Cited by 187SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections Studiesvaccines and immunoinformatics approaches

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Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines

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Walls, Alexandra C., Miranda, Marcos C., Schäfer, Alexandra, Pham, Minh N., Greaney, Allison, Arunachalam, Prabhu S., Navarro, Mary-Jane, Tortorici, M. Alejandra, Rogers, Kenneth, O’Connor, Megan A., Shirreff, Lisa, Ferrell, Douglas E., Bowen, John, Brunette, Natalie, Kepl, Elizabeth, Zepeda, Samantha K., Starr, Tyler, Hsieh, Ching-Lin, Fiala, Brooke, Wrenn, Samuel, Pettie, Deleah, Sydeman, Claire, Sprouse, Kaitlin R., Johnson, Max, Blackstone, Alyssa, Ravichandran, Rashmi, Ogohara, Cassandra, Carter, Lauren, Tilles, Sasha W., Rappuoli, Rino, Leist, Sarah R., Martinez, David R., Clark, Matthew, Tisch, Roland, O’Hagan, Derek T., Van Der Most, Robbert, Van Voorhis, Wesley C., Corti, Davide, McLellan, Jason S., Kleanthous, Harry, Sheahan, Timothy P., Smith, Kelly D., Fuller, Deborah H., Villinger, Francois, Bloom, Jesse, Pulendran, Bali, Baric, Ralph S., King, Neil P., Veesler, David·2021·Cell

DOI 10.1016/j.cell.2021.09.015PMC PMC7986998

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Abstract

Understanding the ability of SARS-CoV-2 vaccine-elicited antibodies to neutralize and protect against emerging variants of concern and other sarbecoviruses is key for guiding vaccine development decisions and public health policies. We show that a clinical stage multivalent SARS-CoV-2 receptor-binding domain nanoparticle vaccine (SARS-CoV-2 RBD-NP) protects mice from SARS-CoV-2-induced disease after a single shot, indicating that the vaccine could allow dose-sparing. SARS-CoV-2 RBD-NP elicits high antibody titers in two non-human primate (NHP) models against multiple distinct RBD antigenic sites known to be recognized by neutralizing antibodies. We benchmarked NHP serum neutralizing activity elicited by RBD-NP against a lead prefusion-stabilized SARS-CoV-2 spike immunogen using a panel of single-residue spike mutants detected in clinical isolates as well as the B.1.1.7 and B.1.351 variants of concern. Polyclonal antibodies elicited by both vaccines are resilient to most RBD mutations tested, but the E484K substitution has similar negative consequences for neutralization, and exhibit modest but comparable neutralization breadth against distantly related sarbecoviruses. We demonstrate that mosaic and cocktail sarbecovirus RBD-NPs elicit broad sarbecovirus neutralizing activity, including against the SARS-CoV-2 B.1.351 variant, and protect mice against severe SARS-CoV challenge even in the absence of the SARS-CoV RBD in the vaccine. This study provides proof of principle that sarbecovirus RBD-NPs induce heterotypic protection and enables advancement of broadly protective sarbecovirus vaccines to the clinic.

