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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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“Taken together, these new results showed that first, human ECs, regardless of the tissue origins of human ECs (umbilical vein, microvascular, or dermal), can be infected by various RNA viruses and DNA viruses, suggesting that human EC express influenza virus receptor a2,6- or a2,3-linked sialic acid (73), MERS recepto…”
BackgroundInfluentialPantazi, I., Al-Qahtani, A. A., Alhamlan, F. S., Alothaid, H., Matou‐Nasri, S., Sourvinos, G., Vergadi, E., & Tsatsanis, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.683800 · Cited by 74
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“[36] has predicted that the single N501T mutation in RBD of S-protein might lead to an augmented binding affinity for ACE2.”
Insights on SARS-CoV-2 Molecular Interactions With the Renin-Angiotensin System
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The Perfect Storm: COVID-19 Health Disparities in US Blacks
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ACE2, COVID-19 Infection, Inflammation, and Coagulopathy: Missing Pieces in the Puzzle
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“The spike protein of SARS-CoV-1 is 76–78% identical to that of SARS-CoV-2 [27].”
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“Diabetes may facilitate the entry of SARS-CoV-2 by increased expression of ACE2 surface receptors because of the disease itself and the treatment strategies used [10, 11, 51-53].”
MethodCOVID-19: Proposing a Ketone-Based Metabolic Therapy as a Treatment to Blunt the Cytokine Storm
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“In the case of MERS-CoV and SARS-CoV subtype viruses, the receptors are human dipeptidyl peptidase 4 (hDPP4) [126] and human angiotensin-converting enzyme 2 (hACE2) [118], respectively.”
BackgroundInfluentialPfizer-BioNTech COVID-19 Vaccine (BNT162b2) Side Effects: A Systematic Review
Dighriri, I. M., Alhusayni, K. M., Mobarki, A. Y., Aljerary, I. S., Alqurashi, K. A., Aljuaid, F., Al-Amri, K. A., Mutwalli, A. A., Maashi, N. A., Aljohani, A., et al. (2022) · Cureus · doi:10.7759/cureus.23526 · Cited by 79
“The coronavirus has a spikeshaped surface feature known as an S protein [15-18].”
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“Crucial for binding of ACE2 receptor amino acids (442, 487, 479, 487, and 491) are 206 located in the RBM of the S protein (17,20).”
BackgroundCOVID-19 PANDEMIA: NEUROPSYCHIATRIC COMORBIDITY AND CONSEQUENCES
Sinanović, O., Muftić, M., & Sinanović, S. (2020) · Psychiatria Danubina · doi:10.24869/psyd.2020.236 · Cited by 71
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BackgroundA short review on antibody therapy for COVID-19
Kumar, G. V., Jeyanthi, V., & Ramakrishnan, S. (2020) · New Microbes and New Infections · doi:10.1016/j.nmni.2020.100682 · Cited by 69
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“ACE2 expression is increased in diabetic patients treated with ACE inhibitors and ARBs [82].”
BackgroundVitamin D and COVID-19: An Overview of Recent Evidence
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“A distinct location, the receptor-binding domain (RBD), in S protein is important for binding to ACE2 (F. Li et al., 2005; Wan et al., 2020).”
Structural Basis for Human Receptor Recognition by SARS-CoV-2 Omicron Variant BA.1
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An ACE2-dependent Sarbecovirus in Russian bats is resistant to SARS-CoV-2 vaccines
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“Since the spike (S) protein has pivotal roles in receptor binding and membrane fusion, this is an attractive antigen for the development of vaccines aimed at inducing antibodies that block virus binding/fusion and ultimately neutralize virus infection [2].”
BackgroundN-Acetylcysteine as a Potential Treatment for COVID-19
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“Tavares 12 Discussion The majority of biophysical and structural studies being conducted on coronaviruses focus on the viral proteins, such as the virion constituents and components of the replicationtranscription machinery (Gao et al. 2020; Wan et al. 2020; Wrapp et al. 2020; Zhang et al. 2020).”
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BackgroundProteasome Inhibitors as a Possible Therapy for SARS-CoV-2
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SARS-CoV-2 spike produced in insect cells elicits high neutralization titres in non-human primates
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“In helicase (nsp13) acting as RNA 5′-triphosphatase [39], one mutation (L (leucine)5604F (phenylalanine)) was present, and in S protein, which binds to the receptors [40], three mutations (T95I (isoleucine), N185K, S (Serine)968A) were present.”
