Human neutralizing antibodies elicited by SARS-CoV-2 infection
Open accessPublished version of a preprint
Abstract
The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents a global health emergency that is in urgent need of intervention 1-3. The entry of SARS-CoV-2 into its target cells depends on binding between the receptor-binding domain (RBD) of the viral spike protein and its cellular receptor, angiotensin-converting enzyme 2 (ACE2)2,4-6. Here we report the isolation and characterization of 206 RBD-specific monoclonal antibodies derived from single B cells from 8 individuals infected with SARS-CoV-2. We identified antibodies that potently neutralize SARS-CoV-2; this activity correlates with competition with ACE2 for binding to RBD. Unexpectedly, the anti-SARS-CoV-2 antibodies and the infected plasma did not cross-react with the RBDs of SARS-CoV or Middle East respiratory syndrome-related coronavirus (MERS-CoV), although there was substantial plasma cross-reactivity to their trimeric spike proteins. Analysis of the crystal structure of RBD-bound antibody revealed that steric hindrance inhibits viral engagement with ACE2, thereby blocking viral entry. These findings suggest that anti-RBD antibodies are largely viral-species-specific inhibitors. The antibodies identified here may be candidates for development of clinical interventions against SARS-CoV-2.
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Most of the strongest neutralizing antibodies against SARS-CoV-2 identified so far bind the RBD.
“We focused on the RBD since it is the target of the majority of the more potent SARS-CoV-2 neutralizing antibodies discovered to date21–26.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [24]
mRNA vaccines induce antibodies to RBD, the main target of neutralizing antibodies, in a way that resembles natural infection.
“The vaccines elicit antibody responses against the RBD, the major target of neutralizing antibodies21–26, in a manner that resembles natural infection.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [24]
Plasma RBD antibodies are strongly correlated with neutralizing activity.
“We limited our analysis to RBD because plasma RBD antibodies are strongly correlated with neutralizing activity3,10–12.”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [12]
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 [35]
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SARS-CoV-2-reactive T cells in healthy donors and patients with COVID-19
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Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
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mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
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BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection
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Self-citationStriking antibody evasion manifested by the Omicron variant of SARS-CoV-2
Liu, L., Iketani, S., Guo, Y., Chan, J. F.-W., Wang, M., Liu, L., Luo, Y., Chu, H., Huang, Y., Nair, M. S., et al. (2022) · Nature · doi:10.1038/s41586-021-04388-0 · Cited by 1,290 · see citing works
Self-citationPotently 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
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“Many of the most potently neutralizing anti-SARS-CoV-2 antibodies target the receptor-binding domain (RBD) of the viral spike protein, often competing with its binding to the ACE2 receptor (Brouwer et al., 2020; Cao et al., 2020; Ju et al., 2020; Liu et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Wec et al.…”
IgA dominates the early neutralizing antibody response to SARS-CoV-2
Sterlin, D., Mathian, A., Miyara, M., Mohr, A., Anna, F., Claër, L., Quentric, P., Fadlallah, J., Devilliers, H., Ghillani, P., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd2223 · Cited by 1,037 · see citing works
Viral targets for vaccines against COVID-19
Dai, L., & Gao, G. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00480-0 · Cited by 949 · see citing works
mRNA-based COVID-19 vaccine boosters induce neutralizing immunity against SARS-CoV-2 Omicron variant
Garcia-Beltran, W. F., St. Denis, K. J., Hoelzemer, A., Lam, E. C., Nitido, A. D., Sheehan, M. L., Berrios, C., Ofoman, O., Chang, C. C., Hauser, B. M., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.033 · Cited by 1,045 · see citing works
“Limitations of the study Although previous studies that used pseudovirus neutralization tomodel the sensitivity of replicating SARS-CoV-2 to neutralizing antibodies have shown excellent correlations (Crawford et al., 2020; Ju et al., 2020;Moore et al., 2004; Pinto et al., 2020; Riepler et al., 2020;Wang et al., 2020;…”
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works
“, 2020), and numerous monoclonal antibodies (mAbs) recognizing this domain have been isolated and characterized (Barnes et al., 2020a, 2020b; Baumet al., 2020b; Brouwer et al., 2020; Hansen et al., 2020; Ju et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Tortorici et al., 2020; Wang et al., 2020; Wu et al., 20…”
The biological and clinical significance of emerging SARS-CoV-2 variants
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A dynamic COVID-19 immune signature includes associations with poor prognosis
Laing, A. G., Lorenc, A., del Molino del Barrio, I., Das, A., Fish, M., Monin, L., Muñoz-Ruiz, M., McKenzie, D. R., Hayday, T. S., Francos-Quijorna, I., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1038-6 · Cited by 946 · see citing works
“Thus, we employed eight multiparameter flow cytometry panels (P1–P8), measuring: (1) broad lymphocyte composition; (2) effector/memory T cell status; (3) γδ T cell status; (4) B cells; (5) cell cycling; (6) leukocyte counts; (7) lymphocyte activation and exhaustion; and (8) innate immune cells.”
