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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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“The RBM motif includes certain important amino acid residues (Gln493, Asn501) that augments the interaction between S protein and ACE2.”
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“While further study is required, it appears that asymptomatic persons are also potential sources of 2019-nCoV infection (Wan et al. 2020; Rothe et al. 2020).”
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“…Luo, et al., 2020), and greater ACE2 gene expression has been observed in smokers compared to non-smokers (Brake et al., 2020; Cai, 2020; Emami, Javanmardi, Pirbonyeh, & Akbari, 2020; Tian et al., 2020; Wan, Shang, Graham, Baric, & Li, 2020; Xu et al., 2020; Zhao et al., 2020; Zhou et al., 2020).”
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“Human coronaviruses SARS-CoV and SARS-CoV-2 bind to their target cells through angiotensin-converting enzyme 2 (ACE2), which is expressed by epithelial cells of the lung, intestine, kidney, and blood vessels (32,33).”
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BackgroundInfluentialACE2 expression and sex disparity in COVID-19
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“The protein component of COVID-19 that binds ACE2 is the spike protein and soluble forms of ACE2 can block virus infection (93, 94).”
BackgroundShajahan, A., Archer‐Hartmann, S. A., Supekar, N. T., Gleinich, A. S., Heiß, C., & Azadi, P. (2020) · Glycobiology · doi:10.1093/glycob/cwaa101 · Cited by 148
Spinello, A., Saltalamacchia, A., & Magistrato, A. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c01148 · Cited by 150
Virology, pathogenesis, diagnosis and in-line treatment of COVID-19
Samudrala, P. K., Kumar, P., Choudhary, K., Thakur, N., Wadekar, G. S., Dayaramani, R. A., Agrawal, M., & Alexander, A. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173375 · Cited by 158
Othman, H., Bouslama, Z., Brandenburg, J., da Rocha, J., Hamdi, Y., Ghedira, K., Srairi‐Abid, N., & Hazelhurst, S. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.05.028 · Cited by 144
“Whole-genome phylogenetic analysis of the different isolates included in this study is consistent with previous works that place the Wuhan-Hu-1 isolate close to Bat-SL-CoVZC45 and Bat-SLCoVZXC21 isolates [10,17] within the Betacoronavirus genus.”
BackgroundResultMohan, S. V., Hemalatha, M., Kopperi, H., Ranjith, I., & Kumar, A. K. (2020) · Chemical Engineering Journal · doi:10.1016/j.cej.2020.126893 · Cited by 152
Glycyrrhizic acid exerts inhibitory activity against the spike protein of SARS-CoV-2
Yu, S., Zhu, Y., Xu, J., Yao, G., Zhang, P., Wang, M., Zhao, Y., Lin, G., Chen, H., Chen, L., et al. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153364 · Cited by 152
Lin, C., Xiang, J., Yan, M., Li, H., Huang, S., & Shen, C. (2020) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2020-0187 · Cited by 145
Curcumin (a constituent of turmeric): New treatment option against COVID‐19
Babaei, F., Nassiri‐Asl, M., & Hosseinzadeh, H. (2020) · Food Science & Nutrition · doi:10.1002/fsn3.1858 · Cited by 146
Can SARS-CoV-2 Virus Use Multiple Receptors to Enter Host Cells?
Gadanec, L. K., McSweeney, K. R., Qaradakhi, T., Ali, B. A., Zulli, A., & Apostolopoulos, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22030992 · Cited by 147
Tunneling nanotubes provide a route for SARS-CoV-2 spreading
Pepe, A., Pietropaoli, S., Vos, M. R. J., Spaeth, G. B., & Zurzolo, C. (2022) · Science Advances · doi:10.1126/sciadv.abo0171 · Cited by 144
Liu, W., Zhang, S.-P., Nekhai, S., & Liu, S.-J. (2020) · Current Clinical Microbiology Reports · doi:10.1007/s40588-020-00140-w · Cited by 135
Abrishami, M., Emamverdian, Z., Shoeibi, N., Omidtabrizi, A., Daneshvar, R., Rezvani, T. S., Saeedian, N., Eslami, S., Mazloumi, M., Sadda, S. R., et al. (2020) · Canadian Journal of Ophthalmology · doi:10.1016/j.jcjo.2020.11.006 · Cited by 144
Singh, S., McNab, C., Olson, R. M., Bristol, N., Nolan, C., Bergstrøm, E., Bartos, M., Mabuchi, S., Panjabi, R., Karan, A., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(21)01897-3 · Cited by 141
Madabhavi, I., Sarkar, M. S., & Kadakol, N. (2020) · Monaldi Archives for Chest Disease · doi:10.4081/monaldi.2020.1298 · Cited by 146
A comparative overview of COVID-19, MERS and SARS: Review article
Liu, J., Xie, W., Wang, Y., Xiong, Y., Chen, S., Han, J., & Wu, Q. (2020) · International Journal of Surgery · doi:10.1016/j.ijsu.2020.07.032 · Cited by 146
“A ten-year structure study based on SARS-CoV shows that the efficiency of SARS-CoV-2 using human ACE2 may be lower than human SARS-CoV (2002) but higher than human SARS-CoV (2003), indicating that COVID-19 has acquired some transmission power between individuals [35].”