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SARS-CoV-2 Infection in Dogs and Cats: Facts and Speculations
Decaro, N., Balboni, A., Bertolotti, L., Martino, P. A., Mazzei, M., Mira, F., & Pagnini, U. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.619207 · Cited by 66
Nguyen, N. H. L., Kim, S., Lindemann, G. W., & Berry, V. (2021) · ACS Nano · doi:10.1021/acsnano.1c02549 · Cited by 66
Zhang, D., Li, L., Chen, Y., Ma, J., Yang, Y., Aodeng, S., Cui, Q., Wen, K., Xiao, M., Xie, J., et al. (2021) · Molecular Medicine · doi:10.1186/s10020-021-00412-1 · Cited by 72
A raising dawn of pentoxifylline in management of inflammatory disorders in Covid-19
Mostafa‐Hedeab, G., Al-Kuraishy, H. M., Al-Gareeb, A. I., Jeandet, P., Saad, . M., & Batiha, G. E. (2022) · Inflammopharmacology · doi:10.1007/s10787-022-00993-1 · Cited by 66
“The main obstacle in for induction of mouse SARS-CoV-2 infection is the lack of suitable receptors to recruit viral infection since mouse ACE2 does not sufficiently bind SARSCoV-2 spike protein (Wan et al. 2020).”
BackgroundAdvances in Research on Antiviral Activities of Sulfated Polysaccharides from Seaweeds
Wei, Q., Fu, G., Wang, K., Yang, Q., Zhao, J., Wang, Y., Ji, K., & Song, S. (2022) · Pharmaceuticals · doi:10.3390/ph15050581 · Cited by 72
Basit, A., Ali, T., & Rehman, S. U. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1768150 · Cited by 67
“Since, the binding residues of ACE2 involve in interaction with RBD are located at amino acid position 21-119 (Wan et al., 2020a; Yan et al., 2020), therefore, we hypothesized that this fragment carrying all the binding residues will have better binding affinity for RBD and can hinder the…”
BackgroundDk, L., & Alkhovsky, S. V. (2020) · Problems of Virology · doi:10.36233/0507-4088-2020-65-2-62-70 · Cited by 92
“Изменение рецепторной специфичности у вирусов SARS-CoV и SARS-CoV-2 связано с определёнными мутациями в рецептор-связывающем домене белка S [31].”
Molecular Pathogenesis, Immunopathogenesis and Novel Therapeutic Strategy Against COVID-19
Chatterjee, S. K., Saha, S., & Muñoz, M. N. M. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00196 · Cited by 65
“have proved that SARS-CoV-2 receptor-binding domain (RBD) contain residue 394 (glutamine), which has sequence similarity with SARS-CoV residue 479, and both can be accepted by the human ACE2 receptor on the critical lysine 31 (Wan et al., 2020).”
BackgroundAngiotensin Converting Enzyme 2 (ACE2) in Pregnancy: Preeclampsia and Small for Gestational Age
Tamanna, S., Clifton, V. L., Rae, K. M., Helden, D. F. V., Lumbers, E. R., & Pringle, K. G. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.590787 · Cited by 64
“The SARS-CoV-2 spike protein binds with human ACE2 with substantially higher affinity than does the spike protein of SARS-CoV (Walls et al., 2020; Wan et al., 2020; Wrapp et al., 2020).”
BackgroundInfluentialExpression Analyses of MicroRNAs in Hamster Lung Tissues Infected by SARS-CoV-2
Kim, W. R., Park, E. G., Kang, K.-W., Lee, S., Kim, B., & Kim, H. (2020) · Molecules and Cells · doi:10.14348/molcells.2020.0177 · Cited by 65
“In accordance with the analysis of receptor affinity, SARSCoV-2 has higher binding affinity to ACE2 than the 2003 strain of SARS-CoV (Wan et al., 2020).”
