, A. J., Bagiński, M., Fåhræus, R., Carragher, N. O., Ball, K. L., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051473 · Cited by 93
“The recognition and subsequently fusion of two membranes from the virus and the host is triggered by the S1 subunit, which binds the host cell receptor: angiotensin-converting enzyme 2 (ACE2) [16, 25-31].”
BackgroundKhan, I. H., Zahra, S. A., Zaim, S., & Harky, A. (2020) · Journal of Cardiac Surgery · doi:10.1111/jocs.14596 · Cited by 91
“SARS‐CoV‐2 can bind to the angiotensin‐converting enzyme 2 (ACE2) and enter the host cell.(11) Severe pneumonia and acute lung failure associated with SARS‐CoV‐2 is postulated to be due to suppression of ACE2 expression.”
BackgroundSk, M. F., Roy, R., Jonniya, N. A., Poddar, S., & Kar, P. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1768149 · Cited by 91
“The S protein attaches with the host receptor by the specific receptor binding domain (RBD) (Wan et al., 2020), while the N protein binds to RNA in multiple sites to make a helical nucleocapsid structure (Chang et al.”
BackgroundMaria, E. D., Latini, A., Borgiani, P., & Novelli, G. (2020) · Human Genomics · doi:10.1186/s40246-020-00280-6 · Cited by 93
“In fact, biochemical interaction studies and crystal structure analyses revealed that the SARS-CoV-2 spike protein has a strong binding affinity with the human ACE2 extracellular domain [16, 17, 69, 70], and that SARS-CoV-2 and the original SARS-CoV display a high degree of homology [16, 71, 72], demonstrating that bo…”
BackgroundThe evolutionary history of ACE2 usage within the coronavirus subgenus Sarbecovirus
Wells, H., Letko, M. C., Lasso, G., Ssebide, B., Nziza, J., Byarugaba, D. K., Navarrete‐Macias, I., Liang, E., Cranfield, M. R., Han, B. A., et al. (2021) · Virus Evolution · doi:10.1093/ve/veab007 · Cited by 97
“Notably, in addition to the large deletions, viruses that cannot use ACE2 deviate considerably at the interacting suface, including positions that play fundamental roles dictating binding and cross-species transmission (Figure 3) [30,36,39,42].”
BackgroundGrover, A., & Oberoi, M. (2020) · European Heart Journal - Cardiovascular Pharmacotherapy · doi:10.1093/ehjcvp/pvaa064 · Cited by 89
Glycyrrhizin: An old weapon against a novel coronavirus
Chrzanowski, J., Chrzanowska, A., & Graboń, W. (2020) · Phytotherapy Research · doi:10.1002/ptr.6852 · Cited by 93
“Thus, blocking ACE2 by binding to it, GZ could potentially inhibit the entry of SARS-CoV-2 into the cell (Wan et al., 2020; Zhou et al., 2020).”
BackgroundOcular Surface Expression of SARS-CoV-2 Receptors
Leonardi, A., Rosani, U., & Brun, P. (2020) · Ocular Immunology and Inflammation · doi:10.1080/09273948.2020.1772314 · Cited by 88
“Similarly, the SARS-CoV-2 encoded a ACE2-receptor-binding motif, which mediated its entry into host cells,(6,8,9) even though less efficiently than human SARS-CoV (year 2002) but more efficiently than human SARS-CoV (year 2003),(8) thus evolving its capability to infect humans.(8) SARS SP engages ACE2 as an entry rece…”
BackgroundMagnavacca, A., Sangiovanni, E., Racagni, G., & Dell’Agli, M. (2021) · Medicinal Research Reviews · doi:10.1002/med.21866 · Cited by 89
“Recent evidence showed that aTMPRSS2 inhibitor approved for clinical use could block viral entry, bringing to light an innovative treatment option.208 Kaempferol, in fact, had been previously shown able to decrease the mRNA expression of TMPRSS2.”
BackgroundThe origins of COVID‐19 pandemic: A brief overview
Hao, Y., Wang, Y., Wang, M.-Y., Zhou, L., Shi, J., Cao, J., & Wang, D. (2022) · Transboundary and Emerging Diseases · doi:10.1111/tbed.14732 · Cited by 139
“Pigs, ferrets, cats and non-human primates contain a larger number of residues that favour the interaction of SARS-CoV-2 with ACE2 and therefore serve as animal models or intermediate hosts for the SARS-CoV-2 (Wan et al., 2020).”
BackgroundInfluentialHwang, J.-M., Kim, J.-H., Park, J.-S., Chang, M. C., & Park, D. (2020) · Neurological Sciences · doi:10.1007/s10072-020-04541-z · Cited by 89
“SARS-CoV-2 binds to ACE2 in the human body [22].”
