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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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“3c).(17) Interestingly, after 9 amino acid residues were mutated in the SARS-CoV-2 to SARS-CoV (L455/ Y442, F456/L443, S459/G46, Q474/S461, A475/P462, F486/L472, F490/W476, Q493/N479 and P499/T485), their binding affinity for hACE2 was abolished, in contrast to that of the WT viruses (Fig.”
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“Six RBD amino acids (L455, F486, Q493, S494, N501 and Y505) are involved in the binding to ACE2 receptors [24], and five of these six residues differ between SARS-CoV and SARS-CoV-2 [25] (Figures 1a and 1b).”
Immune response in COVID-19: A review
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“Although SARSCoV and SARS-CoV-2 share extensive amino acid sequence in the RBD (74%), and both viruses utilize human ACE2 for entry, the amino acid identity in the receptor binding motif is only 50% (Wan et al., 2020).”
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“Early indications suggested that SARS-CoV-2, much like SARS-CoV-1, infects host cells by binding to the angiotensinconverting enzyme 2 (ACE2), a receptor that is expressed in many animal species, although notably not in mice or rats (4).”
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Recapitulation of SARS-CoV-2 infection and cholangiocyte damage with human liver ductal organoids
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“The key AAs in hACE2 for interacting with RBM are K31, E35, D38,M82 and K353 [7,15].”
InfluentialChronic obstructive pulmonary disease is associated with severe coronavirus disease 2019 (COVID-19)
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Detectable 2019-nCoV viral RNA in blood is a strong indicator for the further clinical severity
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“A recent study revealed that SARS-CoV2 also uses the cell entry receptor, e951 angiotensin-converting enzyme 2 (ACE2), similar to SARS-CoV (Wan et al., 2020; Zhou et al., 2020).”
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Aghagoli, G., Gallo Marin, B., Katchur, N. J., Chaves-Sell, F., Asaad, W. F., & Murphy, S. A. (2021) · Neurocritical Care · doi:10.1007/s12028-020-01049-4 · Cited by 357
“Both SARS-CoV and SARS-CoV-2 enter host cells through ACE2 receptors, but phylogenetic data and atomic-level resolution virus–receptor complex analyses suggest that the novel coronavirus may recognize human ACE2 more efficiently [66, 67].”
BackgroundCT Imaging and Differential Diagnosis of COVID-19
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Hypolipidemia is associated with the severity of COVID-19
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Structural variations in human ACE2 may influence its binding with SARS‐CoV‐2 spike protein
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“The virus binds to the ACE2 receptor and enters the alveolar epithelial cells [5], which induces the cells to release inflammatory factors and activate the abundant macrophages in the alveolar tissue; then macrophages releases the inducing factors and chemokines, which recruit a large number of mononuclear immune cell…”
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“Both SARS-CoV-2 and SARS-CoV-1 use angiotensin converting enzyme 2 (ACE2) as an entry receptor in humans, via binding of their outer surface spike S protein [8, 9].”
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COVID-19 and the Chemical Senses: Supporting Players Take Center Stage
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Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy
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Detection technologies and recent developments in the diagnosis of COVID-19 infection
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“The routine clinical diagnosis of COVID-19 is primarily based on epidemiological history, clinical manifestations, and confirmed by a variety of laboratory detectionmethods, including computed tomography (CT) scan, nucleic acid amplification test amplification test (NAAT), and serological techniques (Corman et al. 202…”
BackgroundMethodInfluentialRacial Disparities-Associated COVID-19 Mortality among Minority Populations in the US
Alcendor, D. J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9082442 · Cited by 348
“However, it is known that SARS-CoV-2 binds to the ACE2 receptor, mainly in the lung, to enter cells [45,46].”
