Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology
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Analysis of the specificity and kinetics of neutralizing antibodies (nAbs) elicited by SARS-CoV-2 infection is crucial for understanding immune protection and identifying targets for vaccine design. In a cohort of 647 SARS-CoV-2-infected subjects, we found that both the magnitude of Ab responses to SARS-CoV-2 spike (S) and nucleoprotein and nAb titers correlate with clinical scores. The receptor-binding domain (RBD) is immunodominant and the target of 90% of the neutralizing activity present in SARS-CoV-2 immune sera. Whereas overall RBD-specific serum IgG titers waned with a half-life of 49 days, nAb titers and avidity increased over time for some individuals, consistent with affinity maturation. We structurally defined an RBD antigenic map and serologically quantified serum Abs specific for distinct RBD epitopes leading to the identification of two major receptor-binding motif antigenic sites. Our results explain the immunodominance of the receptor-binding motif and will guide the design of COVID-19 vaccines and therapeutics.
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Most serum nAb responses elicited during natural infection are directed at the RBD.
“Most serum nAb responses elicited during natural infection are directed at the RBD (21, 23, 30, 31).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [30]
Serum neutralising activity is a correlate of protection for other respiratory viruses, including influenza and respiratory syncytial virus.
“Serum neutralising activity is a correlate of protection for other respiratory viruses, including influenza35 and respiratory syncytial virus where prohylaxis with monoclonal antibodies has been used in at-risk groups36,37.”
From Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies (2021) · cites this paper as [37]
Neutralizing antibody titers have not correlated with reduced COVID-19 severity.
“Although neutralizing antibody titers have not correlated with reduced COVID-19 severity (Dan et al., 2021; Piccoli et al., 2020; Robbiani et al., 2020), SARS-CoV-2 cTfh cell frequencies have been associated with reduced disease severity (Rydyznski Moderbacher et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Piccoli et al., 2020
The receptor binding domain of Spike is the target of more than 90% of neutralizing antibodies in COVID-19 cases, with some targeting the N-terminal domain.
“Spike is the target of SARS-CoV-2 neutralizing antibodies, and the receptor binding domain (RBD) of Spike is the target of >90% of neutralizing antibodies in COVID-19 cases (Brouwer et al., 2020; Piccoli et al., 2020; Robbiani et al., 2020; Rogers et al., 2020; Suthar et al., 2020), with some neutralizing antibodies instead targeting the N-terminal domain (NTD) (Liu et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Piccoli et al., 2020
The quality of Spike, neutralizing, and nucleocapsid antibodies is similar in hospitalized and non-hospitalized COVID-19 cases.
“The quality of the Spike, neutralizing, and nucleocapsid antibodies is similar in both hospitalized and non-hospitalized cases (Piccoli et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Piccoli et al., 2020
High neutralizing antibody titers are associated with severe disease and potentially extrafollicular B cell responses.
“High neutralizing antibody titers are associated with severe disease and potentially extrafollicular B cell responses (Piccoli et al., 2020; Woodruff et al., 2020), while SARS-CoV-2-specific Tfh cells have different associations depending on the study (Juno et al., 2020; Meckiff et al., 2020; Rydyznski Moderbacher et al., 2020; Oja et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Piccoli et al., 2020
Neutralizing antibody titers and total Spike antibody titers positively correlate with COVID-19 disease severity in large cohort studies.
“This appears to hold true in the case of SARS-CoV-2, where neutralizing antibody titers (and total Spike antibody titers) have positively correlated with COVID-19 disease severity in large cohort studies (Piccoli et al., 2020; Robbiani et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Piccoli et al., 2020
Asymptomatic SARS-CoV-2 cases tend to have lower Spike and nucleocapsid IgG titers, and it is plausible that they are enriched for individuals with undetectable antibodies by commercial serological assays but circulating SARS-CoV-2 T cells.
