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Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine.
Cell Mol Immunol. 2020 06; 17(6):613-620.CM

Abstract

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.

Authors+Show Affiliations

Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.Beijing Institute of Microbiology and Epidemiology, Beijing, China.Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China.Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. sjiang@nybc.org. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China. sjiang@nybc.org.Beijing Institute of Microbiology and Epidemiology, Beijing, China. yszhou@bmi.ac.cn.Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. ldu@nybc.org.

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

32203189

Citation

Tai, Wanbo, et al. "Characterization of the Receptor-binding Domain (RBD) of 2019 Novel Coronavirus: Implication for Development of RBD Protein as a Viral Attachment Inhibitor and Vaccine." Cellular & Molecular Immunology, vol. 17, no. 6, 2020, pp. 613-620.
Tai W, He L, Zhang X, et al. Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine. Cell Mol Immunol. 2020;17(6):613-620.
Tai, W., He, L., Zhang, X., Pu, J., Voronin, D., Jiang, S., Zhou, Y., & Du, L. (2020). Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine. Cellular & Molecular Immunology, 17(6), 613-620. https://doi.org/10.1038/s41423-020-0400-4
Tai W, et al. Characterization of the Receptor-binding Domain (RBD) of 2019 Novel Coronavirus: Implication for Development of RBD Protein as a Viral Attachment Inhibitor and Vaccine. Cell Mol Immunol. 2020;17(6):613-620. PubMed PMID: 32203189.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine. AU - Tai,Wanbo, AU - He,Lei, AU - Zhang,Xiujuan, AU - Pu,Jing, AU - Voronin,Denis, AU - Jiang,Shibo, AU - Zhou,Yusen, AU - Du,Lanying, Y1 - 2020/03/19/ PY - 2020/03/03/received PY - 2020/03/06/accepted PY - 2020/3/24/pubmed PY - 2020/6/17/medline PY - 2020/3/24/entrez KW - 2019 novel coronavirus KW - SARS-CoV-2 KW - cross-neutralization KW - receptor-binding domain KW - spike protein KW - viral inhibitor SP - 613 EP - 620 JF - Cellular & molecular immunology JO - Cell Mol Immunol VL - 17 IS - 6 N2 - 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. SN - 2042-0226 UR - https://www.unboundmedicine.com/medline/citation/32203189/Characterization_of_the_receptor_binding_domain__RBD__of_2019_novel_coronavirus:_implication_for_development_of_RBD_protein_as_a_viral_attachment_inhibitor_and_vaccine_ L2 - http://dx.doi.org/10.1038/s41423-020-0400-4 DB - PRIME DP - Unbound Medicine ER -