BackgroundNegative Nasopharyngeal and Oropharyngeal Swabs Do Not Rule Out COVID-19
Winichakoon, P., Chaiwarith, R., Liwsrisakun, C., Salee, P., Goonna, A., Limsukon, A., & Kaewpoowat, Q. (2020) · Journal of Clinical Microbiology · doi:10.1128/jcm.00297-20 · Cited by 327
Zhang, X., Cai, H. Q., Hu, J., Lian, J., Gu, J., Zhang, S., Ye, C., Lu, Y., Jin, C., Yu, G., et al. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.03.040 · Cited by 324
“One possible explanation is that SARS-CoV-2 can bind to ACE2 in the intestinal tract (Hao Zhang et al., 2020; Wan et al., 2020) while H1N1 binds to Saα2, 3Gal receptor (Riquelme et al., 2009); however, the specific mechanism is not clear at present.”
BackgroundHuston, N. C., Wan, H., Strine, M. S., Tavares, R. D. C. A., Wilen, C. B., & Pyle, A. M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.041 · Cited by 311
“With most research efforts focusing on viral proteins (Lan et al., 2020a; Yin et al., 2020; Wan et al., 2020), little is known about the viral RNA genome, especially its structural content.”
Wang, Y., Liu, M., & Gao, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008209117 · Cited by 307
“It is interesting to note that the Leu472s→Phe mutation has been identified previously in a set of five amino acid variations of the original SARS virus, engineered to produce a “superaffinity” binder for ACE2 (21).”
BackgroundACE2: Evidence of role as entry receptor for SARS-CoV-2 and implications in comorbidities
Cuervo, N. Z., & Grandvaux, N. (2020) · eLife · doi:10.7554/elife.61390 · Cited by 313
“This structure also demonstrated the role of F486 and N501, which were predicted in silico, and of K417 in the interaction with ACE2 (Wan et al., 2020).”
BackgroundInfluentialPerico, L., Benigni, A., & Remuzzi, G. (2020) · The Nephron journals/Nephron journals · doi:10.1159/000507305 · Cited by 308
Covid‐19 and diabetes mellitus: unveiling the interaction of two pandemics
Maddaloni, E., & Buzzetti, R. (2020) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.3321 · Cited by 309
Zhang, H., Li, H., Lyu, J., Li, W., Li, W., Wu, G., Lyu, J., & Dai, Z.-M. (2020) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2020.04.027 · Cited by 305
“The 2019- nCoV has the same cell entry receptor as the SARS-CoV, the angiotensin converting enzyme 2 (ACE2), which regulates the cross-species and human-to-human transmissions of the SARSCoV (Xu et al., 2020; Wan et al., 2020; Zhou et al., 2020; Letko and Munster, 2020).”
BackgroundGenotyping coronavirus SARS-CoV-2: methods and implications
Yin, C. (2020) · Genomics · doi:10.1016/j.ygeno.2020.04.016 · Cited by 302
“Spike protein S1 attaches the virion to the cell membrane by interacting with host receptor ACE2, initiating the infection [18,19].”
Potential intestinal infection and faecal–oral transmission of SARS-CoV-2
Guo, M., Tao, W., Flavell, R. A., & Zhu, S. (2021) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-021-00416-6 · Cited by 314
Human ACE2 receptor polymorphisms and altered susceptibility to SARS-CoV-2
Suryamohan, K., Diwanji, D. C., Stawiski, E. W., Gupta, R. K., Miersch, S., Liu, J., Chen, C., Jiang, Y.-P., Fellouse, F. A., Sathirapongsasuti, J. F., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02030-3 · Cited by 306
On the origin and evolution of SARS-CoV-2
Singh, D., & Yi, S. V. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00604-z · Cited by 281
Detection of SARS-CoV-2 in Human Retinal Biopsies of Deceased COVID-19 Patients
Casagrande, M. K., Fitzek, A., Püschel, K., Aleshcheva, G., Schultheiß, H., Berneking, L., Spitzer, M. S., & Schultheiß, M. (2020) · Ocular Immunology and Inflammation · doi:10.1080/09273948.2020.1770301 · Cited by 295
“Recent studies have shown that SARS-CoV-2 also uses ACE2 as its viral entering receptor.(4,17) The ACE2 receptor was first discovered in the year 2000(18,19) and gained wide public notice during the first SARS-CoV epidemic 2002/2003.”
