Potently neutralizing and protective human antibodies against SARS-CoV-2
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Abstract
The ongoing pandemic of coronavirus disease 2019 (COVID-19), which is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), is a major threat to global health 1 and the medical countermeasures available so far are limited 2,3. Moreover, we currently lack a thorough understanding of the mechanisms of humoral immunity to SARS-CoV-2 4. Here we analyse a large panel of human monoclonal antibodies that target the spike (S) glycoprotein 5, and identify several that exhibit potent neutralizing activity and fully block the receptor-binding domain of the S protein (S RBD) from interacting with human angiotensin-converting enzyme 2 (ACE2). Using competition-binding, structural and functional studies, we show that the monoclonal antibodies can be clustered into classes that recognize distinct epitopes on the S RBD, as well as distinct conformational states of the S trimer. Two potently neutralizing monoclonal antibodies, COV2-2196 and COV2-2130, which recognize non-overlapping sites, bound simultaneously to the S protein and neutralized wild-type SARS-CoV-2 virus in a synergistic manner. In two mouse models of SARS-CoV-2 infection, passive transfer of COV2-2196, COV2-2130 or a combination of both of these antibodies protected mice from weight loss and reduced the viral burden and levels of inflammation in the lungs. In addition, passive transfer of either of two of the most potent ACE2-blocking monoclonal antibodies (COV2-2196 or COV2-2381) as monotherapy protected rhesus macaques from SARS-CoV-2 infection. These results identify protective epitopes on the S RBD and provide a structure-based framework for rational vaccine design and the selection of robust immunotherapeutic agents.
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IgH CDR3 length was comparable between naturally infected people and vaccinees, and hydrophobicity was lower than average.
“The length of the IgH CDR3 was similar in both natural infected individuals and vaccinees and hydrophobicity was below average27 (Fig. 2h and Extended Data Fig. 5a and b).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [27]
Numerous neutralizing anti-RBD monoclonal antibodies have been characterized, the most potent of which block the RBD-ACE2 interaction.
“Numerous neutralizing anti-RBD monoclonal antibodies (mAbs) have been characterized, the most potent of which block the RBD-ACE2 interaction (16, 17, 22–24, 32–37).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [17]
Passive transfer of nAbs limits respiratory tract infection and protects against infection in animal models.
“passive transfer of nAbs limits respiratory tract infection and protects against infection in animal models (16–20)”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [17]
Passive transfer of neutralizing antibodies before SARS-CoV-2 exposure can prevent or limit upper respiratory tract infection, lung infection, and symptomatic disease in animal models.
“passive transfer of neutralizing antibodies in advance of SARS-CoV-2 infection (mimicking the conditions of 2° infection) can effectively prevent or limit URT infection, lung infection, and symptomatic disease in animal models”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Zost et al., 2020
Neutralizing antibodies against the RBD of SARS-CoV-2 have been discovered in mice and humans.
“Neutralizing antibodies against the RBD of SARS-CoV-2 have been discovered in both mice and humans149,150, and passive transfer of these antibodies reduces disease severity and offers protection in mouse models of SARS-CoV-2.”
From SARS-CoV-2, COVID-19 and the aging immune system (2021) · cites this paper as [150]
Passive transfer of neutralizing antibodies reduces disease severity and offers protection in mouse models of SARS-CoV-2.
“Neutralizing antibodies against the RBD of SARS-CoV-2 have been discovered in both mice and humans149,150, and passive transfer of these antibodies reduces disease severity and offers protection in mouse models of SARS-CoV-2.”
From SARS-CoV-2, COVID-19 and the aging immune system (2021) · cites this paper as [150]
The ACE2 interacting surface of RBD is a small 25-amino-acid patch at the apex of S and is under extreme selection pressure because it mediates receptor interaction and is the binding site for a major class of neutralizing antibodies.