BackgroundSARS-CoV-2 host diversity: An update of natural infections and experimental evidence
Hossain, M. G., Javed, A., Akter, S., & Saha, S. (2020) · Journal of Microbiology Immunology and Infection · doi:10.1016/j.jmii.2020.06.006 · Cited by 89
“A recent study found that SARS-CoV-2 can recognize the host cells receptor ACE2 of pigs, ferrets, cats, orangutans, monkeys, and humans with similar efficiencies.(26) Several cases of SARS-CoV-2, that causes COVID19 in human; have been confirmed in animals.”
BackgroundInfluentialDiehl, J., Péron, N., Chocron, R., Debuc, B., Guérot, E., Hauw‐Berlemont, C., Hermann, B., Augy, J.-L., Younan, R., Novara, A., et al. (2020) · Annals of Intensive Care · doi:10.1186/s13613-020-00716-1 · Cited by 92
“Since the SARSCoV-2 receptor (ACE2) is strongly expressed in endothelial cells [9], infection of endothelial cells could have induced pulmonary endothelial lesions and triggered activation of coagulation, at least in some patients.”
BackgroundZheng, S., Baak, J. P. A., Li, S., Xiao, W., Ren, H. G., Yang, H., Gan, Y., & Wen, C. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153336 · Cited by 88
“SARS-CoV-2 utilizes ACE2 to bind and gain entry to the host pneumocytes (Wan et al., 2020).”
Seroprevalence of SARS-CoV-2 (COVID-19) exposure in pet cats and dogs in Minnesota, USA
Dileepan, M., Di, D., Huang, Q., Ahmed, S., Heinrich, D. A., Ly, H., & Liang, Y. (2021) · Virulence · doi:10.1080/21505594.2021.1936433 · Cited by 83
“SARS-CoV-2 RBD was expressed from mammalian cells as described previously [37] and was a kind gift of Y.”
MethodOcular manifestations of coronavirus disease 2019
Ceran, B. B., & Özateş, S. (2020) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-020-04777-7 · Cited by 87
“Genomic and structural analyses show a similar receptorbinding motive between SARS-CoV and SARS-CoV-2 with resembling pathologic features and epidemiological characteristics [8, 9].”
BackgroundNeurological consequences of COVID-19: what have we learned and where do we go from here?
Jarrahi, A., Ahluwalia, M., Khodadadi, H., Salles, É. L., Kolhe, R. B., Hess, D. C., Vale, F. Ĺ., Kumar, M., Baban, B., Vaibhav, K., et al. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01957-4 · Cited by 91
“Given the genetic similarity and conserved viral structure with SARS-CoV, it appears likely that SARSCoV-2 may also exhibit neurotropic properties [30, 31].”
BackgroundDifferential white blood cell count in the COVID-19: A cross-sectional study of 148 patients
Anurag, A., Jha, P. K., & Kumar, A. (2020) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2020.10.029 · Cited by 87
Methodology-Centered Review of Molecular Modeling, Simulation, and Prediction of SARS-CoV-2
Gao, K., Wang, R., Chen, J., Cheng, L., Frishcosy, J., Huzumi, Y., Qiu, Y., Schluckbier, T., Wei, X., & Wei, G. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00965 · Cited by 93
Dalvie, N. C., Rodriguez‐Aponte, S. A., Hartwell, B. L., Tostanoski, L. H., Biedermann, A. M., Crowell, L. E., Kaur, K., Kumru, O. S., Carter, L. P., Yu, J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106845118 · Cited by 84
Neuroinflammation and Its Impact on the Pathogenesis of COVID-19
Almutairi, M. M., Sivandzade, F., Albekairi, T. H., Alqahtani, F., & Cucullo, L. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.745789 · Cited by 92
A four-part guide to lung immunology: Invasion, inflammation, immunity, and intervention
Gopallawa, I., Dehinwal, R., Bhatia, V., Gujar, V., & Chirmule, N. B. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1119564 · Cited by 102
A child confirmed COVID-19 with only symptoms of conjunctivitis and eyelid dermatitis
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Corona Virus International Public Health Emergencies: Implications for Radiology Management
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“Receptor recognition by novel coronavirus from Wuhan: An analysis based on decade-long structural studies of SARS causing symptoms in humans similar to those caused by SARS coronavirus (SARS-CoV) (Wan et al. 2020).”
Veeramachaneni, G. K., Thunuguntla, V. B. S. C., Bobbillapati, J., & Bondili, J. S. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1773318 · Cited by 93
“CoV S-protein RBD residues 436, 473, 475, 479, 481, 482, 486, 487, 488 and 491 were previously reported as hotspots in several studies (Han et al., 2006; Wan et al., 2020).”
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“to SARS-CoV, contains different amino acids (five amino acids out of six are mutated) composition in its RBD that are crucial for receptor binding (ACE2) with high affinity [17], and has a functional polybasic furin site at S1-S2 boundary that may have a role in defining the viral infectivity and host range [18,19].”
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Point-of-Care Diagnostics of COVID-19: From Current Work to Future Perspectives
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“The particularly critical residue Gln493 in RBD from SARS-CoV-2 provides the high affinity to human cell attachment, as well as with the other residue Asn501, which is compatible with cell binding but to a lesser extent [43].”
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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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