“Given that asymptomatic cases of SARS-CoV-2 infection tend to have lower Spike and nucleocapsid IgG titers (Piccoli et al., 2020), it is plausible that asymptomatic cases are enriched for individuals with undetectable antibodies by commercial serological assays but possess circulating SARS-CoV-2 T cells”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Piccoli et al., 2020
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- Katoh K. Rozewicki J. Yamada K.D. MAFFT online service: multiple sequence alignment, interactive sequence choice and visualization Briefings in Bioinformatics 20 2019 1160 1166 28968734 PMC6781576
- Luchsinger L.L. Ransegnola B. Jin D. Muecksch F. Weisblum Y. Bao W. George P.J. Rodriguez M. Tricoche N. Schmidt F. Serological Analysis of New York City COVID19 Convalescent Plasma Donors medRxiv 2020 10.1101/2020.06.08.20124792 · DOI
- Robbiani D.F. Gaebler C. Muecksch F. Lorenzi J.C.C. Wang Z. Cho A. Agudelo M. Barnes C.O. Gazumyan A. Finkin S. Convergent antibody responses to SARS-CoV-2 in convalescent individuals Nature 584 2020 437 442 32555388 PMC7442695
- Rogers T.F. Zhao F. Huang D. Beutler N. Burns A. He W.T. Limbo O. Smith C. Song G. Woehl J. Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model Science 369 2020 956 963 32540903 PMC7299280
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Odainic, A., Vardaxis, I., Ferraz, M., Wiese, K. E., Cornelissen, L. A. H. M., Sharma, A., Stratford, R., Clancy, T., & Bendjama, K. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1919664
Endemicity of SARS-CoV-2 Omicron Subvariants Is Changing Long COVID
musachia, J. (2026) · COVID · doi:10.3390/covid6100174
Mao, S., Meng, S., & Xiang, Y. (2026) · iScience · doi:10.1016/j.isci.2026.117693
Wang, S., Zhang, X., Zhang, H., Rao, G., Yao, Y., Tian, G., Gao, G., Yun, P., Li, W., Cao, S., et al. (2026) · Virologica Sinica · doi:10.1016/j.virs.2026.09.014
Water treatment research opportunities at synchrotron and neutron user facilities
Landsman, M. R., Hesse, S. A., Göktürk, P. A., Yao, C., Bechtel, H. A., Dudchenko, A. V., Hexemer, A., Jiang, Z., Katz, L. E., Kumar, M., et al. (2026) · Nature Water · doi:10.1038/s44221-026-00723-9
Cui, Z., Wu, W., Lai, Y., Liu, T., Dou, F., Yang, L., & Zou, G. (2026) · Advanced Biology · doi:10.1002/adbi.70163
Tingting, X., Jiang, Y., Li, C., Chen, H., Zhang, Z., Zhang, H., Qiu, Y., & Zhou, L. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1967945
Kochmann, J., Halwe, N. J., Barut, G. T., Ebert, N., Thiel, V., Dorhoi, A., Hoffmann, D., Beer, M., Schön, J., & Corleis, B. (2026) · Vaccine · doi:10.1016/j.vaccine.2026.129298
- Authors
- Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., Acton, O. J., Jaconi, S., Guarino, B., Minola, A., Zatta, F., Sprugasci, N., Bassi, J., Peter, A., De Marco, A., Nix, J. C., Mele, F., Jovic, S., Rodriguez, B. F., Gupta, S. V., Jin, F., Piumatti, G., Lo Presti, G., Pellanda, A. F., Biggiogero, M., Tarkowski, M., Pizzuto, M. S., Cameroni, E., Havenar-Daughton, C., Smithey, M., Hong, D., Lepori, V., Albanese, E., Ceschi, A., Bernasconi, E., Elzi, L., Ferrari, P., Garzoni, C., Riva, A., Snell, G., Sallusto, F., Fink, K., Virgin, H. W., Lanzavecchia, A., Corti, D., & Veesler, D.
- Affiliations
- Vir Biotechnology (Switzerland) (CH)
- University of Washington (US)
- Centre National de la Recherche Scientifique (FR)
- VIR Biotechnology (United States) (US)
- Lawrence Berkeley National Laboratory (US)
- Institute for Research in Biomedicine (CH)
- University Hospital of Geneva (CH)
- Clinica Luganese Moncucco (CH)
- Luigi Sacco Hospital (IT)
- Università della Svizzera italiana (CH)
- Ente Ospedaliero Cantonale (CH)
- UNSW Sydney (AU)
- Corresponding author
- Corti, Davide
- Veesler, David
- ORCID
- Piccoli, Luca
- Park, Young-Jun
- Tortorici, M. Alejandra
- Czudnochowski, Nadine
- Walls, Alexandra C.
- Beltramello, Martina
- Pinto, Dora
- Rosen, Laura E.
- Bowen, John E.
- Acton, Oliver J.
- Jaconi, Stefano
- Guarino, Barbara
- Zatta, Fabrizia
- Sprugasci, Nicole
- Bassi, Jessica
- Peter, Alessia
- Nix, Jay C.
- Mele, Federico
- Jovic, Sandra
- Gupta, Sneha V.
- Piumatti, Giovanni
- Tarkowski, Maciej
- Pizzuto, Matteo S.
- Cameroni, Elisabetta
- Smithey, Megan
- Hong, David
- Albanese, Emiliano
- Ceschi, Alessandro
- Bernasconi, Enos
- Elzi, Luigia
- Ferrari, Paolo
- Garzoni, Christian
- Riva, Agostino
- Snell, Gyorgy
- Sallusto, Federica
- Fink, Katja
- Virgin, Herbert W.
- Lanzavecchia, Antonio
- Corti, Davide
- Veesler, David
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-11
- Volume
- 183
- Issue
- 4
- Pages
- 1024-1042.e21
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7494283
- OpenAlex
- W3086125063
- Cited by
- 1,395
- References
- 0
- Citations by year
- 2026: 65 · 2025: 107 · 2024: 172 · 2023: 223 · 2022: 396 · 2021: 409 · 2020: 22
- FWCI
- 34.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 376 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
- eScholarship (California Digital Library) (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- UNSWorks (University of New South Wales, Sydney, Australia) (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute of General Medical Sciences
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
- Keywords
- SARS-CoV-2, spike protein, receptor binding domain, neutralizing antibodies, immunodominant epitopes, antigenic mapping, antibody avidity, affinity maturation, antibody waning, nucleoprotein antibodies, COVID-19 vaccine design
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Antibodies, Monoclonal, Antibodies, Viral, Antigen-Antibody Reactions, Epitopes, Binding Sites, Humans, Immunoglobulin A, Immunoglobulin G, Immunoglobulin M, Kinetics, Peptidyl-Dipeptidase A, Pneumonia, Viral, Protein Binding, Coronavirus Infections, Epitope Mapping, Protein Structure, Quaternary, Molecular Dynamics Simulation, Antibodies, Neutralizing, Pandemics, Spike Glycoprotein, Coronavirus
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