Imprinted antibody responses against SARS-CoV-2 Omicron sublineages
Open accessPreprint — published as 10.1126/science.adc9127
Abstract
SARS-CoV-2 Omicron sublineages carry distinct spike mutations and represent an antigenic shift resulting in escape from antibodies induced by previous infection or vaccination. We show that hybrid immunity or vaccine boosters result in potent plasma neutralizing activity against Omicron BA.1 and BA.2 and that breakthrough infections, but not vaccination-only, induce neutralizing activity in the nasal mucosa. Consistent with immunological imprinting, most antibodies derived from memory B cells or plasma cells of Omicron breakthrough cases cross-react with the Wuhan-Hu-1, BA.1 and BA.2 receptor-binding domains whereas Omicron primary infections elicit B cells of narrow specificity. While most clinical antibodies have reduced neutralization of Omicron, we identified an ultrapotent pan-variant antibody, that is unaffected by any Omicron lineage spike mutations and is a strong candidate for clinical development.
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Over reliance on immune memory may impact the breadth and strength of antibody and B-cell immunity as new antigenically drifted variants arise.
“Over reliance on immune memory may impact the breadth and strength of antibody and B-cell immunity as new antigenically drifted variants arise 15,21,32,33 .”
From Rapidly shifting immunologic landscape and severity of SARS-CoV-2 in the Omicron era in South Africa (2023) · cites this paper as [32]
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Self-citationSARS-CoV-2 breakthrough infections elicit potent, broad, and durable neutralizing antibody responses
Walls, A. C., Sprouse, K. R., Bowen, J. E., Joshi, A., Franko, N., Navarro, M. J., Stewart, C., Cameroni, E., McCallum, M., Goecker, E. A., et al. (2022) · Cell · doi:10.1016/j.cell.2022.01.011 · Cited by 185 · see citing works
Self-citationA single-dose live-attenuated YF17D-vectored SARS-CoV-2 vaccine candidate
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Self-citationChimeric spike mRNA vaccines protect against Sarbecovirus challenge in mice
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ACE2-binding exposes the SARS-CoV-2 fusion peptide to broadly neutralizing coronavirus antibodies
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Self-citationEmergence of Omicron third lineage BA.3 and its importance
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Self-citationAntibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry
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Richardson, S. I., Madzorera, V. S., Spencer, H., Manamela, N. P., van der Mescht, M. A., Lambson, B. E., Oosthuysen, B., Ayres, F., Makhado, Z., Moyo-Gwete, T., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.03.029 · Cited by 119 · see citing works
LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variantsPreprint
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Automatically Fixing Errors in Glycoprotein Structures with Rosetta
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Self-citationProtection against SARS-CoV-2 Beta variant in mRNA-1273 vaccine–boosted nonhuman primates
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Neutralization Profile after Recovery from SARS-CoV-2 Omicron Infection
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Antibody Response and Variant Cross-Neutralization After SARS-CoV-2 Breakthrough Infection
Bates, T. A., McBride, S. K., Winders, B., Schoen, D., Trautmann, L., Curlin, M. E., & Tafesse, F. (2021) · JAMA · doi:10.1001/jama.2021.22898 · Cited by 91 · see citing works
Omicron sub-lineages BA.4/BA.5 escape BA.1 infection elicited neutralizing immunityPreprint
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Hassan, A. O., Feldmann, F., Zhao, H.-Y., Curiel, D., Okumura, A., Tang-Huau, T.-L., Case, J., Meade-White, K., Callison, J. A., Chen, R. E., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100230 · Cited by 85 · see citing works
Continued Emergence and Evolution of Omicron in South Africa: New BA.4 and BA.5 lineagesPreprint
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Self-citationSARS-CoV-2 Omicron sublineages exhibit distinct antibody escape patterns
