Antibody potency, effector function, and combinations in protection and therapy for SARS-CoV-2 infection in vivo
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Abstract
SARS-CoV-2, the causative agent of COVID-19, has been responsible for over 42 million infections and 1 million deaths since its emergence in December 2019. There are few therapeutic options and no approved vaccines. Here, we examine the properties of highly potent human monoclonal antibodies (hu-mAbs) in a Syrian hamster model of SARS-CoV-2 and in a mouse-adapted model of SARS-CoV-2 infection (SARS-CoV-2 MA). Antibody combinations were effective for prevention and in therapy when administered early. However, in vitro antibody neutralization potency did not uniformly correlate with in vivo protection, and some hu-mAbs were more protective in combination in vivo. Analysis of antibody Fc regions revealed that binding to activating Fc receptors contributes to optimal protection against SARS-CoV-2 MA. The data indicate that intact effector function can affect hu-mAb protective activity and that in vivo testing is required to establish optimal hu-mAb combinations for COVID-19 prevention.
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Non-neutralizing antibodies that bind viral proteins could contribute to immune control by clearing free virus or targeting infected cells.
“Antibodies that bind to viral proteins but do not neutralize SARS-CoV-2 could still contribute to the immune control of infection through the increased clearance of free virus or by targeting infected cells for immune clearance (through antibody-dependent cellular cytotoxicity and other mechanisms)25 (preprint data, not yet peer reviewed)26.”
From Prospects for durable immune control of SARS-CoV-2 and prevention of reinfection (2021) · cites this paper as [25]
Residual non-neutralizing antibodies after infection may provide some protection during reinfection even when serum neutralizing activity is below the protective threshold.
“Thus, residual SARS-CoV-2-specific non-neutralizing antibodies following infection may confer some protective benefit during reinfection, even when serum neutralizing activity has declined below the threshold of protection25–27.”
From Prospects for durable immune control of SARS-CoV-2 and prevention of reinfection (2021) · cites this paper as [25]
Antibodies in classes 1 and 2 are both highly potent and highly abundant.
“Class 1 and 2 antibodies are among the most potent and also the most abundant antibodies7,8,21,22,25,39.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [39]
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 [20]
Antibody functions besides neutralization have been shown to correlate with protection.
“antibody functions other than neutralization have been shown to correlate with protection (Bartsch et al., 2021; Gorman et al., 2021; Schäfer et al., 2021).”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Schäfer et al., 2021
Neutralizing antibody titers in serum are expected to correlate with protection.
“Although serum neutralizing titers are an anticipated correlate of protection38”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [38]
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Cites
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969 · see citing works
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586 · see citing works
SARS and MERS: recent insights into emerging coronaviruses
de Wit, E., van Doremalen, N., Falzarano, D., & Munster, V. J. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.81 · Cited by 3,510 · see citing works
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · see citing works
Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
Clynes, R. A., Towers, T. L., Presta, L. G., & Ravetch, J. V. (2000) · Nature Medicine · doi:10.1038/74704 · Cited by 2,768 · see citing works
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885 · see citing works
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853 · see citing works
Self-citationHuman neutralizing antibodies elicited by SARS-CoV-2 infection
Ju, B., Zhang, Q., Ge, J., Wang, R., Sun, J., Ge, X., Yu, J., Shan, S., Zhou, B., Song, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2380-z · Cited by 1,667 · see citing works
SARS-CoV-2 mRNA Vaccine Design Enabled by Prototype Pathogen Preparedness
Corbett, K. S., Edwards, D. K., Leist, S. R., Abiona, O. M., Boyoglu-Barnum, S., Gillespie, R. A., Himansu, S., Schäfer, A., Ziwawo, C. T., DiPiazza, A. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2622-0 · Cited by 1,615 · see citing works
Self-citationSARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599 · see citing works
Self-citationPotent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349 · see citing works
Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308 · see citing works
