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The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement

View ORCID ProfileBrian D. Quinlan, Huihui Mou, Lizhou Zhang, Yan Guo, Wenhui He, Amrita Ojha, Mark S. Parcells, Guangxiang Luo, Wenhui Li, Guocai Zhong, View ORCID ProfileHyeryun Choe, View ORCID ProfileMichael Farzan
doi: https://doi.org/10.1101/2020.04.10.036418
Brian D. Quinlan
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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Huihui Mou
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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Lizhou Zhang
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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Yan Guo
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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Wenhui He
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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Amrita Ojha
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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Mark S. Parcells
2Department of Animal and Food Sciences, University of Delaware, Newark, DE 19716, USA
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Guangxiang Luo
3Department of Microbiology, University of Alabama at Birmingham School Of Medicine, Birmingham, AL 35294, USA
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Wenhui Li
4National Institute of Biological Sciences, Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing, China
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Guocai Zhong
5Scripps Research | SZBL Chemical Biology Institute, Shenzhen Bay Laboratory (SZBL), Shenzhen, China
6School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China
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Hyeryun Choe
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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  • For correspondence: hchoe@scripps.edu mfarzan@scripps.edu
Michael Farzan
1Department of Immunology and Microbiology, The Scripps Research Institute, Jupiter, FL 33458, USA
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  • For correspondence: hchoe@scripps.edu mfarzan@scripps.edu
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SUMMARY

The SARS-coronavirus 2 (SARS-CoV-2) spike (S) protein mediates entry of SARS-CoV-2 into cells expressing the angiotensin-converting enzyme 2 (ACE2). The S protein engages ACE2 through its receptor-binding domain (RBD), an independently folded 197-amino acid fragment of the 1273-amino acid S-protein protomer. Antibodies to the RBD domain of SARS-CoV (SARS-CoV-1), a closely related coronavirus which emerged in 2002-2003, have been shown to potently neutralize SARS-CoV-1 S-protein-mediated entry, and the presence of anti-RBD antibodies correlates with neutralization in SARS-CoV-2 convalescent sera. Here we show that immunization with the SARS-CoV-2 RBD elicits a robust neutralizing antibody response in rodents, comparable to 100 µg/ml of ACE2-Ig, a potent SARS-CoV-2 entry inhibitor. Importantly, anti-sera from immunized animals did not mediate antibody-dependent enhancement (ADE) of S-protein-mediated entry under conditions in which Zika virus ADE was readily observed. These data suggest that an RBD-based vaccine for SARS-CoV-2 could be safe and effective.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted April 12, 2020.
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The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement
Brian D. Quinlan, Huihui Mou, Lizhou Zhang, Yan Guo, Wenhui He, Amrita Ojha, Mark S. Parcells, Guangxiang Luo, Wenhui Li, Guocai Zhong, Hyeryun Choe, Michael Farzan
bioRxiv 2020.04.10.036418; doi: https://doi.org/10.1101/2020.04.10.036418
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The SARS-CoV-2 receptor-binding domain elicits a potent neutralizing response without antibody-dependent enhancement
Brian D. Quinlan, Huihui Mou, Lizhou Zhang, Yan Guo, Wenhui He, Amrita Ojha, Mark S. Parcells, Guangxiang Luo, Wenhui Li, Guocai Zhong, Hyeryun Choe, Michael Farzan
bioRxiv 2020.04.10.036418; doi: https://doi.org/10.1101/2020.04.10.036418

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