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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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“A 193 amino acid region on the spike protein of SARS-CoV-1 and SARS60 CoV-2 termed the receptor binding domain (RBD) was found to interact with the ACE2 receptor 61 and primarily mediates cell entry(5-10).”
COVID-19 and Diabetes Mellitus: The Link and Clinical Implications
Ugwueze, C. V., Ezeokpo, B. C., Nnolim, B. I., Agim, E. A., Anikpo, N. C., & Onyekachi, K. E. (2020) · Dubai Diabetes and Endocrinology Journal · doi:10.1159/000511354 · Cited by 63
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“Wild type mice inoculated with SARS-CoV-2 do not demonstrate viral infection.(16) While other animals demonstrate SARSCoV-2 infection, including ferrets,(17) cats,(18) cynomolgus macaques(19) and Rhesus macaques,(20-23) their utility as an experimental system is limited by practical issues related to size of the anima…”
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“An envelope-anchored SARS-CoV-2 spike (S) glycoprotein facilitates coronavirus entry into host cells [6,7].”
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“It remains highly controversial what roles ACE2 plays during the progression of COVID-19 and its complications, although it is well established that ACE2 serves as the receptor of the spike protein on SARS-CoV-2 (Wan et al., 2020).”
Animal coronaviruses and SARS‐CoV‐2
Zhang, G., Li, B., Yoo, D., Qin, T., Zhang, X., Jia, Y., & Cui, S. (2020) · Transboundary and Emerging Diseases · doi:10.1111/tbed.13791 · Cited by 56
Chowdhury, R., Boorla, V. S., & Maranas, C. D. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.09.019 · Cited by 56
Capocasale, G., Nocini, R., Faccioni, P., Donadello, D., Bertossi, D., Albanese, M., & Zotti, F. (2020) · Clinical and Experimental Dental Research · doi:10.1002/cre2.332 · Cited by 58
Mutational spectra of SARS-CoV-2 isolated from animals
Elaswad, A., Fawzy, M., Basiouni, S., & Shehata, A. A. (2020) · PeerJ · doi:10.7717/peerj.10609 · Cited by 58
“Computational models 310 and data have identified additional mutations that might further strengthen the binding affinity of 311 SARS-CoV-2 to ACE2 receptors (Wan et al. 2020).”
BackgroundHalwe, S., Kupke, A., Vanshylla, K., Liberta, F., Gruell, H., Zehner, M., Rohde, C., Krähling, V., Serra, M. G., Kreer, C., et al. (2021) · Viruses · doi:10.3390/v13081498 · Cited by 53
SARS-CoV-2 involvement in central nervous system tissue damage
Sabra, M., Kobeissy, F. H., Bizri, M., Haidar, M. A., Shakkour, Z., Reslan, M. A., Al-Haj, N., Chamoun, P., Habashy, K. J., Kaafarani, H., et al. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.327323 · Cited by 58
“Reported cross-reactivities with host proteins in severe SARSCoV-2 infections include autoimmunity against INFs type I, phospholipids, and annexin A2 (Bastard et al., 2020; Woodruff et al., 2020; Zuo et al., 2020; Wang et al., 2021; Zuniga et al., 2021).”
BackgroundMethodContribution of Syndecans to the Cellular Entry of SARS-CoV-2
Hudák, A., Letoha, A., Szilák, L., & Letoha, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105336 · Cited by 56
“Endocytic uptake of monomeric amyloid- beta peptides is clathrin- and dynamin-independent and results in selective accumulation of Abeta(1-42) compared to Abeta(1-40).”
BackgroundNew SARS-CoV-2 Infection Detected in an Italian Pet Cat by RT-qPCR from Deep Pharyngeal Swab
Musso, N., Costantino, A., Spina, S. L., Finocchiaro, A., Andronico, F., Stracquadanio, S., Liotta, L., Visalli, R., & Emmanuele, G. (2020) · Pathogens · doi:10.3390/pathogens9090746 · Cited by 55
Han, K., Blair, R. V., Iwanaga, N., Liu, F., Russell‐Lodrigue, K., Qin, Z., Midkiff, C. C., Golden, N., Doyle‐Meyers, L. A., Kabir, M. E., et al. (2020) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2020-0354oc · Cited by 57
Critical complications of COVID-19: A descriptive meta-analysis study
Vakili, K. G., Fathi, M., Sayehmiri, F., Mohamadkhani, A., Hajiesmaeili, M., Rezaei–Tavirani, M., & Pezeshgi, A. (2020) · Reviews in Cardiovascular Medicine · doi:10.31083/j.rcm.2020.03.129 · Cited by 58
“Human pathogenic coronaviruses (i.e., SARS-CoV2 and SARS-CoV) may bind to their target cells through ACE2, which is expressed by the epithelial cells of the kidney, the intestine, the blood vessels, and the lung (Fang et al., 2020; Y. Wan et al., 2020).”