Gruell, H., Vanshylla, K., Korenkov, M., Tober‐Lau, P., Zehner, M., Münn, F., Janicki, H., Augustin, M., Schommers, P., Sander, L. E., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.002 · Cited by 75 · see citing works
Molecular basis of immune evasion by the delta and kappa SARS-CoV-2 variantsPreprint
McCallum, M., Walls, A. C., Sprouse, K. R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.11.455956 · Cited by 74 · see citing works
Self-citationBreadth of SARS-CoV-2 neutralization and protection induced by a nanoparticle vaccine
Li, D., Martinez, D. R., Schäfer, A., Chen, H., Barr, M., Sutherland, L. L., Lee, E., Parks, R., Mielke, D., Edwards, W., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33985-4 · Cited by 67 · see citing works
Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shiftPreprint
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Self-citationShifting mutational constraints in the SARS-CoV-2 receptor-binding domain during viral evolutionPreprint
Starr, T. N., Greaney, A. J., Hannon, W. W., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.24.481899 · Cited by 49 · see citing works
Comparative neutralisation profile of SARS-CoV-2 omicron subvariants BA.2.75 and BA.5
Tan, C. W., Lim, B. L., Young, B. E., Yeoh, A. Y.-Y., Yung, C.-F., Yap, W. C., Althaus, T., Chia, W., Zhu, F., Lye, D. C., et al. (2022) · The Lancet Microbe · doi:10.1016/s2666-5247(22)00220-8 · Cited by 46 · see citing works
Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagementPreprint
McCallum, M., Czudnochowski, N., Rosen, L. E., et al. (2021) · bioRxiv · doi:10.1101/2021.12.28.474380 · Cited by 41 · see citing works
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Omicron BA.1 and BA.2 neutralizing activity elicited by a comprehensive panel of human vaccinesPreprint
Bowen, J. E., Sprouse, K. R., Walls, A. C., Mazzitelli, I. G., Logue, J. K., Franko, N., Ahmed, K., Ansari, A. S., Cameroni, E., Gori, A., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.15.484542 · Cited by 38 · see citing works
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Different Neutralization Profiles After Primary SARS-CoV-2 Omicron BA.1 and BA.2 Infections
Medits, I., Springer, D. N., Graninger, M., Camp, J. V., Höltl, E., Aberle, S. W., Traugott, M. T., Hoepler, W., Deutsch, J., Lammel, O., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.946318 · Cited by 36 · see citing works
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de Melo, G. D., Lazarini, F., Levallois, S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.18.388819 · Cited by 29 · see citing works
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Safety, Immunogenicity and Antibody Persistence of a Bivalent Beta-Containing Booster VaccinePreprint
Chalkias, S., Eder, F. S., Essink, B. J., Khetan, S. K., Nestorova, B., Feng, J., Chen, X., Chang, Y., Zhou, H., Montefiori, D. C., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1555201/v1 · Cited by 22 · see citing works
SARS-CoV-2 spike conformation determines plasma neutralizing activityPreprint
Bowen, J. E., Walls, A. C., Joshi, A., Sprouse, K. R., Stewart, C., Tortorici, M. A., Franko, N., Logue, J. K., Mazzitelli, I. G., Tilles, S. W., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.19.473391 · Cited by 21 · see citing works
Self-citationDifferential escape of neutralizing antibodies by SARS-CoV-2 Omicron and pre-emergent sarbecovirusesPreprint
Wang, L., Tan, C. W., Chia, W. N., Zhu, F., Young, B. E., Chantasrisawad, N., Hwa, S.-H., Yeoh, A. Y.-Y., Lim, B. L., Yap, W. C., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1362541/v1 · Cited by 13 · see citing works
Delineating antibody escape from Omicron sublineagesPreprint
Gruell, H., Vanshylla, K., Korenkov, M., Tober‐Lau, P., Zehner, M., Münn, F., Janicki, H., Augustin, M., Schommers, P., Sander, L. E., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.06.487257 · Cited by 13 · see citing works
Omicron breakthrough infection drives cross-variant neutralization and memory B cell formationPreprint
Quandt, J., Muik, A., Salisch, N. C., Lui, B. G., Lutz, S., Krüger, K., Wallisch, A.-K., Adams‐Quack, P., Bacher, M., Finlayson, A., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.01.486695 · Cited by 10 · see citing works
Human primary Omicron BA.1 and BA.2 infections result in sub-lineage-specific neutralizationPreprint
