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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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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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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“For all CoVs, S is further cleaved and processed by host proteases, TMPRSS2 (Walls et al., 2020) at the S 2 ′ site and in a recent study it has been reported that a serine protease inhibitor, which act on TMPRSS2 significantly inhibit novel coronavirus entry (Wan et al., 2020).”
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“The plausible mechanism of actions includes inhibition of angiotensin converting enzyme 2 (ACE-2) present on the cell surface for virus entry (by reduction of glycosylation in the enzyme) (4, 5), inhibition of release of viral particles into intracellular space (6, 7), and an anti-inflammatory effect (inhibition of in…”
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Natural and Synthetic Drugs as Potential Treatment for Coronavirus Disease 2019 (COVID-2019)
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Polyphenols are potential nutritional adjuvants for targeting COVID ‐19
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Did Climate Change Influence the Emergence, Transmission, and Expression of the COVID-19 Pandemic?
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“In concurrent to SARS-CoV-2 outbreak, this review explores and highlights similarity between the binding affinity of spike glycoprotein to Angiotensin-converting enzyme receptor-2(ACE 2) as a primary cell entry receptor for both Severe acute respiratory syndrome Coronavirus (SARS-CoV) and Severe acute respiratory synd…”
The emerging role of probiotics as a mitigation strategy against coronavirus disease 2019 (COVID-19)
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“[48] reported that SARS-CoV-2 is optimized to bind”
Exploring salivary diagnostics in COVID-19: a scoping review and research suggestions
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InfluentialDemyelination as a result of an immune response in patients with COVID-19
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“Similar to SARS-CoV, the SARSCoV-2 and a host receptor, Angiotensin-converting enzyme 2 (ACE2) have a stronger binding capacity [18].”
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BackgroundInfluentialCOVID‐19 and Acute Coronary Syndromes: From Pathophysiology to Clinical Perspectives
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“Among them, the S glycoprotein is an important target of therapies since it is responsible for entry into host cells via its interaction with the angiotensin-converting enzyme 2 (ACE2) cell receptor [17,18].”
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Non-Coding RNAs and SARS-Related Coronaviruses
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ResultCoronavirus 2019 Infectious Disease Epidemic: Where We Are, What Can Be Done and Hope For
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BackgroundThe Impact of COVID-19 on Cancer Risk and Treatment
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“Elevated blood glucose levels also affect ACE2 expression, which is the COVID-19 viral binding site for host cell entry [10].”
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“Even though SARS-S and SARS-2-S share 76% of amino acid identity, no study has shown how SARS-2-S or SARS-S uses ACE2 and TMPRSS2 to adhere to the target cell (15, 16).”
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“Association of SARS-CoV-2 and TLR4 In addition to the ACE2, binding to toll-like receptors (TLRs), especially TLR-4, may contribute to the infectivity and pathogenesis of SARS-CoV-2 (49).”
BackgroundGastrointestinal Involvement in SARS-CoV-2 Infection
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Susceptibility Analysis of COVID-19 in Smokers Based on ACE2Preprint
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“Studies have established that ACE2 is the receptor for the SARS-CoV [9,10] and Wuhan new coronavirus (COVID-19) [11-13].”
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“Preliminary treatment of COVID–19 depends upon the severity of infection which ranges from mild to strong including, if necessary administration of oxygen, maintaining the body fluids and administration of antibiotics and antiviral drugs to combat coinfections because of numerous types of bacteria and virus [9].”
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“The interaction of inhibitory peptidyl residues with these amino acids is expected to impede the attachment of SARS-CoV-2 spike protein to ACE2 receptor (Wan et al., 2020).”
BackgroundEpigenetic mechanisms influencing COVID-19
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The coronavirus global pandemic and its impacts on society
Sawicka, B., Aslan, I., Corte, V. D., Periasamy, A., Krishnamurthy, S. K., Mohammed, A., Said, M. M. T., Saravanan, P., Gaudio, G. D., Adom, D., et al. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85156-5.00037-7 · Cited by 49
Janus sword actions of chloroquine and hydroxychloroquine against COVID-19
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“Further, CQ-induced Golgi de-acidification may result in decreased expression levels of ACE2.”
InfluentialCoronavirus and Cardiometabolic Syndrome
Mechanick, J. I., Rosenson, R. S., Pinney, S., MANCINI, D. M., Narula, J., & Fuster, V. (2020) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2020.07.069 · Cited by 51
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“The residues Leu455, Phe486 and Gln493 of RBD have been reported to interact with Lys31 (hotspot 31), whereas residues Asn487 and Ser494 of the RBD are described to interact with Lys353 (hotspot 353) of the human ACE2 [73,74].”