MethodBarnes, 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
“Other studies have also reported anti-SARS-CoV-2 mAbs derived from these genes (Brouwer et al., 2020; Cao et al., 2020; Chi et al., 2020; Ju et al., 2020; Rogers et al., 2020; Seydoux et al., 2020; Wu et al., 2020c; Zost et al., 2020).”
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“ACE2 is a surrogate for virus neutralization [134].”
BackgroundSARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development
Wang, M.-Y., Zhao, R., Gao, L.-J., Gao, X.-F., Wang, D.-P., & Cao, J.-M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.587269 · Cited by 874 · see citing works
Preexisting and de novo humoral immunity to SARS-CoV-2 in humans
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Antibody evasion properties of SARS-CoV-2 Omicron sublineages
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Self-citationNaturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection
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Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5
Wang, Q., Guo, Y., Iketani, S., Nair, M. S., Li, Z., Mohri, H., Wang, M., Yu, J., Bowen, A. D., Chang, J. Y., et al. (2022) · Nature · doi:10.1038/s41586-022-05053-w · Cited by 768 · see citing works
Self-citationLoss of Bcl-6-Expressing T Follicular Helper Cells and Germinal Centers in COVID-19
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“In persons with COVID-19, the magnitude and durability of antibody responses are greater in those with more severe disease (Ju et al., 2020; Amanat et al., 2020) but are often of low magnitude (Robbiani et al.”
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Genomic evidence for reinfection with SARS-CoV-2: a case study
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COVID-19 neutralizing antibodies predict disease severity and survival
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“Although non-RBD anti-spike antibodies can cross-react between different coronaviruses (Secchi et al., 2020; Chan et al., 2005; Ju et al., 2020), we assessed for cross-reactivity of antiRBD IgG in sera of SARS-CoV-2 seropositive individuals by modifying our ELISA to detect IgG antibodies against the RBD of SARS-CoV an…”
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589 · see citing works
Antibody-dependent enhancement and SARS-CoV-2 vaccines and therapies
Lee, W. S., Wheatley, A. K., Kent, S. J., & DeKosky, B. J. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00789-5 · Cited by 676 · see citing works
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“22 Early in-silico analysis suggests that the mutations present in B.1.1.7 might confer only small changes in epitope signal.”
InfluentialMeasuring 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
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
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mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
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Large-Scale Multi-omic Analysis of COVID-19 Severity
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“To better understand production of protective or possibly injurious antibodies, serial studies and characterization of the properties of individual antibodies is required (Ju et al., 2020; Seydoux et al., 2020).”
BackgroundImmunity, endothelial injury and complement-induced coagulopathy in COVID-19
Perico, L., Benigni, A., Casiraghi, F., Ng, L. F. P., Rénia, L., & Remuzzi, G. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-00357-4 · Cited by 603 · see citing works
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“The sera of the three individuals with neutralizing titers also had high activity in an assay that measures the ability of antibodies to block RBD binding to ACE2, as well as in IgG ELISAs against spike and RBD (Table 1; Fig.”
