Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine
Open accessAbstract
The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.
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Immunization with recombinant RBD of SARS-CoV-2 induced high titers of neutralizing antibodies in the absence of antibody-dependent enhancement (ADE) of infection.
“Some recent studies also demonstrated that immunization with the recombinant RBD of SARS-CoV-2 induced high titers of neutralizing antibodies in the absence of antibody-dependent enhancement (ADE) of infection (Quinlan et al., 2020; Tai et al., 2020).”
From A thermostable mRNA vaccine against COVID-19 (2020) · cites this paper as Tai et al., 2020
The Results and discussion report that sera from mice immunized with SARS-CoV RBD neutralized SARS-CoV-2 pseudovirus, with a neutralizing antibody titer of 1:323. They do not report immunization with SARS-CoV-2 RBD or assess antibody-dependent enhancement (ADE), so those parts of the claim are unsupported. (LLM, conf=0.88)
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- Authors
- Tai, W., He, L., Zhang, X., Pu, J., Voronin, D., Jiang, S., Zhou, Y., & Du, L.
- Affiliations
- New York Blood Center (US)
- Beijing Institute of Microbiology and Epidemiology (CN)
- Shanghai Medical College of Fudan University (CN)
- Corresponding author
- Jiang, Shibo
- Zhou, Yusen
- Du, Lanying
- Venue
- Cellular & Molecular Immunology
- Published
- 2020-03-19
- Volume
- 17
- Issue
- 6
- Pages
- 613-620
- ISSN
- 1672-7681 (ISSN-L)
- 2042-0226
- PMC
- PMC7091888
- OpenAlex
- W3011537081
- Cited by
- 1,654
- References
- 34
- Citations by year
- 2026: 28 · 2025: 68 · 2024: 120 · 2023: 184 · 2022: 296 · 2021: 482 · 2020: 475
- FWCI
- 47.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Cellular and Molecular Immunology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Informationszentrum Lebenswissenschaften (ZB MED) (submittedVersion, cc-by)
- Funders
- U.S. Department of Health & Human Services | National Institutes of Health (R01AI137472, R01AI139092)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- SARS-CoV-2, receptor binding domain, spike protein, ACE2 receptor, viral attachment inhibition, entry inhibitors, vaccine development, cross-reactive antibodies, SARS-CoV, COVID-19 pandemic, neutralizing antibodies, receptor binding affinity
- MeSH terms
- Betacoronavirus, COVID-19, SARS-CoV-2, COVID-19 Vaccines, Amino Acid Sequence, Animals, Antibodies, Viral, Binding Sites, Chiroptera, Cross Reactions, Humans, Pneumonia, Viral, Protein Binding, Viral Vaccines, Sequence Alignment, Coronavirus Infections, Receptor, Angiotensin, Type 2, Severe acute respiratory syndrome-related coronavirus, Mice, Virus Internalization, HEK293 Cells, Pandemics, Spike Glycoprotein, Coronavirus
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