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
Pymm, P., Adair, A., Chan, L., Cooney, J. P., Mordant, F. L., Allison, C. C., López, E., Haycroft, E. R., O’Neill, M. T., Tan, L. L., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2101918118 · Cited by 137
Immunogenic potential of DNA vaccine candidate, ZyCoV-D against SARS-CoV-2 in animal models
Dey, A., Rajanathan, T. M. C., Chandra, H., Pericherla, H. P. R., Mendiratta, S. K., Choonia, H. S., Bajpai, M., Singh, A. K., Sinha, A., Saini, G., et al. (2021) · Vaccine · doi:10.1016/j.vaccine.2021.05.098 · Cited by 143
Drug repurposing strategies for COVID-19
Senanayake, S. L. (2020) · Future Drug Discovery · doi:10.4155/fdd-2020-0010 · Cited by 141
Evolutionary trajectory of SARS-CoV-2 and emerging variants
Singh, J., Pandit, P., McArthur, A. G., Banerjee, A., & Mossman, K. L. (2021) · Virology Journal · doi:10.1186/s12985-021-01633-w · Cited by 150
Zhao, K. F., Huang, J., Dai, D., Feng, Y., Liu, L., & Nie, S. (2020) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofaa250 · Cited by 141
“Scientists have noted that SARS-CoV-2 enters the human body through angiotensin-converting enzyme 2 (ACE2) receptors on the membrane of cells [5].”
BackgroundIsolation and characterization of SARS-CoV-2 from the first US COVID-19 patientPreprint
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) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.02.972935 · Cited by 134
Galson, J. D., Schätzle, S., Bashford-Rogers, R. J. M., Raybould, M. I. J., Kovaltsuk, A., Kilpatrick, G. J., Minter, R., Finch, D. K., Dias, J. C., James, L. K., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.605170 · Cited by 136
Pharmacological perspective: glycyrrhizin may be an efficacious therapeutic agent for COVID-19
Luo, P., Liu, D., & Li, J. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105995 · Cited by 142
The Potential Intermediate Hosts for SARS-CoV-2
Zhao, J., Cui, W., & Tian, B. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.580137 · Cited by 148
COVID-19 and Alzheimer’s disease: how one crisis worsens the other
Xia, X., Wang, Y., & Zheng, J. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00237-2 · Cited by 138
“sine 31 on ACE2 with high affinity [11, 13, 14].”
Backgroundde Oliveira, O. V., Rocha, G. B., Paluch, A. S., & da Costa, L. T. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1772885 · Cited by 141
“However, the RBD from SARS-CoV-2 has highest affinity with the ACE2 than SARS-CoV as confirmed and evidenced by experimental (Wrapp et al., 2020; Wan et al., 2020), and theoretical data (Peng et al., 2020).”
Wu, Z., Hu, R., Zhang, C., Ren, W., Yu, A., & Zhou, X. (2020) · Critical Care · doi:10.1186/s13054-020-03015-0 · Cited by 138
Velázquez-Salinas, L., Zárate, S., Eberl, S., Gladue, D. P., Novella, I. S., & Borca, M. V. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.550674 · Cited by 135
Okada, P. A., Buathong, R., Phuygun, S., Thanadachakul, T., Parnmen, S., Wongboot, W., Waicharoen, S., Wacharapluesadee, S., Uttayamakul, S., Vachiraphan, A., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.8.2000097 · Cited by 137
Zhen, W., Manji, R., Smith, E., & Berry, G. J. (2020) · Journal of Clinical Microbiology · doi:10.1128/jcm.00743-20 · Cited by 134
Chemistry and Biology of SARS-CoV-2
Dömling, A. S. S., & Gao, L. (2020) · Chem · doi:10.1016/j.chempr.2020.04.023 · Cited by 138
“The SARS-CoV-2 entry through receptor binding was elucidated independently by several groups.(31,32) On the basis of the rich knowledge about SARS-CoV and the sequence homology, it was suggested that SARS-CoV-2 uses angiotensin-converting enzyme 2 (ACE2) as its receptor (Figure 6).”
