Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections

The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two g...

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Published inNature communications Vol. 12; no. 1; pp. 264 - 16
Main Authors Zhang, Chao, Wang, Yifan, Zhu, Yuanfei, Liu, Caixuan, Gu, Chenjian, Xu, Shiqi, Wang, Yalei, Zhou, Yu, Wang, Yanxing, Han, Wenyu, Hong, Xiaoyu, Yang, Yong, Zhang, Xueyang, Wang, Tingfeng, Xu, Cong, Hong, Qin, Wang, Shutian, Zhao, Qiaoyu, Qiao, Weihua, Zang, Jinkai, Kong, Liangliang, Wang, Fangfang, Wang, Haikun, Qu, Di, Lavillette, Dimitri, Tang, Hong, Deng, Qiang, Xie, Youhua, Cong, Yao, Huang, Zhong
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 11.01.2021
Nature Publishing Group
Nature Portfolio
Subjects
101/28
631/326
631/535
82/1
ACE2
Allosteric properties
Angiotensin-converting enzyme 2
Animals
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - pharmacology
Antibodies, Monoclonal - therapeutic use
Antibodies, Neutralizing - immunology
Antibodies, Viral - chemistry
Antibodies, Viral - immunology
Antibodies, Viral - pharmacology
Antibodies, Viral - therapeutic use
Antigens
Antiviral agents
Antiviral drugs
Binding
Coronaviridae
Coronaviruses
COVID-19
COVID-19 - drug therapy
Cryoelectron Microscopy
Drug development
Emerging diseases
Epitope Mapping
Epitopes
Female
Human health and pathology
Humanities and Social Sciences
Immunology
Immunotherapy
Infectious diseases
Life Sciences
Mice
Mice, Inbred BALB C
Microbiology and Parasitology
Models, Molecular
Monoclonal antibodies
multidisciplinary
Neutralizing
Pandemics
Prophylaxis
Protein Binding - drug effects
Protein Conformation
Proteins
Respiratory diseases
SARS-CoV-2 - drug effects
Science
Science (multidisciplinary)
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - immunology
Spike protein
Trimers
Viral diseases
Virology
Online AccessGet full text

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Abstract The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen–antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections. Here, the authors identify and characterize two mouse-derived monoclonal antibodies against SARS-CoV-2 spike protein that target different epitopes in RBD and block the interaction S/ACE2 and show that a formulated humanized version cocktail exhibits prophylaxis and therapeutic antiviral effects in an hACE2-adenovector expressed mouse model.
AbstractList The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen–antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections.Here, the authors identify and characterize two mouse-derived monoclonal antibodies against SARS-CoV-2 spike protein that target different epitopes in RBD and block the interaction S/ACE2 and show that a formulated humanized version cocktail exhibits prophylaxis and therapeutic antiviral effects in an hACE2-adenovector expressed mouse model.
The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen–antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections. Here, the authors identify and characterize two mouse-derived monoclonal antibodies against SARS-CoV-2 spike protein that target different epitopes in RBD and block the interaction S/ACE2 and show that a formulated humanized version cocktail exhibits prophylaxis and therapeutic antiviral effects in an hACE2-adenovector expressed mouse model.
The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen–antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections.
The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen-antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections.The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies against SARS-CoV-2 are an option for drug development for treating COVID-19. Here, we report the identification and characterization of two groups of mouse neutralizing monoclonal antibodies (MAbs) targeting the receptor-binding domain (RBD) on the SARS-CoV-2 spike (S) protein. MAbs 2H2 and 3C1, representing the two antibody groups, respectively, bind distinct epitopes and are compatible in formulating a noncompeting antibody cocktail. A humanized version of the 2H2/3C1 cocktail is found to potently neutralize authentic SARS-CoV-2 infection in vitro with half inhibitory concentration (IC50) of 12 ng/mL and effectively treat SARS-CoV-2-infected mice even when administered at as late as 24 h post-infection. We determine an ensemble of cryo-EM structures of 2H2 or 3C1 Fab in complex with the S trimer up to 3.8 Å resolution, revealing the conformational space of the antigen-antibody complexes and MAb-triggered stepwise allosteric rearrangements of the S trimer, delineating a previously uncharacterized dynamic process of coordinated binding of neutralizing antibodies to the trimeric S protein. Our findings provide important information for the development of MAb-based drugs for preventing and treating SARS-CoV-2 infections.
Here, the authors identify and characterize two mouse-derived monoclonal antibodies against SARS-CoV-2 spike protein that target different epitopes in RBD and block the interaction S/ACE2 and show that a formulated humanized version cocktail exhibits prophylaxis and therapeutic antiviral effects in an hACE2-adenovector expressed mouse model.
ArticleNumber 264
Author Qiao, Weihua
Zhou, Yu
Zang, Jinkai
Xu, Cong
Zhu, Yuanfei
Gu, Chenjian
Wang, Haikun
Cong, Yao
Xie, Youhua
Deng, Qiang
Huang, Zhong
Wang, Yanxing
Wang, Shutian
Yang, Yong
Qu, Di
Liu, Caixuan
Xu, Shiqi
Hong, Qin
Han, Wenyu
Wang, Tingfeng
Zhang, Chao
Wang, Fangfang
Zhao, Qiaoyu
Kong, Liangliang
Zhang, Xueyang
Lavillette, Dimitri
Hong, Xiaoyu
Wang, Yifan
Tang, Hong
Wang, Yalei
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/33431876$$D View this record in MEDLINE/PubMed
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SSID ssj0000391844
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Snippet The ongoing pandemic of coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Neutralizing antibodies...
Here, the authors identify and characterize two mouse-derived monoclonal antibodies against SARS-CoV-2 spike protein that target different epitopes in RBD and...
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StartPage 264
SubjectTerms 101/28
631/326
631/535
82/1
ACE2
Allosteric properties
Angiotensin-converting enzyme 2
Animals
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - immunology
Antibodies, Monoclonal - pharmacology
Antibodies, Monoclonal - therapeutic use
Antibodies, Neutralizing - immunology
Antibodies, Viral - chemistry
Antibodies, Viral - immunology
Antibodies, Viral - pharmacology
Antibodies, Viral - therapeutic use
Antigens
Antiviral agents
Antiviral drugs
Binding
Coronaviridae
Coronaviruses
COVID-19
COVID-19 - drug therapy
Cryoelectron Microscopy
Drug development
Emerging diseases
Epitope Mapping
Epitopes
Female
Human health and pathology
Humanities and Social Sciences
Immunology
Immunotherapy
Infectious diseases
Life Sciences
Mice
Mice, Inbred BALB C
Microbiology and Parasitology
Models, Molecular
Monoclonal antibodies
multidisciplinary
Neutralizing
Pandemics
Prophylaxis
Protein Binding - drug effects
Protein Conformation
Proteins
Respiratory diseases
SARS-CoV-2 - drug effects
Science
Science (multidisciplinary)
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - immunology
Spike protein
Trimers
Viral diseases
Virology
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Title Development and structural basis of a two-MAb cocktail for treating SARS-CoV-2 infections
URI https://link.springer.com/article/10.1038/s41467-020-20465-w
https://www.ncbi.nlm.nih.gov/pubmed/33431876
https://www.proquest.com/docview/2476779671
https://www.proquest.com/docview/2477265126
https://hal.science/hal-05023875
https://pubmed.ncbi.nlm.nih.gov/PMC7801428
https://doaj.org/article/c3382a0b06624f9aa3dc99ff11e7fed0
Volume 12
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