BackgroundAn aberrant STAT pathway is central to COVID-19
Matsuyama, T., Kubli, S. P., Yoshinaga, S. K., Pfeffer, K., & Mak, T. W. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00633-7 · Cited by 295
A systematic review of neurological symptoms and complications of COVID-19
Chen, X., Laurent, S. A., Onur, O. A., Kleineberg, N. N., Fink, G. R., Schweitzer, F., & Warnke, C. (2020) · Journal of Neurology · doi:10.1007/s00415-020-10067-3 · Cited by 314
“The SARS-CoV-2 spike (S) protein can bind to the host cellular angiotensin-converting enzyme 2 (ACE-2) receptor, which is of relevance to cell tropism [3, 4].”
BackgroundCalisher, C. H., Carroll, D., Colwell, R. R., Corley, R. B., Daszak, P., Drosten, C., Enjuanes, L., Farrar, J., Field, H. E., Golding, J., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30418-9 · Cited by 300
COVID-19 pandemic: Insights into structure, function, and hACE2 receptor recognition by SARS-CoV-2
Mittal, A., Manjunath, K., Ranjan, R. K., Kaushik, S., Kumar, S., & Verma, V. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008762 · Cited by 304
“Specifically, decade-long structural studies on the S proteins of SARS-CoVs have designated 6 key residues (Y442, L472, N479, D480, T487, and Y491 for SARS-CoV) [67] in the RBDs that are critical for the host-cell ACE2 receptor binding, as well as for playing important roles in the cross-species transmission.”
BackgroundComorbidities in SARS-CoV-2 Patients: a Systematic Review and Meta-Analysis
Ng, W. H., Tipih, T., Aminake, M. N., Vermeulen, J., Goedhals, D., Sempa, J. B., Burt, F. J., Taylor, A., & Mahalingam, S. (2021) · mBio · doi:10.1128/mbio.03647-20 · Cited by 296
“ACE2 receptor is commonly identified in the epithelial cells of the lungs, intestine, kidney, and blood vessel (79).”
BackgroundAl-Karmalawy, A. A., Dahab, M. A., Metwaly, A. M., Elhady, S. S., Elkaeed, E. B., Eissa, I. H., & Darwish, K. M. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.661230 · Cited by 294
“The S protein-hACE2 complex is internalized by endocytosis and facilitates the entry of each virion into the cytoplasm (Wan et al., 2020).”
BackgroundCOVID-19 and Cancer: a Comprehensive Review
Gosain, R., Abdou, Y. G., Singh, A., Rana, N. K., Puzanov, I. J., & Ernstoff, M. S. (2020) · Current Oncology Reports · doi:10.1007/s11912-020-00934-7 · Cited by 295
“Based on the sequencing and evolutionary data, bats are the proposed reservoir for the coronavirus [2, 3] .”
BackgroundCurrent epidemiological and clinical features of COVID-19; a global perspective from China
Tu, H., Tu, S., Gao, S., Shao, A., & Sheng, J. (2020) · Journal of Infection · doi:10.1016/j.jinf.2020.04.011 · Cited by 293
Body Localization of ACE-2: On the Trail of the Keyhole of SARS-CoV-2
Salamanna, F., Maglio, M., Landini, M. P., & Fini, M. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.594495 · Cited by 298
Yeung, M. L., Teng, J. L. L., Jia, L., Zhang, C., Huang, C., Cai, J., Zhou, R., Chan, K., Zhao, H., Zhu, L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.053 · Cited by 276
“ACE2, being a receptor for SARS-CoV-2 (Wan et al., 2020), is also known to serve as one of the key regulators controlling the release of vasopressin into the plasma for the maintenance of blood pressure homeostasis via the RAS”
COVID-19 vaccine: A recent update in pipeline vaccines, their design and development strategies
Rawat, K., Kumari, P., & Saha, L. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173751 · Cited by 282
The outbreak of SARS-CoV-2 pneumonia calls for viral vaccines
Shang, W., Yang, Y., Rao, Y., & Rao, X. (2020) · npj Vaccines · doi:10.1038/s41541-020-0170-0 · Cited by 275
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Current status of probiotic and related health benefits
Das, T. K., Pradhan, S., Chakrabarti, S., Mondal, K. C., & Ghosh, K. (2022) · Applied Food Research · doi:10.1016/j.afres.2022.100185 · Cited by 308
Propolis and its potential against SARS-CoV-2 infection mechanisms and COVID-19 disease
Berretta, A. A., Silveira, M. A. D., Capcha, J. M. C., & JONG, D. D. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110622 · Cited by 288
“Infection by SARS-CoV-2, the virus that causes COVID-19, is characterized by binding between viral spike proteins and angiotensinconverting enzyme 2 (ACE2) [16].”
