Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine
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...
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| Veröffentlicht in: | Cellular & molecular immunology Jg. 17; H. 6; S. 613 - 620 |
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| Hauptverfasser: | , , , , , , , |
| Format: | Journal Article |
| Sprache: | Englisch |
| Veröffentlicht: |
China
Nature Publishing Group
01.06.2020
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| ISSN: | 1672-7681, 2042-0226, 2042-0226 |
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| 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. |
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| AbstractList | 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. 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.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. |
| Author | Du, Lanying Pu, Jing Zhou, Yusen Voronin, Denis Tai, Wanbo Jiang, Shibo He, Lei Zhang, Xiujuan |
| Author_xml | – sequence: 1 givenname: Wanbo surname: Tai fullname: Tai, Wanbo organization: Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA – sequence: 2 givenname: Lei surname: He fullname: He, Lei organization: Beijing Institute of Microbiology and Epidemiology, Beijing, China – sequence: 3 givenname: Xiujuan surname: Zhang fullname: Zhang, Xiujuan organization: Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA – sequence: 4 givenname: Jing surname: Pu fullname: Pu, Jing organization: Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China – sequence: 5 givenname: Denis orcidid: 0000-0003-2652-0787 surname: Voronin fullname: Voronin, Denis organization: Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA – sequence: 6 givenname: Shibo surname: Jiang fullname: Jiang, Shibo email: sjiang@nybc.org, sjiang@nybc.org organization: Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China. sjiang@nybc.org – sequence: 7 givenname: Yusen surname: Zhou fullname: Zhou, Yusen email: yszhou@bmi.ac.cn organization: Beijing Institute of Microbiology and Epidemiology, Beijing, China. yszhou@bmi.ac.cn – sequence: 8 givenname: Lanying surname: Du fullname: Du, Lanying email: ldu@nybc.org organization: Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. ldu@nybc.org |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32203189$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | ACE2 Amino Acid Sequence Angiotensin Angiotensin-converting enzyme 2 Animals Antibodies Antibodies, Viral - immunology Antisera Betacoronavirus - immunology Betacoronavirus - metabolism Binding Sites Chiroptera Coronaviridae Coronavirus Infections - immunology Coronavirus Infections - metabolism Coronavirus Infections - prevention & control Coronavirus Infections - therapy Coronavirus Infections - virology Coronaviruses COVID-19 COVID-19 Vaccines Cross Reactions HEK293 Cells Humans Infections Mice Pandemics Peptidyl-dipeptidase A Pneumonia, Viral - immunology Pneumonia, Viral - metabolism Pneumonia, Viral - therapy Pneumonia, Viral - virology Protein Binding Proteins Public health Receptor, Angiotensin, Type 2 - metabolism SARS Virus - immunology SARS Virus - metabolism SARS-CoV-2 Sequence Alignment Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - metabolism Vaccines Viral Vaccines - immunology Viral Vaccines - metabolism Virus attachment Virus Internalization |
| Title | Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine |
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