BackgroundInfluentialBinding mode of SARS-CoV-2 fusion peptide to human cellular membrane
Gorgun, D., Lihan, M., Kapoor, K., & Tajkhorshid, E. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.02.041 · Cited by 48
“SARS-CoV2 recognizes and infects human cells that express a cell surface receptor termed angiotensin-converting enzyme 2 (ACE2) (4), which is specifically recognized by the viral spike glycoprotein (S-protein).”
Verkhivker, G. M., Agajanian, S., Öztaş, D. Y., & Gupta, G. (2021) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c00372 · Cited by 40
Impact of Expressing Cells on Glycosylation and Glycan of the SARS-CoV-2 Spike Glycoprotein
Wang, Y., Wu, Z., Hu, W., Hao, P., & Yang, S. (2021) · ACS Omega · doi:10.1021/acsomega.1c01785 · Cited by 50
Mechanisms of Lung Injury Induced by SARS-CoV-2 Infection
Upadhya, S. W., Rehman, J., Malik, A. B., & Chen, S. (2021) · Physiology · doi:10.1152/physiol.00033.2021 · Cited by 54
Qing, E., & Gallagher, T. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.02.007 · Cited by 48
SARS-CoV-2 leading to acute pancreatitis: an unusual presentation
Alves, A. M., Yvamoto, E. Y., Marzinotto, M. A. N., Teixeira, A. C. D. S., & Carrilho, F. J. (2020) · The Brazilian Journal of Infectious Diseases · doi:10.1016/j.bjid.2020.08.011 · Cited by 50
ACTIVating Resources for the COVID-19 Pandemic: In Vivo Models for Vaccines and Therapeutics
Hewitt, J., Lutz, C. M., Florence, W. C., Pitt, M. L. M., Rao, S., Rappaport, J., & Haigwood, N. L. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.09.016 · Cited by 47
“Phylogenetic comparisons of ACE2 proteins allowed for predictions of species that are susceptible to SARS-CoV-2 infection (Liu et al., 2020a; Luan et al., 2020; Qiu et al., 2020; Wan et al., 2020), as ACE2 is a key determinant of infectivity (Liu et al., 2020a).”
Gyebi, G. A., Adegunloye, A. P., Ibrahim, I. M., Ogunyemi, O. M., Afolabi, S. O., & Ogunro, O. B. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1835726 · Cited by 49
“Relative to SARS-CoV, SARS-CoV-2 is believed to bind human ACE2 more efficiently, thereby increasing its chance of human to human transmission (Wan et al., 2020).”
BackgroundResultEvaluating angiotensin-converting enzyme 2-mediated SARS-CoV-2 entry across species
Zhang, H.-L., Li, Y., Sun, J., Zhang, Y.-Y., Wang, T.-Y., Sun, M.-X., Wang, M.-H., Yang, Y.-L., Hu, X.-L., Tang, Y., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100435 · Cited by 47
Nag, A., Paul, S., Banerjee, R., & Kundu, R. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104818 · Cited by 50
“Contents lists available at ScienceDirect Computers in Biology and Medicine journal homepage: www.elsevier.com/locate/compbiomed https://doi.org/10.1016/j.compbiomed.2021.104818 Received 26 April 2021; Received in revised form 26 August 2021; Accepted 26 August 2021 Computers in Biology and Medicine 137 (2021) 104818…”
InfluentialTragni, V., Preziusi, F., Laera, L., Onofrio, A., Mercurio, I., Todisco, S., Volpicella, M., Grassi, A., & Pierri, C. L. (2022) · The EPMA Journal · doi:10.1007/s13167-021-00267-w · Cited by 49
“Indeed, it is well established that protein–protein interactions depend both on residues at the protein–protein interface but also on residues far from the protein–protein interface that can participate to protein folding through long-range interactions [40–44].”
BackgroundCross-species transmission, evolution and zoonotic potential of coronaviruses
Li, Q., Shah, T., Wang, B., Qu, L., Wang, R., Hou, Y., Baloch, Z., & Xia, X. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1081370 · Cited by 46
“SARS-CoV, HCoV-NL63, and SARSCoV-2 use the host cellular ACE2 receptor to enter the host cell cytoplasm (Hofmann et al., 2005; Wan et al., 2020).”