BackgroundCOVID-19 Outbreak: Pathogenesis, Current Therapies, and Potentials for Future Management
Hossain, M. F., Hasana, S., Mamun, A. A., Uddin, M. S., Wahed, M. I. I., Sarker, S., Behl, T., Ullah, I., Begum, Y., Bulbul, I. J., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.563478 · Cited by 57
“The genomic sequence of COVID-19 exhibited 88% identity with bird-derived SARS-like COV (Lu R. et al., 2020; Wan et al., 2020) ensuring a link between humans and COVID-19.”
MethodVaccine design based on 16 epitopes of SARS‐CoV‐2 spike protein
He, J., Fan, H., Zhang, J., Chen, Q., Zheng, Z., Zhou, Q., Chen, D., Li, J., & Chen, J. (2020) · Journal of Medical Virology · doi:10.1002/jmv.26596 · Cited by 53
“The spike protein on the virion surface is thought to bind to the host receptor angiotensin‐converting enzyme 2 (ACE2) and plays an important role in cell adhesion and virulence similar to SARS‐CoV.(1) As the spike protein plays key roles in inducing neutralizing antibodies and protective immunity during SARS‐CoV infe…”
BackgroundTomaszewski, T., DeVries, R. S., Dong, M., Bhatia, G., Norsworthy, M. D., Zheng, X., & Caetano‐Anollés, G. (2020) · Evolutionary Bioinformatics · doi:10.1177/1176934320965149 · Cited by 57
“Ferrets, cats, pigs, orangutans, monkeys share similar critical virus-binding residues with humans, suggesting SARS-CoV-2 could infect these animals 16 .”
BackgroundResultInfluentialAwadasseid, A., Wu, Y., Tanaka, Y., & Zhang, W. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.47827 · Cited by 56
“ACE2 comprises at least five essential amino acids for binding the SARSr-CoV S protein [15].”
BackgroundPlant-Based Drugs and Vaccines for COVID-19
Mahmood, N., Nasir, S. B., & Hefferon, K. L. (2020) · Vaccines · doi:10.3390/vaccines9010015 · Cited by 55
“The receptor-binding domain (RBD) of the spike protein is the most variable portion of the CoV genome [12,18] Six amino acids in the RBD are critical for attachment to the ACE2 receptors as well as determination of host range of viruses like SARS-CoV [29].”
BackgroundÖz, M., & Lorke, D. E. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.111193 · Cited by 57
Rosenfeld, R., Noy-Porat, T., Mechaly, A., Makdasi, E., Levy, Y., Alcalay, R., Falach, R., Aftalion, M., Epstein, E., Gur, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21239-8 · Cited by 55
Insights into SARS-CoV-2 Persistence and Its Relevance
Desimmie, B. A., Raru, Y., Awadh, H., He, P., Teka, S., & Willenburg, K. S. (2021) · Viruses · doi:10.3390/v13061025 · Cited by 58
“SARS-CoV-2 tropism SARS-CoV-2 infects the target cell by binding to its cognate cell surface receptor, the ACE2 protein using the RBD of the S protein (Figure 1c) [3, 5, 9, 21, 22, 28-32].”
BackgroundMethodKarnik, M., Beeraka, N. M., Uthaiah, C. A., Nataraj, S. M., Bettadapura, A. D. S., Aliev, G., & Madhunapantula, S. V. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02399-6 · Cited by 56
“The conserved viral structure and genetic similarity of SARS-CoV-2 with SARS-CoV provide further evidence that the virus can enter into the CNS [89, 90].”
BackgroundPathogenesis of taste impairment and salivary dysfunction in COVID-19 patients
Okada, Y., Yoshimura, K., Toya, S., & Tsuchimochi, M. (2021) · Japanese Dental Science Review · doi:10.1016/j.jdsr.2021.07.001 · Cited by 56
Pokhrel, S., Bouback, T. A., Samad, A., Nur, S. M., Alam, R., Abdullah-Al-Mamun, M., Nain, Z., Imon, R. R., Talukder, M. E. K., Tareq, M. M. I., et al. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.09.146 · Cited by 57
Potential Effects of Coronaviruses on the Liver: An Update
Wang, X., Lei, J., Li, Z., & Yan, L. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.651658 · Cited by 56
“This may be explained by differences in the structure of spike proteins (S proteins) among coronaviruses (19).”