“The ACE2 interacting surface of RBD is a small 25-amino-acid patch at the apex of S and is under extreme selection pressure, as it mediates interaction with the cellular receptor and is also the site of binding for a major class of neutralizing antibodies that block the interaction of ACE2 with the RBD (Zost et al., 2020; Kreye et al., 2020; Wu et al., 2020; Yuan et al., 2020; Dejnirattisai et al.”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Zost et al., 2020
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- Authors
- Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., Sutton, R. E., Suryadevara, N., Martinez, D. R., Williamson, L. E., Chen, E. C., Jones, T., Day, S., Myers, L., Hassan, A. O., Kafai, N. M., Winkler, E. S., Fox, J. M., Shrihari, S., Mueller, B. K., Meiler, J., Chandrashekar, A., Mercado, N. B., Steinhardt, J. J., Ren, K., Loo, Y.-M., Kallewaard, N. L., McCune, B. T., Keeler, S. P., Holtzman, M. J., Barouch, D. H., Gralinski, L. E., Baric, R. S., Thackray, L. B., Diamond, M. S., Carnahan, R. H., & Crowe, J. E.
- Affiliations
- Vanderbilt University Medical Center (US)
- Washington University in St. Louis (US)
- Beth Israel Deaconess Medical Center (US)
- University of North Carolina at Chapel Hill (US)
- Vanderbilt University (US)
- AstraZeneca (United States) (US)
- Corresponding author
- Carnahan, Robert H.
- Crowe, James E.
- ORCID
- Zost, Seth J.
- Gilchuk, Pavlo
- Case, James Brett
- Binshtein, Elad
- Chen, Rita E.
- Nkolola, Joseph P.
- Schäfer, Alexandra
- Suryadevara, Naveenchandra
- Martinez, David R.
- Williamson, Lauren E.
- Chen, Elaine C.
- Jones, Taylor
- Myers, Luke
- Hassan, Ahmed O.
- Kafai, Natasha M.
- Winkler, Emma S.
- Fox, Julie M.
- Shrihari, Swathi
- Mueller, Benjamin K.
- Meiler, Jens
- Chandrashekar, Abishek
- Mercado, Noe B.
- Steinhardt, James J.
- Ren, Kuishu
- Loo, Yueh-Ming
- Kallewaard, Nicole L.
- McCune, Broc T.
- Keeler, Shamus P.
- Holtzman, Michael J.
- Barouch, Dan H.
- Gralinski, Lisa E.
- Baric, Ralph S.
- Thackray, Larissa B.
- Diamond, Michael S.
- Carnahan, Robert H.
- Crowe, James E.
- Venue
- Nature
- Published
- 2020-07-15
- Volume
- 584
- Issue
- 7821
- Pages
- 443-449
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7584396
- OpenAlex
- W3042323010
- Cited by
- 1,041
- References
- 65
- Citations by year
- 2026: 32 · 2025: 51 · 2024: 93 · 2023: 129 · 2022: 245 · 2021: 367 · 2020: 122
- FWCI
- 28.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- PubMed Central (submittedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- UNC Libraries
- Funders
- AstraZeneca
- Vanderbilt University
- Vanderbilt Institute for Clinical and Translational Research (UL1-TR002243)
- Merck KGaA
- Wellcome Trust
- Vanderbilt University Medical Center (UL1 TR002243)
- National Institutes of Health (NIH T32, -0001, COVID-19, 75N93019C00062, 75N93019C00074, UL1TR002243)
- Defense Advanced Research Projects Agency (HR0011, 75N93019C00074, HR0011‐18‐2‐0001, HR00 11-18-3-0001, AI095202, 75N93019C00062)
- Advanced Research Projects Agency (HR0011-18-2-0001)
- National Heart, Lung, and Blood Institute (R35HL145242)
- National Institute of Allergy and Infectious Diseases (R01AI157155, 75N93019C00074, F30AI152327, T32AI138932, F31AI145189, U01AI150739, R01AI130591, F32AI138392, 75N93019C00062, T32AI007163, T32AI095202, T32AI007151)
- U.S. National Library of Medicine (T15LM007450)
- National Center for Research Resources (S10RR028106)
- National Center for Advancing Translational Sciences
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- SARS-CoV-2, COVID-19 pandemic, human monoclonal antibodies, spike protein, receptor binding domain, ACE2, neutralizing antibodies, passive immunotherapy, antibody synergy, epitope mapping, mouse infection model, vaccine design, therapeutic antibodies
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