BackgroundMethodVivarelli, S., Falzone, L., Torino, F., Scandurra, G., Russo, G. L., Bordonaro, R., Pappalardo, F., Spandidos, D. A., Raciti, G., & Libra, M. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5159 · Cited by 64
“To enter the host cells, SARS-CoV-2, similar to SARS-CoV, binds to the extracellular enzymatic domain of the single pass transmembrane angiotensin-converting enzyme 2 (ACE2) receptor (14).”
BackgroundBalmeh, N., Mahmoudi, S., & Fard, N. A. (2021) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2021.100515 · Cited by 65
Lee, C.-Y., & Lowen, A. C. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.03.009 · Cited by 71
“found that ferrets and humans share critical virus-binding residues in their ACE2 sequences and suggested that ferrets may serve as an animal model for SARS-CoV-2 [75].”
BackgroundGurunathan, S., Kang, M.-H., & Kim, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.716407 · Cited by 67
“The stronger affinity between SARS-CoV-2 and ACE2 could promote infection and viral spread (87).”
BackgroundMontezano, A. C. I., Camargo, L. L., Mary, S., Neves, K. B., Rios, F. J. O., Stein, R., Alves-Lopes, R., Beattie, W., Thomson, J., Herder, V., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-41115-3 · Cited by 71
“…many possible mechanisms whereby ACE2 could influence SARS-CoV-2 inflammatory actions: (1) ACE2 as the viral entry receptor facilitates infection 4, 6 ; (2) loss of enzymatic activity leads to a shift to a cardiovascular pro-damaging axis of the RAAS involving higher levels of Ang II followed…”
BackgroundBallesteros, M. Á., Hernández-Tejedor, A., Estella, Á., Rivera, J. J. J., de Molina, F. J. G., Camps, A. S., Vidal, P., de Haro, C., Aguilar-Alonso, E., Laguna, L. B., et al. (2020) · Medicina Intensiva · doi:10.1016/j.medin.2020.04.001 · Cited by 70
Association of vitamin D with the modulation of the disease severity in COVID-19
Mardani, R., Alamdary, A., Nasab, S. D. M., Gholami, R., Ahmadi, N., & Gholami, A. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198148 · Cited by 65
Elrashdy, F., Redwan, E. M. M. M., & Uversky, V. N. (2020) · Biomolecules · doi:10.3390/biom10091312 · Cited by 64
“This is in line with the outputs of the computational analysis showing that when all the residues favoring interaction of the CoV S protein with human ACE2 would be combined into one RBD, this RBD would bind to ACE2 with super affinity, and the corresponding spike protein would mediate viral entry into human cells wit…”
Ambient PM2.5 exposure and rapid spread of COVID-19 in the United States
Chakrabarty, R. K., Beeler, P., Liu, P., Goswami, S., Harvey, R. D., Pervez, S., van Donkelaar, A., & Martin, R. V. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.143391 · Cited by 67
“The viral entry of SARS-CoV-2 has been shown to use Angiotensin-converting enzyme 2 (ACE2) as its co-host receptor (Wan et al., 2020).”
Occurrence, fate and removal of SARS-CoV-2 in wastewater: Current knowledge and future perspectives
Saawarn, B., & Hait, S. (2020) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2020.104870 · Cited by 65
“This suggests an efficient human to human transmission [6,16,17,19,20].”
BackgroundPasini, A. M. F., Stranieri, C., Cominacini, L., & Mozzini, C. (2021) · Antioxidants · doi:10.3390/antiox10020272 · Cited by 68
Kiew, L. V., Chang, C.-Y., Huang, S., Wang, P., Heh, C.-H., Liu, C.-T., Cheng, C.-H., Lu, Y.-X., Chen, Y., Huang, Y.-X., et al. (2021) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2021.113213 · Cited by 64
Verkhivker, G. M., & Paola, L. D. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00395 · Cited by 55
Retrieval and Investigation of Data on SARS-CoV-2 and COVID-19 Using Bioinformatics Approach
Fahmi, M., Kharisma, V. D., Ansori, A. N. M., & Ito, M. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-63761-3_47 · Cited by 65
The Repurposed ACE2 Inhibitors: SARS-CoV-2 Entry Blockers of Covid-19
Ahmad, I., Pawara, R. H., Surana, S. J., & Patel, H. (2021) · Topics in Current Chemistry · doi:10.1007/s41061-021-00353-7 · Cited by 68
Souza, P. F. N., Mesquita, F. P., Amaral, J. L., Landim, P. G. C., Lima, K. R. P., Costa, M. B., Farias, I. R., Belém, M. O., Pinto, Y. O., Moreira, H. H. T., et al. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.03.058 · Cited by 67
“from the S protein from SARS-CoV-2, suggesting it may not bind to human ACE2 [53].”