InfluentialCOVID-19 outbreak: history, mechanism, transmission, structural studies and therapeutics
Yesudhas, D., Srivastava, A., & Gromiha, M. M. (2020) · Infection · doi:10.1007/s15010-020-01516-2 · Cited by 329
“Until the first identification of human coronaviruses 229E and OC43, in the late 1960s, coronavirus infections were witnessed as harmless for humans [14, 15].”
BackgroundInfluentialCherian, S., Potdar, V., Jadhav, S., Yadav, P., Gupta, N., Das, M., Rakshit, P., Singh, S., Abraham, P., Panda, S., et al. (2021) · doi:10.1101/2021.04.22.440932 · Cited by 730
Tan, W., & Aboulhosn, J. (2020) · International Journal of Cardiology · doi:10.1016/j.ijcard.2020.03.063 · Cited by 279
Rao, S., Lau, A., & So, H. (2020) · Diabetes Care · doi:10.2337/dc20-0643 · Cited by 277
Perspectives on therapeutic neutralizing antibodies against the Novel Coronavirus SARS-CoV-2
Zhou, G., & Zhao, Q. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.45123 · Cited by 266
Wu, J., Shi, Y., Pan, X., Wu, S., Hou, R., Zhang, Y., Zhong, T., Tang, H., Du, W., Wang, L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108761 · Cited by 278
The role of IL-6 and other mediators in the cytokine storm associated with SARS-CoV-2 infection
Copaescu, A. M., Smibert, O. C., Gibson, A., Phillips, E. J., & Trubiano, J. A. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.07.001 · Cited by 263
Mody, V. V., Ho, J., Wills, S., Mawri, A., Lawson, L., Ebert, M. C. C. J. C., Fortin, G. M., Rayalam, S., & Taval, S. (2021) · Communications Biology · doi:10.1038/s42003-020-01577-x · Cited by 272
Susceptibility of White-Tailed Deer (Odocoileus virginianus) to SARS-CoV-2
Palmer, M. V., Martins, M., Falkenberg, S. M., Buckley, A., Caserta, L. C., Mitchell, P. K., Cassmann, E. D., Rollins, A., Zylich, N. C., Renshaw, R. W., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00083-21 · Cited by 257
“85 The SARS-CoV-2 S protein binds host cells through the angiotensin-converting enzyme 2 86 (ACE2) protein receptor (17).”
BackgroundUpdated Approaches against SARS-CoV-2
Li, H., Zhou, Y., Zhang, M., Wang, H., Zhao, Q., & Liu, J. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00483-20 · Cited by 263
SARS-CoV-2 Productively Infects Human Gut EnterocytesPreprint
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Cui, H., Gao, Z., Liu, M., Liu, M., Mo, S., Mkandawire, W., Narykov, O., Sun, M., & Korkin, D. (2020) · Viruses · doi:10.3390/v12040360 · Cited by 257
“Surprisingly, it was recently established that the interaction was preserved [76], in spite of a number of mutations in the receptor binding site of wS.”
BackgroundThe 2019 novel coronavirus disease (COVID-19) pandemic
Chatterjee, P., Nagi, N., Agarwal, A., Das, B., Banerjee, S., Sarkar, S., Gupta, N., & Gangakhedkar, R. (2020) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_519_20 · Cited by 265
Datta, P. K., Liu, F., Fischer, T., Rappaport, J., & Qin, X. (2020) · Theranostics · doi:10.7150/thno.48076 · Cited by 262
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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