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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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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969 · cited 1×
“Our structural analyses confidently predict that 2019-nCoV uses ACE2 as its host receptor, consistent with two other new publications (30, 31).”
ResultFast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · cited 1×
“Protein sequence alignments were done using Clustal Omega (33).”
MethodAngiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
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. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923 · cited 2×
“2) but is ancestral to both human SARS-CoV (epidemic strain isolated in year 2002) and bat SARS-CoV strains that use ACE2 receptor to enter and infect primary host lung cells (11, 17).”
BackgroundOrigin and evolution of pathogenic coronaviruses
Cui, J., Li, F., & Shi, Z. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0118-9 · Cited by 5,729 · cited 2×
“It is believed that bats and palm civets were the natural and intermediate reservoirs for SARS-CoV, respectively, and that SARS-CoV transmitted from palm civets to humans in an animal market in Southern China (12–14).”
BackgroundSelf-citationLetko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
Coronavirus as a possible cause of severe acute respiratory syndrome
Peiris, M. J. S., Lai, S., Poon, L. L. M., Guan, Y., Yam, L., Lim, W., Nicholls, J. M., Yee, W., Yan, W., Cheung, M., et al. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13077-2 · Cited by 2,916
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740 · cited 1×
“An envelope-anchored spike protein mediates coronavirus entry into host cells by first binding to a host receptor and then fusing viral and host membranes (16).”
BackgroundSelf-citationA Major Outbreak of Severe Acute Respiratory Syndrome in Hong Kong
Lee, N. L. S., Hui, D. S. C., Wu, A. K. L., Chan, P. K. S., Cameron, P. A., Joynt, G. M., Ahuja, A. T., Yung, M. Y., Leung, C. B., To, K. F., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030685 · Cited by 2,638
Guan, Y., Zheng, B., He, Y., Liu, X. L., Zhuang, Z. X., Cheung, C. L., Luo, S., Li, P. H., Zhang, L., Guan, Y., et al. (2003) · Science · doi:10.1126/science.1087139 · Cited by 2,404
Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
Raj, V. S., Mou, H., Smits, S. L., Dekkers, D. H. W., Müller, M. A., Dijkman, R., Muth, D., Demmers, J. A. A., Zaki, A., Fouchier, R. A. M., et al. (2013) · Nature · doi:10.1038/nature12005 · Cited by 2,061 · cited 2×
“3C), and yet they recognize the same 124 receptor dipeptidyl peptidase 4 (DPP4) (27, 28).”
BackgroundStructure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
Li, F., Li, W., Farzan, M., & Harrison, S. C. (2005) · Science · doi:10.1126/science.1116480 · Cited by 2,035 · cited 4×
“at the RBD/human ACE2 interface, enhances viral binding to human ACE2, and played a 158 critical role in the human-to-human transmission of SARS-CoV (24-26).”
BackgroundMethodInfluentialSelf-citationThe Genome Sequence of the SARS-Associated Coronavirus
Marra, M. A., Jones, S. J. M., Astell, C. R., Holt, R. A., Brooks-Wilson, A. R., Butterfield, Y. S. N., Khattra, J. S., Asano, J. K., Barber, S., Chan, S. Y., et al. (2003) · Science · doi:10.1126/science.1085953 · Cited by 2,027
Coronaviruses post-SARS: update on replication and pathogenesis
Perlman, S. M., & Netland, J. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2147 · Cited by 1,797 · cited 1×
“Coronaviruses are a large family of single-stranded enveloped RNA viruses and 81 can be divided into four major genera (15).”
BackgroundIsolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778 · cited 1×
“2), but is ancestral to both human SARS-CoV 117 (epidemic strain isolated in year 2002) and bat SARS-CoV strains that use ACE2 118 receptor to enter and infect primary host lung cells (11, 17).”
BackgroundEvidence of Airborne Transmission of the Severe Acute Respiratory Syndrome Virus
Yu, I. T. S., Li, Y., Wong, T. W., Tam, W., Chan, A., Lee, J. H. W., Leung, D. Y. C., & Ho, T. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa032867 · Cited by 1,255
Lethal Infection of K18- hACE2 Mice Infected with Severe Acute Respiratory Syndrome Coronavirus
McCray, P. B., Pewe, L., Wohlford-Lenane, C., Hickey, M., Manzel, L., Shi, L., Netland, J., Jia, H. P., Halabi, C., Sigmund, C. D., et al. (2007) · Journal of Virology · doi:10.1128/jvi.02012-06 · Cited by 1,010
Receptor and viral determinants of SARS‐coronavirus adaptation to human ACE2
Li, W., Zhang, C., Sui, J., Kuhn, J. H., Moore, M. J., Luo, S., Wong, S.-K., Huang, I., Xu, K., Vasilieva, N. Y., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600640 · Cited by 993
Hu, B., Zeng, L., Yang, X., Ge, X.-Y., Zhang, W., Li, B., Xie, J., Shen, X.-R., Zhang, Y.-Z., Wang, N., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006698 · Cited by 956
Cross-host evolution of severe acute respiratory syndrome coronavirus in palm civet and human
Song, H., Tu, C., Zhang, G., Wang, S., Zheng, K. C., Lei, L., Chen, Q., Gao, Y., Zhou, H., Xiang, H., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409608102 · Cited by 693
Receptor Recognition Mechanisms of Coronaviruses: a Decade of Structural Studies
Li, F. (2014) · Journal of Virology · doi:10.1128/jvi.02615-14 · Cited by 583 · cited 3×
“In a span of about 10 years, we determined a series of crystal 89 structures of SARS-CoV RBD complexed with ACE2; the RBDs were from SARS-CoV 90 strains isolated from different hosts species in different years and the ACE2 receptor 91 orthologues were derived from different animal species (18, 24-26).”