BackgroundHoque, M. N., Chaudhury, A., Akanda, M. A. M., Hossain, M. A., & Islam, T. (2020) · PeerJ · doi:10.7717/peerj.9689 · Cited by 53
“Structural and biochemical studies revealed that the SARS-CoV228 2 has an RBD which binds with high affinity to ACE2 from humans, ferrets, cats and other species 229 with high receptor homology (Andersen et al., 2020; Wan et al., 2020; Walls et al., 2020; Wrapp 230 et al., 2020; Zhou et al., 2020a).”
BackgroundUpdate on the target structures of SARS-CoV-2: A systematic review
Medhi, B., Prajapat, M., Sarma, P., Shekhar, N., Prakash, A., Avti, P., Bhattacharyya, A., Kaur, H., Kumar, S., Bansal, S., et al. (2020) · Indian Journal of Pharmacology · doi:10.4103/ijp.ijp_338_20 · Cited by 54
“[10] As compared to SARS‐CoV, a mutation (N501T) in the spike protein of SARS‐CoV‐2 confers higher‐binding affinity of SARS‐CoV2 to the ACE2 receptor.[11]”
ResultIftikhar, H., Ali, H. N., Farooq, S., Naveed, H., & Shahzad‐ul‐Hussan, S. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.103848 · Cited by 55
A Model for SARS-CoV-2 Infection with Treatment
Chatterjee, A. N., & Basir, F. A. (2020) · Computational and Mathematical Methods in Medicine · doi:10.1155/2020/1352982 · Cited by 54
“The angiotensin-converting enzyme 2 (ACE2) receptor of epithelial cells plays an important role in cellular entry [1, 7].”
BackgroundInfluentialMohammad, A., ALSHAWAF, E. M. M., Marafie, S. K., Abu‐Farha, M., Abubaker, J. A., & Al‐Mulla, F. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.10.033 · Cited by 54
Bats, pangolins, minks and other animals - villains or victims of SARS-CoV-2?
do Vale, B., Lopes, A. P., Fontes, M. D. C., Silvestre, A. M., Cardoso, L., & Coelho, A. C. (2021) · Veterinary Research Communications · doi:10.1007/s11259-021-09787-2 · Cited by 55
COVID-19 and human reproduction: A pandemic that packs a serious punch
Anifandis, G., Tempest, H. G., Oliva, R., Swanson, G., Simopoulou, M., Easley, C. A., Primig, M., Messini, C. I., Turek, P. J., Šutovský, P., et al. (2021) · Systems Biology in Reproductive Medicine · doi:10.1080/19396368.2020.1855271 · Cited by 53
Boswellic acids/Boswellia serrata extract as a potential COVID-19 therapeutic agent in the elderly
Gomaa, A. A., Mohamed, H. S., Abd-ellatief, R. B., & Gomaa, M. A. (2021) · Inflammopharmacology · doi:10.1007/s10787-021-00841-8 · Cited by 56
A mini-review on the impact of COVID 19 on vital organs
Shah, M. D., Sumeh, A. S., Sheraz, M. A., Kavitha, M. S., Maran, B. A. V., & Rodrigues, K. F. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112158 · Cited by 54
Murphy, H. L., & Ly, H. (2021) · Virulence · doi:10.1080/21505594.2021.1996519 · Cited by 54
Kidney Angiotensin in Cardiovascular Disease: Formation and Drug Targeting
Lin, H., Geurts, F., Hassler, L., BATLLE, D. C., Colafella, K. M. M., Denton, K. M., Zhuo, J. L., Li, X. C., Ramkumar, N., Koizumi, M., et al. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000236 · Cited by 58
“The importance of the location of ACE2 protein in these alveolar cells stems from it being the main cell entry receptor for severe acute respiratory syndrome coro-navirus 2 (SARS-CoV-2) (Wan et al., 2020).”
BackgroundStucki, A., Sauer, U. G., Allen, D., Kleinstreuer, N., Perron, M. M., Yozzo, K., Lowit, A., & Clippinger, A. J. (2024) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2024.105648 · Cited by 56
Targeting SARS-CoV-2 spike protein by stapled hACE2 peptides
Maas, M. N., Hintzen, J. C. J., Löffler, P. M. G., & Mecinović, J. (2021) · Chemical Communications · doi:10.1039/d0cc08387a · Cited by 52
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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