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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The receptor-binding domain directly contacts ACE-2 and contributes to host-cell attachment.
“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]
The Introduction (page unavailable) states that the SARS-CoV RBD has a core and an RBM that binds ACE2, and links RBD–ACE2 affinity to initial host-cell attachment. The Results model ACE2 recognition by the 2019-nCoV RBD. The cited sentence’s specific RBM range of amino acids 437–508 is not established in the passages from our copy. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe RBD contains a core structure and a variable receptor-binding motif (RBM; residues 437-508) that interacts with and attaches to the host ACE-2 receptor.
“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]
The Introduction (page not provided) says the SARS-CoV RBD has a core structure and an RBM that binds ACE2; the Results discuss ACE2-interacting residues in the 2019-nCoV RBM. Our copy does not give the claimed RBM boundaries of residues 437–508, so it does not support that specific range. (LLM, conf=0.86)
Experimental — accuracy not yet measured
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Coronavirus disease 2019 (COVID-19): A literature review
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“9 It is well-known that viral mutations occur during transmission and spreading.”
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COVID-19 Vaccine: A comprehensive status report
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BackgroundRelationship Between the ABO Blood Group and the Coronavirus Disease 2019 (COVID-19) Susceptibility
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Genomic characterization of a novel SARS-CoV-2
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“This area of ORF1ab is the most important factor among coronaviruses (Wan et al., 2020).”
BackgroundPathogenesis of COVID-19 from a cell biology perspective
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COVID-19 with Different Severities: A Multicenter Study of Clinical Features
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“SARS-CoV-2 has a receptor-binding domain structure similar to that of SARS-CoV, as shown by homology modeling (1).”
BackgroundInfluentialEnteric involvement of coronaviruses: is faecal–oral transmission of SARS-CoV-2 possible?
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Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
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Neutralizing monoclonal antibodies for treatment of COVID-19
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Angiotensin receptor blockers as tentative SARS‐CoV‐2 therapeutics
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“A number of naturally selected mutations in the RBM have been shown to affect infectivity, human-to-human transmission, pathogenesis and immune escape [2].”
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COVID-19: A promising cure for the global panic
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“The distinguishing factor is probably the nucleotide changes in the spike (S) protein and its receptor-binding domain (RBD) (Kannan et al., 2020; Coutard et al., 2020;Wan et al., 2020).”
BackgroundEngineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2
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“When ACE2 from species in our study were compared with results of other studies there were many consistencies, such as the low risk for rodents, but some predictions differ, such as the relatively high risk predicted by others for SARS-CoV-2 S binding in pangolin and horse (39), civet (40), Chinese rufous horseshoe ba…”
mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
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The Natural History, Pathobiology, and Clinical Manifestations of SARS-CoV-2 Infections
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“The virus was quickly identified as a coronavirus sharing genomic homology with SARS-CoV-1 (Lu et al. 2020a; Wan et al. 2020).”
BackgroundThe signal pathways and treatment of cytokine storm in COVID-19
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Immunity, endothelial injury and complement-induced coagulopathy in COVID-19
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“Moreover, the entry of SARS-CoV-2 into human host cells has been found to rely on the same receptor as SARS-CoV: the surface angiotensin-converting enzyme 2 (ACE2), which is expressed in the type II surfactant-secreting alveolar cells of the lungs.(8,9) Consistently, despite amino acid variations at specific key resid…”
BackgroundAn Update on Current Therapeutic Drugs Treating COVID-19
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“It is speculated that SARS-CoVand SARS-CoV-2 bind to human cells via interaction with ACE2 receptors [118, 119] .”
BackgroundDiarrhea During COVID-19 Infection: Pathogenesis, Epidemiology, Prevention, and Management
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“Structural studies 17 showed that the new SARS-CoV-2 not only binds ACE2, but its binding affinity for human ACE2 is significantly stronger (10-20 times more) 18 than its 2003 SARS-CoV predecessor.”
The Effects of Type 2 Diabetes Mellitus on Organ Metabolism and the Immune System
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Acute SARS-CoV-2 Infection Impairs Dendritic Cell and T Cell Responses
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“…and SARS-CoV use the same cellular entry receptor angiotensinconverting enzyme 2 (ACE2) to initiate infection, despite that only 40% amino acids are identical in the receptor binding domain (RBD) external subdomain (Chan et al., 2020; Lan et al., 2020; Wan et al., 2020; Zhou et al., 2020).”
The N501Y spike substitution enhances SARS-CoV-2 infection and transmission
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Bat-borne virus diversity, spillover and emergence
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The laboratory tests and host immunity of COVID-19 patients with different severity of illness
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“The current studies focus on the genome sequences (1, 8), epidemiology and outbreak investigation (9, 10), detection methods (11, 12), receptor recognition (13), and drug treatment of SARS-CoV-2 (14).”
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“In contrast, RaTG13 (Figure 2B), pangolin/MP789/2019 (Figure 2C), and pangolin/P5L/2017 (Figure 2D) did not have the deletions, and had similar conformations at their external domains, indicating that they may also use ACE2 as cell receptor, although with the exception of pangolin/MP789/2019 (see below), all exhibited…”
InfluentialCOVID-19: Disease, management, treatment, and social impact
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“It depends on the age, health and clinical conditions of the patients (Wan et al., 2020).”
BackgroundA systematic review of SARS-CoV-2 vaccine candidates
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Severe Acute Respiratory Syndrome Coronavirus 2 from Patient with Coronavirus Disease, United States
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Impaired immune cell cytotoxicity in severe COVID-19 is IL-6 dependent
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“ACE2 is expressed in the respiratory tract, by mucosal epithelial cells, lung alveolar type 2 pneumocytes, and arterial and venous endothelial cells but also in other tissues, including the gastrointestinal tract, accounting for the mild enteritis that sometimes is present in patients with COVID-19 (15, 16).”
BackgroundCOVID-19: The Inflammation Link and the Role of Nutrition in Potential Mitigation
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The molecular virology of coronaviruses
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“Comparing the SARS-CoV-2 S protein sequence with that of closely related SARS-CoV–like viruses revealed that almost all the residues important for ACE2 engagement are not conserved in SARS-CoV-2 (32), although the SARS-CoV-2 S RBD has a 10–20-fold higher binding affinity to ACE2 than SARS-CoV S RBD (33).”
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“In addition, SARS-CoV-2 does not readily infect wild-type mice because of incompatibilities between the virus spike and the murine ACE2 ortholog, which serves as the SARS-CoV-2 entry receptor (Wan et al., 2020).”
BackgroundSelf-citationA comprehensive review of COVID-19 characteristics
Esakandari, H., Nabi‐Afjadi, M., Afjadi, J. F., Farahmandian, N., Miresmaeili, S. M., & Bahreini, E. (2020) · Biological Procedures Online · doi:10.1186/s12575-020-00128-2 · Cited by 511 · see citing works
“cluding lung, intestine, kidney, and blood vessels [25].”
Background
- 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 · 2019: 5 · 2018: 2 · 2012: 1
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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