Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody

The newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a serious threat to human health. Currently, however, there is no specific antiviral treatment or vaccine. Considering the relatively high identity...

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Published in	Emerging microbes & infections Vol. 9; no. 1; pp. 382 - 385
Main Authors	Tian, Xiaolong, Li, Cheng, Huang, Ailing, Xia, Shuai, Lu, Sicong, Shi, Zhengli, Lu, Lu, Jiang, Shibo, Yang, Zhenlin, Wu, Yanling, Ying, Tianlei
Format	Journal Article
Language	English
Published	United States Taylor & Francis 01.01.2020 Taylor & Francis Ltd Taylor & Francis Group
Subjects	2019-nCoV ACE2 Amino Acid Sequence Antibodies, Monoclonal - immunology Antibodies, Viral - immunology Betacoronavirus - immunology Binding sites Coronavirus Infections Coronaviruses COVID-19 Cross Reactions Humans Letter Monoclonal antibodies monoclonal antibody Pneumonia, Viral Protein Structure, Tertiary Proteins RBD SARS Virus - immunology SARS-CoV SARS-CoV-2 Spike Glycoprotein, Coronavirus - immunology ACE2 2019-nCoV monoclonal antibody RBD SARS-CoV
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Abstract	The newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a serious threat to human health. Currently, however, there is no specific antiviral treatment or vaccine. Considering the relatively high identity of receptor-binding domain (RBD) in 2019-nCoV and SARS-CoV, it is urgent to assess the cross-reactivity of anti-SARS CoV antibodies with 2019-nCoV spike protein, which could have important implications for rapid development of vaccines and therapeutic antibodies against 2019-nCoV. Here, we report for the first time that a SARS-CoV-specific human monoclonal antibody, CR3022, could bind potently with 2019-nCoV RBD (KD of 6.3 nM). The epitope of CR3022 does not overlap with the ACE2 binding site within 2019-nCoV RBD. These results suggest that CR3022 may have the potential to be developed as candidate therapeutics, alone or in combination with other neutralizing antibodies, for the prevention and treatment of 2019-nCoV infections. Interestingly, some of the most potent SARS-CoV-specific neutralizing antibodies (e.g. m396, CR3014) that target the ACE2 binding site of SARS-CoV failed to bind 2019-nCoV spike protein, implying that the difference in the RBD of SARS-CoV and 2019-nCoV has a critical impact for the cross-reactivity of neutralizing antibodies, and that it is still necessary to develop novel monoclonal antibodies that could bind specifically to 2019-nCoV RBD.
AbstractList	The newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a serious threat to human health. Currently, however, there is no specific antiviral treatment or vaccine. Considering the relatively high identity of receptor-binding domain (RBD) in 2019-nCoV and SARS-CoV, it is urgent to assess the cross-reactivity of anti-SARS CoV antibodies with 2019-nCoV spike protein, which could have important implications for rapid development of vaccines and therapeutic antibodies against 2019-nCoV. Here, we report for the first time that a SARS-CoV-specific human monoclonal antibody, CR3022, could bind potently with 2019-nCoV RBD (KD of 6.3 nM). The epitope of CR3022 does not overlap with the ACE2 binding site within 2019-nCoV RBD. These results suggest that CR3022 may have the potential to be developed as candidate therapeutics, alone or in combination with other neutralizing antibodies, for the prevention and treatment of 2019-nCoV infections. Interestingly, some of the most potent SARS-CoV-specific neutralizing antibodies (e.g. m396, CR3014) that target the ACE2 binding site of SARS-CoV failed to bind 2019-nCoV spike protein, implying that the difference in the RBD of SARS-CoV and 2019-nCoV has a critical impact for the cross-reactivity of neutralizing antibodies, and that it is still necessary to develop novel monoclonal antibodies that could bind specifically to 2019-nCoV RBD. The newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a serious threat to human health. Currently, however, there is no specific antiviral treatment or vaccine. Considering the relatively high identity of receptor-binding domain (RBD) in 2019-nCoV and SARS-CoV, it is urgent to assess the cross-reactivity of anti-SARS CoV antibodies with 2019-nCoV spike protein, which could have important implications for rapid development of vaccines and therapeutic antibodies against 2019-nCoV. Here, we report for the first time that a SARS-CoV-specific human monoclonal antibody, CR3022, could bind potently with 2019-nCoV RBD (KD of 6.3 nM). The epitope of CR3022 does not overlap with the ACE2 binding site within 2019-nCoV RBD. These results suggest that CR3022 may have the potential to be developed as candidate therapeutics, alone or in combination with other neutralizing antibodies, for the prevention and treatment of 2019-nCoV infections. Interestingly, some of the most potent SARS-CoV-specific neutralizing antibodies (e.g. m396, CR3014) that target the ACE2 binding site of SARS-CoV failed to bind 2019-nCoV spike protein, implying that the difference in the RBD of SARS-CoV and 2019-nCoV has a critical impact for the cross-reactivity of neutralizing antibodies, and that it is still necessary to develop novel monoclonal antibodies that could bind specifically to 2019-nCoV RBD.The newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a serious threat to human health. Currently, however, there is no specific antiviral treatment or vaccine. Considering the relatively high identity of receptor-binding domain (RBD) in 2019-nCoV and SARS-CoV, it is