Self-citationA human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286 · see citing works
Baum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253 · see citing works
Rogers, T. F., Zhao, F., Huang, D., Beutler, N., Burns, A., He, W.-T., Limbo, O., Smith, C., Song, G., Woehl, J., et al. (2020) · Science · doi:10.1126/science.abc7520 · Cited by 1,230 · see citing works
Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
Hansen, J., Baum, A., Pascal, K. E., Russo, V., Giordano, S., Wloga, E., Fulton, B. O., Yan, Y., Koon, K., Patel, K., et al. (2020) · Science · doi:10.1126/science.abd0827 · Cited by 1,210 · see citing works
Cao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.025 · Cited by 1,188 · see citing works
Potently neutralizing and protective human antibodies against SARS-CoV-2
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., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041 · see citing works
Self-citationDivergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding
Nimmerjahn, F., & Ravetch, J. V. (2005) · Science · doi:10.1126/science.1118948 · Cited by 1,040 · see citing works
Self-citationBarnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795 · see citing works
Self-citationSingle-Shot Ad26 Vaccine Protects Against SARS-CoV-2 in Rhesus Macaques
Mercado, N. B., Zahn, R., Wegmann, F., Loos, C., Chandrashekar, A., Yu, J., Liu, J., Peter, L., McMahan, K., Tostanoski, L. H., et al. (2020) · Nature · doi:10.1038/s41586-020-2607-z · Cited by 789 · see citing works
Self-citationDiLillo, D. J., Tan, G. S., Palese, P., & Ravetch, J. V. (2014) · Nature Medicine · doi:10.1038/nm.3443 · Cited by 749 · see citing works
Self-citationA mouse-adapted model of SARS-CoV-2 to test COVID-19 countermeasures
Dinnon, K. H., Leist, S. R., Schäfer, A., Edwards, C. E., Martinez, D. R., Montgomery, S. A., West, A., Yount, B. L., Hou, Y. J., Adams, L. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2708-8 · Cited by 675 · see citing works
Self-citationEnhanced antibody half-life improves in vivo activity
Zalevsky, J., Chamberlain, A. K., Horton, H. M., Karki, S., Leung, I., Sproule, T. J., Lazar, G. A., Roopenian, D. C., & Desjarlais, J. R. (2010) · Nature Biotechnology · doi:10.1038/nbt.1601 · Cited by 657 · see citing works
The role of IgG Fc receptors in antibody-dependent enhancement
Bournazos, S., Gupta, A., & Ravetch, J. V. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00410-0 · Cited by 619 · see citing works
Self-citationMeasuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses
Schmidt, F., Weisblum, Y., Muecksch, F., Hoffmann, H.-H., Michailidis, E., Lorenzi, J. C. C., Mendoza, P., Rutkowska, M., Bednarski, E., Gaebler, C., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201181 · Cited by 572 · see citing works
Self-citationBroadly Neutralizing Anti-HIV-1 Antibodies Require Fc Effector Functions for In Vivo Activity
Bournazos, S., Klein, F., Pietzsch, J., Seaman, M. S., Nussenzweig, M. C., & Ravetch, J. V. (2014) · Cell · doi:10.1016/j.cell.2014.08.023 · Cited by 493 · see citing works
Self-citationZost, S. J., Gilchuk, P., Chen, R. E., Case, J. B., Reidy, J. X., Trivette, A., Nargi, R. S., Sutton, R. E., Suryadevara, N., Chen, E. C., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0998-x · Cited by 423 · see citing works
Self-citationBroadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
DiLillo, D. J., Palese, P., Wilson, P. C., & Ravetch, J. V. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84428 · Cited by 409 · see citing works
Self-citationHalper-Stromberg, A., Lu, C.-L., Klein, F., Horwitz, J. A., Bournazos, S., Nogueira, L., Eisenreich, T., Liu, C., Gazumyan, A., Schaefer, U., et al. (2014) · Cell · doi:10.1016/j.cell.2014.07.043 · Cited by 378 · see citing works
Self-citationIgG antibodies to dengue enhanced for FcγRIIIA binding determine disease severity
Wang, T. T., Sewatanon, J., Memoli, M. J., Wrammert, J., Bournazos, S., Bhaumik, S. K., Pinsky, B. A., Chokephaibulkit, K., Onlamoon, N., Pattanapanyasat, K., et al. (2017) · Science · doi:10.1126/science.aai8128 · Cited by 371 · see citing works
Self-citationLaczko, D. I., Hogan, M. J., Toulmin, S. A., Hicks, P. D., Lederer, K., Gaudette, B. T., Castaño, D., Amanat, F., Muramatsu, H., Oguin, T. H., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.019 · Cited by 366 · see citing works
Enhanced clearance of HIV-1–infected cells by broadly neutralizing antibodies against HIV-1 in vivo
Lu, C.-L., Murakowski, D. K., Bournazos, S., Schoofs, T., Sarkar, D., Halper-Stromberg, A., Horwitz, J. A., Nogueira, L., Golijanin, J., Gazumyan, A., et al. (2016) · Science · doi:10.1126/science.aaf1279 · Cited by 348 · see citing works
Self-citationRecurrent Potent Human Neutralizing Antibodies to Zika Virus in Brazil and Mexico
Robbiani, D. F., Bozzacco, L., Keeffe, J. R., Khouri, R., Olsen, P. C., Gazumyan, A., Schaefer-Babajew, D. J., Ávila‐Ríos, S., Nogueira, L., Patel, R., et al. (2017) · Cell · doi:10.1016/j.cell.2017.04.024 · Cited by 335 · see citing works