MethodSelf-citationYang, Y., Du, L., Liu, C., Wang, L., Ma, C., Tang, J., Baric, R. S., Jiang, S., & Li, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405889111 · Cited by 279
Self-citationLi, W., Wong, S.-K., Li, F., Kuhn, J. H., Huang, I., Choe, H., & Farzan, M. (2006) · Journal of Virology · doi:10.1128/jvi.80.9.4211-4219.2006 · Cited by 278
Self-citationReceptor recognition and cross-species infections of SARS coronavirus
Li, F. (2013) · Antiviral Research · doi:10.1016/j.antiviral.2013.08.014 · Cited by 266 · cited 3×
“It is believed that bats and palm civets were the natural and intermediate reservoirs for SARS-CoV, respectively, and that SARS-CoV transmitted from palm civets to humans in an animal market in Southern China (12–14).”
BackgroundSelf-citationMechanisms of Host Receptor Adaptation by Severe Acute Respiratory Syndrome Coronavirus
Wu, K., Peng, G., Wilken, M. S., Geraghty, R. J., & Li, F. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.325803 · Cited by 252 · cited 2×
“Importantly, we identified two virus-binding hot spots on human ACE2 (24, 26).”
BackgroundMethodSelf-citationMoore, M. J., Dorfman, T., Li, W., Wong, S. K., Li, Y., Kuhn, J. H., Coderre, J. A., Vasilieva, N. Y., Han, Z., Greenough, T. C., et al. (2004) · Journal of Virology · doi:10.1128/jvi.78.19.10628-10635.2004 · Cited by 239
D‐Dimer and Prothrombin Time Are the Significant Indicators of Severe COVID‐19 and Poor Prognosis
Long, H., Nie, L., Xiang, X., Li, H., Zhang, X., Fu, X., Ren, H., Liu, W., Wang, Q., & Wu, Q. (2020) · BioMed Research International · doi:10.1155/2020/6159720 · Cited by 219
Li, F. (2008) · Journal of Virology · doi:10.1128/jvi.00442-08 · Cited by 184 · cited 4×
“at the RBD/human ACE2 interface, enhances viral binding to human ACE2, and played a 158 critical role in the human-to-human transmission of SARS-CoV (24-26).”
BackgroundMethodInfluentialSelf-citationGut-lung axis and dysbiosis in COVID-19
Aktaş, B., & Aslım, B. (2020) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-2005-102 · Cited by 170
Li, W., Greenough, T. C., Moore, M. J., Vasilieva, N. Y., Somasundaran, M., Sullivan, J. L., Farzan, M., & Choe, H. (2004) · Journal of Virology · doi:10.1128/jvi.78.20.11429-11433.2004 · Cited by 168
Qu, X., Hao, P., Song, X., Jiang, S., Liu, Y., Wang, P., Rao, X., Song, H., Wang, S., Zuo, Y., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500662200 · Cited by 160
Neuromechanisms of SARS-CoV-2: A Review
DosSantos, M. F. H., Devalle, S., Aran, V., Capra, D., Roque, N. R., Coelho‐Aguiar, J. D. M., Spohr, T. C. L. D. S. E., Subilhaga, J. G., Pereira, C. M., Meira, I. D., et al. (2020) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2020.00037 · Cited by 158
Letko, M. C., & Munster, V. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.22.915660 · Cited by 139 · cited 1×
“Our structural analyses confidently predict that 2019-nCoV uses ACE2 as its host 221 receptor, consistent to two other new publications (30, 31).”
Liang, G., Chen, Q., Xu, J., Liu, Y., Lim, W. W. L., Peiris, M. J. S., Anderson, L. J., Ruan, L., Li, H., Kan, B., et al. (2004) · Emerging infectious diseases · doi:10.3201/eid1010.040445 · Cited by 136 · cited 1×
“It briefly re-emerged in 2003-2004, with 4 72 confirmed cases of mild human infections and no human-to-human transmission (5-7).”
BackgroundSheahan, T. P., Rockx, B., Donaldson, E., Sims, A. M., Pickles, R. J., Corti, D., & Baric, R. S. (2007) · Journal of Virology · doi:10.1128/jvi.02041-07 · Cited by 129
Self-citationHou, Y.-X., Peng, C., Yu, M., Li, Y., Han, Z., Li, F., Wang, L., & Shi, Z. (2010) · Archives of Virology · doi:10.1007/s00705-010-0729-6 · Cited by 81 · cited 1×
“The 208 situation involving bat ACE2 is complex because of the diversity of bat species (29).”
BackgroundSelf-citationLiu, L., Fang, Q., Dèng, F., Wang, H., Yi, C. E., Ba, L., Yu, W., Lin, R. D., Li, T., Hú, Z., et al. (2007) · Journal of Virology · doi:10.1128/jvi.02389-06 · Cited by 57 · cited 1×
“It is worth noting that SARS-CoV was isolated in wild palm civets near Wuhan in 250 2005 (9), and its RBD had already been well adapted to civet ACE2 (except for residue 251 487).”
BackgroundA contemporary review on pathogenesis and immunity of COVID-19 infection
Mirzaei, R., Karampoor, S., Sholeh, M., Moradi, P., Ranjbar, R., & Ghasemi, F. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05621-1 · Cited by 57
Molecular Aspects of Co-morbidities in COVID-19 Infection.
Pouya, F., Saber, Z. I., & Kerachian, M. A. (2020) · PubMed Central · doi:10.22038/abjs.2020.47828.2361 · Cited by 15
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Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
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Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983
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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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