Stiasny, K., Medits, I., Springer, D. N., Graninger, M., Camp, J. V., Höltl, E., Aberle, S. W., Traugott, M. T., Hoepler, W., Deutsch, J., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1536794/v1 · Cited by 8 · see citing works
Durable protection against SARS-CoV-2 Omicron induced by an adjuvanted subunit vaccinePreprint
Arunachalam, P. S., Feng, Y., Ashraf, U., Hu, M., Edara, V. V., Zarnitsyna, V. I., Aye, P. P., Golden, N., Green, K. M., Threeton, B., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.18.484950 · Cited by 5 · see citing works
Self-citationACE2 engagement exposes the fusion peptide to pan-coronavirus neutralizing antibodiesPreprint
Low, J., Jerak, J., Tortorici, M. A., et al. (2022) · bioRxiv · doi:10.1101/2022.03.30.486377 · Cited by 5 · see citing works
Mosaic RBD nanoparticles protect against multiple sarbecovirus challenges in animal modelsPreprint
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J., Fan, C.-H., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · bioRxiv · doi:10.1101/2022.03.25.485875 · Cited by 5 · see citing works
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Rapidly shifting immunologic landscape and severity of SARS-CoV-2 in the Omicron era in South Africa
Sun, K., Tempia, S., Kleynhans, J., von Gottberg, A., McMorrow, M. L., Wolter, N., Bhiman, J. N., Moyes, J., Carrim, M., Martinson, N. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-022-35652-0 · Cited by 45 · see citing works
- Authors
- Park, Y.-J., Pinto, D., Walls, A. C., Liu, Z., De Marco, A., Benigni, F., Zatta, F., Silacci-Fregni, C., Bassi, J., Sprouse, K. R., Addetia, A., Bowen, J. E., Stewart, C., Giurdanella, M., Saliba, C., Guarino, B., Schmid, M. A., Franko, N., Logue, J., Dang, H. V., Hauser, K., di Iulio, J., Rivera, W., Schnell, G., Rajesh, A., Zhou, J., Farhat, N., Kaiser, H., Montiel-Ruiz, M., Noack, J., Lempp, F. A., Janer, J., Abdelnabi, R., Maes, P., Ferrari, P., Ceschi, A., Giannini, O., Dias de Melo, G., Kergoat, L., Bourhy, H., Neyts, J., Soriaga, L., Purcell, L. A., Snell, G., Whelan, S. P. J., Lanzavecchia, A., Virgin, H. W., Piccoli, L., Chu, H., Pizzuto, M. S., Corti, D., & Veesler, D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Vir Biotechnology (Switzerland) (CH)
- Washington University in St. Louis (US)
- University of Washington (US)
- VIR Biotechnology (United States) (US)
- Rega Institute for Medical Research (BE)
- UNSW Sydney (AU)
- Ente Ospedaliero Cantonale (CH)
- Institut Pasteur (FR)
- Corresponding author
- Corti, Davide
- Veesler, David
- ORCID
- Park, Young-Jun
- Pinto, Dora
- Walls, Alexandra C.
- Liu, Zhuoming
- Benigni, Fabio
- Zatta, Fabrizia
- Bassi, Jessica
- Sprouse, Kaitlin R.
- Addetia, Amin
- Bowen, John E.
- Stewart, Cameron
- Saliba, Christian
- Guarino, Barbara
- Schmid, Michael A.
- Franko, Nicholas
- Logue, Jennifer
- Dang, Ha V.
- Hauser, Kevin
- Rajesh, Anushka
- Zhou, Jiayi
- Farhat, Nisar
- Kaiser, Hannah
- Montiel-Ruiz, Martin
- Noack, Julia
- Lempp, Florian A.
- Janer, Javier
- Abdelnabi, Rana
- Maes, Piet
- Ferrari, Paolo
- Ceschi, Alessandro
- Giannini, Olivier
- Kergoat, Lauriane
- Bourhy, Hervé
- Neyts, Johan
- Soriaga, Leah
- Purcell, Lisa A.
- Snell, Gyorgy
- Whelan, Sean P.J.
- Lanzavecchia, Antonio
- Virgin, Herbert W.
- Piccoli, Luca
- Chu, Helen
- Pizzuto, Matteo Samuele
- Corti, Davide
- Veesler, David
- Venue
- Science
- Publisher
- openRxiv
- Published
- 2022-05-10
- Volume
- 378
- Issue
- 6620
- Pages
- 619-627
- ISSN
- 0036-8075 (ISSN-L)
- PMC
- PMC9176643
- OpenAlex
- W4306902076
- Cited by
- 251
- References
- 129
- Citations by year
- 2026: 28 · 2025: 50 · 2024: 62 · 2023: 83 · 2022: 28
- FWCI
- 27.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, other-oa)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, cc-by)
- HAL (submittedVersion, cc-by)
- Lirias (KU Leuven) (submittedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (1s10od023476-01)
- National Institute of Allergy and Infectious Diseases (DP1AI158186, 75N93022C00036, R01AI163019)
- 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
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- immunological imprinting, neutralizing antibodies, spike protein mutations, antibody escape, hybrid immunity, booster vaccination, breakthrough infection, nasal mucosa, memory B cells, receptor binding domain, Omicron BA.4/BA.5
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.
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