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Self-citationREGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters
Baum, A., Ajithdoss, D., Copin, R., Zhou, A., Lanza, K., Negron, N., Ni, M., Wei, Y., Mohammadi, K., Musser, B., et al. (2020) · Science · doi:10.1126/science.abe2402 · Cited by 517 · see citing works
Structural biology of SARS-CoV-2 and implications for therapeutic development
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A systematic review of SARS-CoV-2 vaccine candidates
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Self-citationEnhanced SARS-CoV-2 neutralization by dimeric IgA
Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Viant, C., Gaebler, C., Cipolla, M., Hoffmann, H.-H., Oliveira, T. Y., Oren, D. A., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf1555 · Cited by 475 · see citing works
The COVID-19 puzzle: deciphering pathophysiology and phenotypes of a new disease entity
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“22 Some antibodies that bind to specific epitopes on the spike RBD and NTD can block 435 SARS-CoV-2 infection of respiratory epithelial cells by inhibiting the interactions of the 436 viral spike with the ACE2 receptor.(17-20) Thus, as expected, the early rise and decline of 437”
Zost, 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
An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike
Schoof, M., Faust, B., Saunders, R. A., Sangwan, S., Rezelj, V. V., Hoppe, N., Boone, M., Billesbølle, C. B., Puchades, C., Azumaya, C. M., et al. (2020) · Science · doi:10.1126/science.abe3255 · Cited by 428 · see citing works
“High-affinity monoclonal antibodies, many identified from convalescent 290 patients, are leading the way as potential therapeutics [22-29].”
Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity
García-Beltrán, W. F., Lam, E. C., Denis, K. S., Nitido, A. D., Garcia, Z. H., Hauser, B. M., Feldman, J. E., Pavlovic, M., Gregory, D. J., Poznansky, M. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.006 · Cited by 446 · see citing works
“…now demonstrated a close correlation between neutralization titers measured against pseudovirus and live SARS-CoV-2 cultures (Wang et al., 2020; Ju et al., 2020; Pinto et al., 2020; Yang et al., 2020; Moore et al., 2004; Crawford et al., 2020; Riepler et al., 2020), it is unclear what impact…”
InfluentialThe antigenic anatomy of SARS-CoV-2 receptor binding domain
Dejnirattisai, W., Zhou, D., Ginn, H. M., Duyvesteyn, H. M. E., Supasa, P., Case, J. B., Zhao, Y., Walter, T. S., Mentzer, A. J., Liu, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.032 · Cited by 371 · see citing works
“Although the orientation of 384 is similar to a group of previously reported Fabs (CV07-270, p2b-2f6 and bd629, (Kreye et al., 2020; Ju et al., 2020; Du et al., 2020)), it is shifted 20 Å towards the left shoulder such that it does not contact the right chest ( Figures 3, 4E).”
The first 12 months of COVID-19: a timeline of immunological insights
Carvalho, T., Krammer, F., & Iwasaki, A. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00522-1 · Cited by 448 · see citing works
CoV-AbDab: the coronavirus antibody database
Raybould, M. I. J., Kovaltsuk, A., Marks, C., & Deane, C. M. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btaa739 · Cited by 383 · see citing works
COVID-19: Discovery, diagnostics and drug development
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“Indeed, antibodies to this protein are frequently detected in COVID-19 patient [64-65], suggesting that N protein may be one of the immunodominant antigens in the early diagnosis of COVID-19 [60, 66-67].”
BackgroundQuantification of SARS-CoV-2 neutralizing antibody by a pseudotyped virus-based assay
Nie, J., Li, Q., Wu, J., Zhao, C., Hao, H., Liu, H., Zhang, L., Nie, L., Qin, H., Wang, M., et al. (2020) · Nature Protocols · doi:10.1038/s41596-020-0394-5 · Cited by 418 · see citing works
Self-citationGruell, H., Vanshylla, K., Tober-Lau, P., Hillus, D., Schommers, P., Lehmann, C., Kurth, F., Sander, L. E., & Klein, F. (2022) · Nature Medicine · doi:10.1038/s41591-021-01676-0 · Cited by 410 · see citing works
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“overlapping epitopes and show differences in neutralization potency (Alsoussi et al., 2020; Cao et al., 2020; Hansen et al., 2020; Ju et al., 2020; Liu et al., 2020; Noy-Porat et al., 2020; Pinto et al., 2020; Robbiani et al., 2020; Zost et al., 2020a).”