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Result
Sustained exposure to multivalent antigen-decorated nanoparticles generates broad anti-coronavirus responses
Baillet, J., Klich, J. H., Ou, B. S., Meany, E. L., Yan, J., Bruun, T. U. J., Utz, A., Jons, C. K., Lecommandoux, S., & Appel, E. A. (2025) · Matter · doi:10.1016/j.matt.2025.102006 · Cited by 4
Development of robust, indigenous ELISA for detection of IgG antibodies against CoV-2 N and S proteins: mass screening
Srivastava, A. K., Gupta, A., Chauhan, D., Meena, R. C., Sugadev, R., Eslavath, M. R., Gupta, H., Karuna, K., Singh, S., Singh, Y., et al. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12113-8 · Cited by 4
Human neutralizing antibodies to cold linear epitopes and to subdomain 1 of SARS-CoV-2Preprint
Bianchini, F., Crivelli, V., Abernathy, M. E., Guerra, C., Palus, M., Muri, J., Marcotte, H., Piralla, A., Pedotti, M., Gasparo, R. D., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.24.515932 · Cited by 4
A Multivalent Pan-Ebolavirus Nanoparticle Vaccine Provides Protection in Rodents from Lethal Infection by Adapted Zaire and Sudan VirusesPreprint
Brunette, N., Weidle, C., Wrenn, S. P., Fiala, B., Ravichandran, R., Carr, K. D., Zak, S. E., Zumbrun, E. E., Bakken, R. R., Murphy, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.29.635581 · Cited by 4
“The naked I53-50 nanoparticle chassis samples have been produced and purified on numerous occasions 19,22,23,25,26,34 .”
InfluentialSelf-citation
Phylogeny-driven design of broadly protective sarbecovirus receptor-binding domain nanoparticle vaccinesPreprint
Addetia, A., Schäfer, A., Sprouse, K. R., Valdez, A., Taylor, A., Navarro, M.-J., Brown, J. T., Leaf, E. M., Miranda, M. C., Walls, A. C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.11.652904 · Cited by 4
Self-citation
Multivalent Vaccine Strategies in Battling the Emergence of COVID-19 Variants
Guest, P. C. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2395-4_2 · Cited by 3
Characterization of cross‐reactive monoclonal antibodies against SARS‐CoV‐1 and SARS‐CoV‐2: Implication for rational design and development of pan‐sarbecovirus vaccines and neutralizing antibodies
Li, S., Wu, J., Jiang, W., He, H., Zhou, Y., Wu, W., Gao, Y., Xie, M., Xia, A., He, J., et al. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28440 · Cited by 3
Vaccination strategy for preventing the spread of SARS‐CoV‐2 in the limited supply condition: A mathematical modeling study
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“Moreover, how to cope with the evolution of the SARS‐CoV‐2 and develop a vaccine with a "broad‐spectrum effect" in avoiding virus escape is an important problem that researchers need to urgently solve.(56,57) The variants reduced the VE to varying degrees, but the vaccine is still protective.”
Background
Production of Clinical-Grade SARS-CoV-2 Spike Ferritin Nanoparticle Protein Immunogen by Transient Transfection
Hajduczki, A., Chang, W. C., Barrera, R. A. D. L., Wood, J. F., Chen, W.-H., Martinez, E. J., Jensen, J. L., Sankhala, R. S., Smith, C., Anderson, A., et al. (2025) · Vaccines · doi:10.3390/vaccines13101041 · Cited by 2
“The laboratory-scale SpFN was purified using lectin affinity followed by size exclusion chromatography, similar to other viral glycoprotein vaccine candidates [13,37–39].”
Heterologous betacoronavirus spike immunization in non-human primates elicits antibodies that neutralize both sarbeco- and merbecoviruses
Dueker, K., Capozzola, T., Feng, Z., Lin, R. N., Hurtado, J., Bangaru, S., Yuan, M., Beutler, N., Garcia, E., He, W.-T., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117439 · Cited by 2
Protein engineering: status report
Ai, H., Arnold, F. H., Barrick, D., Bayley, H., Brownless, A.-L. R., Campbell, R. E., Castells‐Graells, R., Chaiyen, P., Chica, R. A., Chisholm, L. O., et al. (2026) · Protein Engineering Design and Selection · doi:10.1093/protein/gzag020 · Cited by 2
Humoral responses to the SARS-CoV-2 spike and receptor binding domain in context of pre-existing immunity confer broad sarbecovirus neutralization
Hauser, B. M., Sangesland, M., Lam, E. C., Feldman, J. E., Balazs, A. B., Lingwood, D., & Schmidt, A. G. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.902260 · Cited by 2
Innovation-driven trend shaping COVID-19 vaccine development in China
Zhang, Y., Zhao, Y., Liang, H., Xu, Y. M., Zhou, C., Yao, Y., Wang, H., & Yang, X. (2023) · Frontiers of Medicine · doi:10.1007/s11684-023-1034-6 · Cited by 2
Low-dose bivalent mRNA vaccine is highly effective against different SARS-CoV-2 variants in a transgenic mouse modelPreprint
Corleis, B., Hoffmann, D., Rauch, S., Fricke, C., Roth, N., Gergen, J., Kovacikova, K., Schlottau, K., Halwe, N. J., Ulrich, L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.20.485440 · Cited by 2
Rational Design of Multiclade Coronavirus Spike Immunodominant Domain Nanoparticles to Elicit Broad Antibody ResponsesPreprint
Dzuvor, C. K. O., Moak, S. P., McManus, L. R., Thomas, A., Dzordzorme, A. E., Kim, T., Joseph, J., Foley, V., Gordon, I. J., Novik, L., et al. (2025) · Research Square · doi:10.1101/2025.10.01.679649 · Cited by 2
Spatial Engineering of Heterotypic Antigens on a DNA Framework for the Preparation of Mosaic Nanoparticle Vaccines with Enhanced Immune Activation against SARS‐CoV‐2 Variants