Self-citationAn update on feline infectious peritonitis: Virology and immunopathogenesis
Pedersen, N. C. (2014) · The Veterinary Journal · doi:10.1016/j.tvjl.2014.04.017 · Cited by 247 · see citing works
Signaling by Antibodies: Recent Progress
Bournazos, S., Wang, T. T., Dahan, R., Maamary, J., & Ravetch, J. V. (2017) · Annual Review of Immunology · doi:10.1146/annurev-immunol-051116-052433 · Cited by 230 · see citing works
Self-citationEscape from neutralizing antibodies by SARS-CoV-2 spike protein variantsPreprint
Weisblum, Y., Schmidt, F., Zhang, F., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.21.214759 · Cited by 172 · see citing works
Self-citationHigh Potency of a Bivalent Human VH Domain in SARS-CoV-2 Animal Models
Li, W., Schäfer, A., Kulkarni, S. S., Liu, X., Martinez, D. R., Chen, C., Sun, Z., Leist, S. R., Drelich, A. K., Zhang, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.007 · Cited by 117 · see citing works
Self-citationMemory B Cell Antibodies to HIV-1 gp140 Cloned from Individuals Infected with Clade A and B Viruses
Mouquet, H., Klein, F., Scheid, J. F., Warncke, M. L., Pietzsch, J., Oliveira, T. Y., Velinzon, K., Seaman, M. S., & Nussenzweig, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024078 · Cited by 111 · see citing works
Self-citationCOVID 19 Vaccines: Should we fear ADE?
Halstead, S. B., & Katzelnick, L. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa518 · Cited by 69 · see citing works
Differential requirements for FcγR engagement by protective antibodies against Ebola virus
Bournazos, S., DiLillo, D. J., Goff, A. J., Glass, P. J., & Ravetch, J. V. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911842116 · Cited by 45 · see citing works
Self-citationBarnes, C. O., Jette, C. A., Abernathy, M. E., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.30.273920 · Cited by 38 · see citing works
Wang, B., Asarnow, D. E., Lee, W.-H. S., Huang, C.-W., Faust, B., Ng, P. M. L., Ngoh, E. Z. X., Bohn, M., Bulkley, D. P., Pizzorno, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.14.203414 · Cited by 21 · see citing works
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Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674 · see citing works
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Chen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881 · see citing works
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- Authors
- Schäfer, A., Muecksch, F., Lorenzi, J. C. C., Leist, S. R., Cipolla, M., Bournazos, S., Schmidt, F., Maison, R. M., Gazumyan, A., Martinez, D. R., Baric, R. S., Robbiani, D. F., Hatziioannou, T., Ravetch, J. V., Bieniasz, P. D., Bowen, R. A., Nussenzweig, M. C., & Sheahan, T. P.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Rockefeller University (US)
- Colorado State University (US)
- Institute for Research in Biomedicine (CH)
- Laboratory of Retrovirology, The Rockefeller University, New York, NY 2
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nussenzweig, Michel C.
- Sheahan, Timothy P.
- ORCID
- Schäfer, Alexandra
- Muecksch, Frauke
- Lorenzi, Julio C.C.
- Leist, Sarah R.
- Cipolla, Melissa
- Bournazos, Stylianos
- Schmidt, Fabian
- Maison, Rachel M.
- Gazumyan, Anna
- Martinez, David R.
- Baric, Ralph S.
- Robbiani, Davide F.
- Hatziioannou, Theodora
- Ravetch, Jeffrey V.
- Bieniasz, Paul D.
- Bowen, Richard A.
- Nussenzweig, Michel C.
- Sheahan, Timothy P.
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2020-11-19
- Volume
- 218
- Issue
- 3
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC7673958
- OpenAlex
- W3099530525
- Cited by
- 305
- References
- 43
- Citations by year
- 2026: 9 · 2025: 19 · 2024: 25 · 2023: 45 · 2022: 81 · 2021: 124 · 2020: 2
- FWCI
- 8.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The Journal of Experimental Medicine (publishedVersion, cc-by-nc-sa)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- UNC Libraries
- Funders
- George Mason University
- National Institute of Allergy and Infectious Diseases (1U19AI142759)
- Antiviral Drug Discovery and Development Center (P01-AI138398-S1, 2U1 9AI111825, R01AI137276, U19AI111825)
- Howard Hughes Medical Institute
- The Rockefeller University
- North Carolina Policy Collaboratory
- University of North Carolina at Chapel Hill
- North Carolina Coronavirus Relief Fund
- North Carolina General Assembly
- 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 › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, COVID-19 pandemic, human monoclonal antibodies, antibody combinations, antibody potency, neutralization, Fc receptors, effector function, Syrian hamster model, passive immunization, prevention and treatment
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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