Self-citationCheng, M. H., Zhang, S., Porritt, R. A., Rivas, M. N., Paschold, L., Willscher, E., Binder, M., Arditi, M., & Bahar, İ. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010722117 · Cited by 390 · see citing works
Self-citationTackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.05.005 · Cited by 375 · see citing works
Broadly neutralizing antibodies to SARS-CoV-2 and other human coronaviruses
Chen, Y., Zhao, X., Zhou, H., Zhu, H., Jiang, S., & Wang, P. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00784-3 · Cited by 371 · see citing works
Antibody response to SARS-CoV-2 infection in humans: A systematic review
Post, N., Eddy, D., Huntley, C., van Schalkwyk, M. C. I., Shrotri, M., Leeman, D., Rigby, S., Williams, S., Bermingham, W., Kellam, P., et al. (2020) · medRxiv · doi:10.1371/journal.pone.0244126 · Cited by 341 · see citing works
“Neutralising ability correlated in particular with competition for the angiotensin converting enzyme - 2 (ACE2) receptor.(70,72,106) Two studies demonstrated a lack of association with affinity,(73,106) although a moderate correlation with binding affinity was reported in one study.”
BackgroundCOVID-19 and Cardiovascular Disease
Chung, M. K., Zidar, D. A., Bristow, M. R., Cameron, S. J., Chan, T. A.-T., Harding, C. V., Kwon, D. H., Singh, T. K., Tilton, J. C., Tsai, E. J., et al. (2021) · Circulation Research · doi:10.1161/circresaha.121.317997 · Cited by 371 · see citing works
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
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“6 Following the emergence of SARS-CoV-2, monoclonal antibodies targeting the spike receptor binding domain were rapidly isolated from humanised mice and from peripheral B cells of recovered patients.”
Virus-induced senescence is a driver and therapeutic target in COVID-19
Lee, S., Yu, Y., Trimpert, J., Benthani, F., Mairhofer, M., Richter-Pechanska, P., Wyler, E., Belenki, D., Kaltenbrunner, S., Pammer, M., et al. (2021) · Nature · doi:10.1038/s41586-021-03995-1 · Cited by 350 · see citing works
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“Most neutralizing SARS-CoV-2 mAbs block RBD interactions with ACE2 (Brouwer et al., 2020; Cao et al., 2020; Ju et al., 2020; Liu et al., 2020a; Rogers et al., 2020; Seydoux et al., 2020; Wec et al., 2020; Wu et al., 2020; Zost et al., 2020a, 2020b).”
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., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20201993 · Cited by 305 · see citing works
D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization
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SARS-CoV-2 501Y.V2 variants lack higher infectivity but do have immune escape
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- Authors
- Ju, B., Zhang, Q., Ge, J., Wang, R., Sun, J., Ge, X., Yu, J., Shan, S., Zhou, B., Song, S., Tang, X., Yu, J., Lan, J., Yuan, J., Wang, H., Zhao, J., Zhang, S., Wang, Y., Shi, X., Liu, L., Zhao, J., Wang, X., Zhang, Z., & Zhang, L.
- Affiliations
- Southern University of Science and Technology (CN)
- Tsinghua University (CN)
- First Affiliated Hospital of Guangzhou Medical University (CN)
- Shenzhen Third People’s Hospital (CN)
- Shanghai Medical College of Fudan University (CN)
- National Institutes for Food and Drug Control (CN)
- Corresponding author
- Zhang, Qi
- Wang, Xinquan
- Zhang, Zheng
- Zhang, Linqi
- ORCID
- Venue
- Nature
- Published
- 2020-05-26
- Volume
- 584
- Issue
- 7819
- Pages
- 115-119
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W3029682964
- Cited by
- 1,667
- References
- 55
- Citations by year
- 2026: 33 · 2025: 62 · 2024: 108 · 2023: 156 · 2022: 346 · 2021: 613 · 2020: 345 · 2018: 1 · 2014: 1
- FWCI
- 48.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Bill and Melinda Gates Foundation
- Tsinghua University (20201080053)
- 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, neutralizing antibodies, receptor binding domain, spike protein, ACE2, monoclonal antibodies, steric hindrance, cross-reactivity, SARS-CoV, MERS-CoV, viral entry inhibition, antibody crystal structure
- MeSH terms
- Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Adult, Aged, Antibodies, Viral, B-Lymphocytes, Child, Clone Cells, Cross Reactions, Crystallization, Female, Humans, Peptidyl-Dipeptidase A, Male, Middle Aged, Models, Molecular, Neutralization Tests, Plasma, Pneumonia, Viral, Coronavirus Infections, Crystallography, X-Ray, Antibodies, Neutralizing, Pandemics, Spike Glycoprotein, Coronavirus
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