Lópes, R. D., Macedo, A. V. S., Silva, P. G. M. D. B. E., Moll-Bernardes, R. J., Feldman, A., Arruda, G., de Souza, A. S., de Albuquerque, D. C., Barbosa, L. M., Santos, M. F., et al. (2020) · American Heart Journal · doi:10.1016/j.ahj.2020.05.002 · Cited by 138
“Abbreviations: ACE = angiote ACEI = ACE inhibitor; Ang (1–7)=angiotensin 1–7; Ang I = Angiotensin I; alveolar cells; ARBs = angiotensin receptor blockers; COVID-19 = coron activator inhibitor 1; RAAS = renin-angiotensin-aldosterone system; SARS-C (and other human pathogenic coronaviruses) binds to target cells through…”
BackgroundDoes SARS-CoV-2 Bind to Human ACE2 More Strongly Than Does SARS-CoV?
Nguyen, H. L., Lan, P. D., Thai, N. Q., Nissley, D. A., O’Brien, E. P., & Li, M. S. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c04511 · Cited by 137
Efforts at COVID-19 Vaccine Development: Challenges and Successes
Haque, A., & Pant, A. B. (2020) · Vaccines · doi:10.3390/vaccines8040739 · Cited by 141
“Analysis of the receptor binding motif (RBM) in the spike protein showed that most of the amino acid residues essential for receptor binding were conserved between SARS-CoV and SARS-CoV-2, suggesting that the 2 CoV strains use the same host receptor for cell entry [11].”
BackgroundNeurological complications and infection mechanism of SARS-CoV-2
Wan, D., Du, T., Hong, W., Chen, L., Que, H., Lu, S., & Peng, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00818-7 · Cited by 140
“CNS CELL LINES Most research methods of SARS-CoV-2 currently available are based on SARS-CoV due to their 78% nucleotide homology.(205) Although the neurotropism of SARS-CoV-2 has been demonstrated,(206) no specialized neural cell line models have been applied to study it.”
MethodCoronavirus disease (COVID-19): a scoping review
Lv, M., Luo, X., Estill, J., Liu, Y., Ren, M., Wang, J., Wang, Q., Zhao, S., Wang, X., Yang, S., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.15.2000125 · Cited by 122
Potential role of ACE2 in coronavirus disease 2019 (COVID-19) prevention and management
Liu, M., Wang, T., Zhou, Y., Zhao, Y., Zhang, Y., & Li, J. (2020) · Journal of Translational Internal Medicine · doi:10.2478/jtim-2020-0003 · Cited by 137
Children’s heart and COVID-19: Up-to-date evidence in the form of a systematic review
Sanna, G., Serrau, G., Bassareo, P. P., Neroni, P., Fanos, V., & Marcialis, M. A. (2020) · European Journal of Pediatrics · doi:10.1007/s00431-020-03699-0 · Cited by 136
Angiotensin-converting enzyme 2 (ACE2): SARS-CoV-2 receptor and RAS modulator
Bian, J., & Li, Z. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.006 · Cited by 148
“membrane fusion (2b), virus replication (3), virus assembly (4), and virus exit (5).”
Qi, J., Zhou, Y., Hua, J., Zhang, L., Bian, J., Liu, B., Zhao, Z., & Jin, S. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18010284 · Cited by 135
Emergence of Novel Coronavirus 2019-nCoV: Need for Rapid Vaccine and Biologics Development
Shanmugaraj, B., Malla, A., & Phoolcharoen, W. (2020) · Pathogens · doi:10.3390/pathogens9020148 · Cited by 139
Silhol, F., Sarlon, G., Deharo, J., & Vaisse, B. (2020) · Hypertension Research · doi:10.1038/s41440-020-0476-3 · Cited by 137
“2), COVID-19 virus uses the enzymatic receptor of ACE2 to penetrate the host cell [9, 10].”
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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