BackgroundDouble Jeopardy: Methamphetamine Use and HIV as Risk Factors for COVID-19
Carrico, A. W., Horvath, K. J., Grov, C., Moskowitz, J. T., Pahwa, S. G., Pallikkuth, S., & Hirshfield, S. (2020) · AIDS and Behavior · doi:10.1007/s10461-020-02854-w · Cited by 48
“Meth use could also contribute local immune dysregulation as well as alter the expression of angiotensin-converting enzyme 2 (ACE-2) receptors, a key site for SARS-CoV-2 binding in the lungs and small intestine [30] .”
BackgroundAleksova, A., Ferro, F., Gagno, G., Cappelletto, C., Santon, D., Rossi, M., Ippolito, G., Zumla, A. I., Beltrami, A. P., & Sinagra, G. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13101 · Cited by 48
Tariq, A., Mateen, R. M., Afzal, M. S., & Saleem, M. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.06.063 · Cited by 48
da Silva, P. G., Mesquita, J. R., Nascimento, M. D. S. J., & Ferreira, V. A. M. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.141483 · Cited by 53
“…frequency of homologous recombination and genetic diversity, another key determinant of interspecies transmission and host speci fi city of SARS-CoV-like viruses is the interaction of the spike (S) protein with the host receptor angiotensin-converting enzyme 2 (ACE2) (F. Li, 2013; Wan et al., 2020).”
BackgroundRaghav, A., Khan, Z. A., Upadhayay, V. K., Tripathi, P., Gautam, K. A., Mishra, B. K., Ahmad, J., & Jeong, G. (2021) · Cells · doi:10.3390/cells10030587 · Cited by 48
“It has been previously reported that ACE2 is the primary receptor for both SARS-CoV-2 and SARS-CoV [12,13].”
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The role of vitamin D in reducing SARS-CoV-2 infection: An update
Alam, M. S., Czajkowsky, D. M., Islam, M. A., & Rahman, M. A. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107686 · Cited by 49
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“S is composed of two subunits: S1, which mediates attachment to the host cell receptor angiotensin-converting enzyme 2 (ACE2) and, S2, which facilitates membrane fusion (Shang et al., 2020; Wan et al., 2020; Letko et al., 2020).”
The COVID-19 Pandemic and its Impact on the Cardio-Oncology Population
Asokan, I., Rabadia, S. V., & Yang, E. H. (2020) · Current Oncology Reports · doi:10.1007/s11912-020-00945-4 · Cited by 49
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Genetic and Pathogenic Characterization of SARS-CoV-2: A Review
Bahrami, A., & Ferns, G. A. (2020) · Future Virology · doi:10.2217/fvl-2020-0129 · Cited by 49
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Derivation and Validation of a Predictive Score for Disease Worsening in Patients with COVID-19
Gerotziafas, G., Sergentanis, T. Ν., Voiriot, G., Lassel, L., Papageorgiou, C., Elabbadi, A., Turpin, M., Dreden, P. V., Papageorgiou, L., Ψαλτοπούλου, Θ., et al. (2020) · Thrombosis and Haemostasis · doi:10.1055/s-0040-1716544 · Cited by 46
Micronutrients and bioactive substances: Their potential roles in combating COVID-19
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“The receptor-binding domain of the virus S attaches to the ACE2 receptor of lung epithelial cells [12,13].”
Identification of presented SARS-CoV-2 HLA class I and HLA class II peptides using HLA peptidomics
Nagler, A., Kalaora, S., Barbolin, C., Gangaev, A., Ketelaars, S. L. C., Alon, M., Pai, J. A., Benedek, G., Yahalom-Ronen, Y., Noam Erez, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109305 · Cited by 47
“First, we confirmed that these cells express the ACE2 receptor and transmembrane protease serine 2 (TMPRSS), which are known to be required for SARS-CoV-2 entry into the cells (Hoffmann et al., 2020; Matsuyama et al., 2020; Wan et al., 2020; Zhou et al., 2020; Figure S2B).”
Defining the Innate Immune Responses for SARS-CoV-2-Human Macrophage Interactions
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“Pigs are most likely to contract SARS-CoV-2 because they have the same ACE2 receptor binding sites as humans (Wan et al. 2020).”
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Coronavirus Disease 2019 and the Cerebrovascular‐Cardiovascular Systems: What Do We Know So Far?
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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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