urgent to assess the cross-reactivity of anti-SARS CoV antibodies with 2019-nCoV spike protein, which could have important implications for rapid development of vaccines and therapeutic antibodies against 2019-nCoV. Here, we report for the first time that a SARS-CoV-specific human monoclonal antibody, CR3022, could bind potently with 2019-nCoV RBD (KD of 6.3 nM). The epitope of CR3022 does not overlap with the ACE2 binding site within 2019-nCoV RBD. These results suggest that CR3022 may have the potential to be developed as candidate therapeutics, alone or in combination with other neutralizing antibodies, for the prevention and treatment of 2019-nCoV infections. Interestingly, some of the most potent SARS-CoV-specific neutralizing antibodies (e.g. m396, CR3014) that target the ACE2 binding site of SARS-CoV failed to bind 2019-nCoV spike protein, implying that the difference in the RBD of SARS-CoV and 2019-nCoV has a critical impact for the cross-reactivity of neutralizing antibodies, and that it is still necessary to develop novel monoclonal antibodies that could bind specifically to 2019-nCoV RBD. ABSTRACTThe newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a serious threat to human health. Currently, however, there is no specific antiviral treatment or vaccine. Considering the relatively high identity of receptor-binding domain (RBD) in 2019-nCoV and SARS-CoV, it is urgent to assess the cross-reactivity of anti-SARS CoV antibodies with 2019-nCoV spike protein, which could have important implications for rapid development of vaccines and therapeutic antibodies against 2019-nCoV. Here, we report for the first time that a SARS-CoV-specific human monoclonal antibody, CR3022, could bind potently with 2019-nCoV RBD (KD of 6.3 nM). The epitope of CR3022 does not overlap with the ACE2 binding site within 2019-nCoV RBD. These results suggest that CR3022 may have the potential to be developed as candidate therapeutics, alone or in combination with other neutralizing antibodies, for the prevention and treatment of 2019-nCoV infections. Interestingly, some of the most potent SARS-CoV-specific neutralizing antibodies (e.g. m396, CR3014) that target the ACE2 binding site of SARS-CoV failed to bind 2019-nCoV spike protein, implying that the difference in the RBD of SARS-CoV and 2019-nCoV has a critical impact for the cross-reactivity of neutralizing antibodies, and that it is still necessary to develop novel monoclonal antibodies that could bind specifically to 2019-nCoV RBD.
Author	Tian, Xiaolong Shi, Zhengli Li, Cheng Lu, Lu Huang, Ailing Xia, Shuai Yang, Zhenlin Ying, Tianlei Jiang, Shibo Wu, Yanling Lu, Sicong
Author_xml	– sequence: 1 givenname: Xiaolong surname: Tian fullname: Tian, Xiaolong organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 2 givenname: Cheng surname: Li fullname: Li, Cheng organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 3 givenname: Ailing surname: Huang fullname: Huang, Ailing organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 4 givenname: Shuai surname: Xia fullname: Xia, Shuai organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 5 givenname: Sicong surname: Lu fullname: Lu, Sicong organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 6 givenname: Zhengli orcidid: 0000-0001-8089-163X surname: Shi fullname: Shi, Zhengli organization: CAS Key Laboratory of Special Pathogens, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences – sequence: 7 givenname: Lu surname: Lu fullname: Lu, Lu organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 8 givenname: Shibo orcidid: 0000-0001-8283-7135 surname: Jiang fullname: Jiang, Shibo organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 9 givenname: Zhenlin surname: Yang fullname: Yang, Zhenlin email: yang_zhenlin@fudan.edu.cn organization: Department of Pulmonary Medicine, Zhongshan Hospital, Fudan University – sequence: 10 givenname: Yanling surname: Wu fullname: Wu, Yanling email: yanlingwu@fudan.edu.cn organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University – sequence: 11 givenname: Tianlei orcidid: 0000-0002-9597-2843 surname: Ying fullname: Ying, Tianlei email: tlying@fudan.edu.cn organization: MOE/NHC/CAMS Key Laboratory of Medical Molecular Virology, School of Basic Medical Sciences, Shanghai Medical College, Fudan University
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/32065055$$D View this record in MEDLINE/PubMed
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Snippet	The newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing a... ABSTRACTThe newly identified 2019 novel coronavirus (2019-nCoV) has caused more than 11,900 laboratory-confirmed human infections, including 259 deaths, posing...
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SubjectTerms	2019-nCoV ACE2 Amino Acid Sequence Antibodies, Monoclonal - immunology Antibodies, Viral - immunology Betacoronavirus - immunology Binding sites Coronavirus Infections Coronaviruses COVID-19 Cross Reactions Humans Letter Monoclonal antibodies monoclonal antibody Pneumonia, Viral Protein Structure, Tertiary Proteins RBD SARS Virus - immunology SARS-CoV SARS-CoV-2 Spike Glycoprotein, Coronavirus - immunology
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Title	Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody
URI	https://www.tandfonline.com/doi/abs/10.1080/22221751.2020.1729069 https://www.ncbi.nlm.nih.gov/pubmed/32065055 https://www.proquest.com/docview/2508720762 https://www.proquest.com/docview/2356593290 https://pubmed.ncbi.nlm.nih.gov/PMC7048180 https://doaj.org/article/60f7c5ac04154d338a3564ec6b669f7e
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