Campos, M. C., Nery, T., Starke, A. C., Alves, A. C. D. B., Speck, A. E., & Aguiar, A. S. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104902 · Cited by 71
Yazdani, Z., Rafiei, A., Yazdani, M., & Valadan, R. (2020) · Infection and Drug Resistance · doi:10.2147/idr.s264573 · Cited by 67
Characterization of neutralizing antibodies from a SARS-CoV-2 infected individualPreprint
Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.12.091298 · Cited by 64
“Indeed, the S proteins of the two viruses share a high degree of amino acid sequence homology; 76% overall and 74% in RBD (Wan et al., 2020).”
BackgroundSelf-citationTouyz, R. M., Li, H., & Delles, C. (2020) · Clinical Science · doi:10.1042/cs20200363 · Cited by 63
Ismail, S., Ahmad, S., & Azam, S. S. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.113612 · Cited by 63
“This critical role of the spike protein makes it an important candidate for neutralization by antibodies, and detailed atomic level studies of the pre-fusion spike structure are important in the design and development of a vaccine [17 – 21].”
Mutational Frequencies of SARS-CoV-2 Genome during the Beginning Months of the Outbreak in USA
Kaushal, N., Gupta, Y., Goyal, M., Khaiboullina, S. F., Baranwal, M., & Verma, S. C. (2020) · Pathogens · doi:10.3390/pathogens9070565 · Cited by 61
“Most of the antibody isolates from patient blood are shown to target the S1 subunit, typically RBD domain [61,62].”
Yatoo, M. I., Hamid, Z., Parray, O. R., Wani, A. H., Haq, A. U., Saxena, A., Patel, S. K., Pathak, M., Tiwari, R., Malik, Y. S., et al. (2020) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2020.1788310 · Cited by 64
“Moreover, the external subdomain of the RBD that helps in virus and host receptor binding exhibits the highest number of amino acid variations.(11,28) Strategies that target the initial entry of virus are considered to be effective for the prevention and control of COVID-19;(26) consequently, elucidation of the mechan…”
BackgroundMethodInfluentialACE2 Protein Landscape in the Head and Neck Region: The Conundrum of SARS-CoV-2 Infection
Descamps, G., Verset, L., Trelcat, A., Hopkins, C. L., Lechien, J. R., Journé, F., & Saussez, S. (2020) · Biology · doi:10.3390/biology9080235 · Cited by 65
“Indeed, genomic analyses have recently demonstrated a homology of almost 80% between the two viruses, suggesting that they may infect human cells through the binding of the same ACE2 receptor [7,8].”
BackgroundSevere Acute Respiratory Syndrome Coronavirus 2, COVID-19, and the Renin-Angiotensin System
Sparks, M. A., South, A. M., Badley, A. D., Baker-Smith, C. M., BATLLE, D. C., Bozkurt, B., Cattaneo, R., Crowley, S. D., Dell’Italia, L. J., Ford, A. L., et al. (2020) · Hypertension · doi:10.1161/hypertensionaha.120.15948 · Cited by 62
Ghorbani, M., Brooks, B. R., & Klauda, J. B. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c05994 · Cited by 61
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Next-Generation Sequencing Reveals the Progression of COVID-19
Chen, X., Kang, Y., Luo, J., Pang, K., Xu, X. Y., Wu, J., Li, X., & Jin, S. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.632490 · Cited by 69
“Because the six RBD amino acids residues (L, F, Q, S, N, and Y, Figure 1B) on the S1 protein of Pangolin-CoV-2020 are exactly the same as those of SARS-CoV2 ((Wan et al., 2020), Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus), while Bat…”
BackgroundChen, W., Wei, J., Kundu, R. T., Adhikari, R., Liu, Z., Lee, J., Versteeg, L., Poveda, C., Keegan, B. P., Villar, M. J., et al. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129893 · Cited by 62
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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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