Zhang, J., Xu, Y., Chen, M., Wang, S., Lin, G., Huang, Y., Yang, C. J., Yang, Y., & Song, Y. (2024) · Angewandte Chemie · doi:10.1002/ange.202412294 · Cited by 1
A SARS‐CoV and SARS‐CoV‐2 RBD Heterodimer Vaccine Candidate
Zhang, R., Li, D., Gao, P., Ruan, W., Qiao, S., Xu, S., Dai, L., Luo, T., Zhao, X., & Gao, G. F. (2025) · Journal of Medical Virology · doi:10.1002/jmv.70367 · Cited by 1
Characterization of the Binding and Inhibition Mechanisms of a Novel Neutralizing Monoclonal Antibody Targeting the Stem Helix Region in the S2 Subunit of the Spike Protein of SARS-CoV-2
Tan, S. S. E., Tam, E.-H., Lai, K. M., Wu, Y., Xiao, T., & Tan, Y. (2025) · Vaccines · doi:10.3390/vaccines13070688 · Cited by 1
“GBP511 also contains RBD from SARS-CoV-2 and different animal coronavirus, and showed protection against animal sarbecoviruses and SARS-CoV-1 infection [48].”
Vaccine-derived T-cell responses are insufficient to generate protective immunity to SARS-CoV-2
Cha, S.-C., Szymura, S. J., Anderson, A., Dong, Z., Kandel, A., Oh, E., Palmer, M., Arango, K., Zhang, J., & Kwak, L. W. (2026) · Scientific Reports · doi:10.1038/s41598-026-44391-x · Cited by 1
“Similarly, recombinant prefusion-stabilized Spike proteins, formulated with potent adjuvants such as the saponin-based Matrix-M employed in NVX-CoV2373, have exhibited robust neutralizing activity and demonstrated clinical efficacy 33, 34 .”
Heterologous saRNA prime – multivalent protein boost strategy induces broad and durable immunity against SARS-CoV-2 and MERS-CoV
Renn, D., McPartlan, J. S., Banala, S., Kiessling, F. M., Talukder, P., Mandl, C. W., Eppinger, J., Chahal, J. S., & Rueping, M. (2026) · Scientific Reports · doi:10.1038/s41598-026-44645-8 · Cited by 1
“The multivalent RBD booster appeared to preferentially expand cross-reactive lineages that recognize conserved RBD epitopes 61,62 , while preserving potent homologous responses, a pattern previously reported in mixed-antigen nanoparticle vaccines 63,64 .”
Macaque-human differences in SARS-CoV-2 Spike antibody response elicited by vaccination or infectionPreprint
Willcox, A. C., Sung, K., Garrett, M. E., Galloway, J., O’Connor, M. A., Erasmus, J. H., Logue, J. K., Hawman, D. W., Chu, H. Y., Hasenkrug, K. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.01.470697 · Cited by 1
Self-citation
Virus-like particle displaying SARS-CoV-2 receptor binding domain elicits neutralizing antibodies and is protective in a challenge modelPreprint
McKechnie, J. L., Fiala, B., Wolf, C., Ellis, D., Holtzman, D. A., & Feldhaus, A. L. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.29.518404 · Cited by 1
“381 These data for IVX-411 are consistent with a large number of preclinical studies on I53382 50 immunogens displaying RBD antigens from SARS-CoV-2 and/or other sarbecoviruses 383 [24,31,38], and further demonstrate the precision and immunogenic potency of this platform.”
ResultSelf-citation
Design of a Streptolysin O Epitope-Centric Nanoparticle Vaccine Against Streptococcus pyogenesPreprint
Tang, D., Chao, Y., Hjortswang, E., Ströbaek, J., Hultgren, L., Mohanty, T., Karlsson, C. A. Q., Ekström, S., Happonen, L., Shannon, O., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.25.655993 · Cited by 1
Protective pan-betacoronavirus neutralizing antibodies by vaccinationPreprint
Zhou, P.-P., Feng, Z., He, W.-T., Zhu, Y., Yuan, M., Li, X., Zhang, Y., Vo, L., Capozzola, T., Callaghan, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.06.743418 · Cited by 1
Self-citation
Coronavirus Pandemics Era and Cancer Patients
Tomás, M. (2021) · Revista Brasileira de Cancerologia · doi:10.32635/2176-9745.rbc.2021v67n4.2430
Mosaic receptor-binding domain nanoparticles induce protective immunity against SARS-CoV-2 challengesPreprint
Lee, D. B., Kim, H., Jeong, J. H., Jang, U. S., Chang, Y. Y., Roh, S., Jeon, H., Kim, E. J., Han, S. Y., Maeng, J. Y., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.18.480994
Tiny particles could make a powerful COVID vaccine
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Viral infection and immunity view of SARS-CoV-2 using RBD-assembled DNA Soccer-ball FrameworkPreprint
Zhang, J., Xu, Y., Chen, M., Huang, Y., Song, T., Yang, C. J., Yang, Y., & Song, Y. (2022) · ChemRxiv · doi:10.26434/chemrxiv-2022-wwxr7
Engineering a SARS-CoV-2 vaccine targeting the RBD cryptic-face via immunofocusingPreprint
Bruun, T. U. J., Do, J., Weidenbacher, P. A. B., & Kim, P. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.05.597541
Development of Plant-Based Multivalent Vaccine Candidates for SARS-CoV-2 and Influenza Virus Using Inactivated Lactococcus
Lee, D.-S., Banna, H., Kim, H., Khan, M. R. I., Diao, H., Song, S., Kim, Y.-E., Kang, H. J., Ryou, J., Lee, J.-Y., et al. (2025) · Vaccines · doi:10.3390/vaccines13030254
“The full-length S protein offers distinct advantages, particularly because it contains conserved T-cell epitopes within its S2 domain, which have the potential to provide cross-protection against emerging viral variants—an essential feature considering the ongoing viral evolution [36].”
Heterologous saRNA Prime – Multivalent Protein Boost Strategy Induces Broad and Durable Immunity Against SARS-CoV-2 and MERS-CoVPreprint
Renn, D., McPartlan, J. S., Banala, S., Kiessling, F. M., Taldukder, P., Mandl, C. W., Chahal, J. S., Eppinger, J., & Rueping, M. (2025) · Research Square · doi:10.21203/rs.3.rs-7875217/v1
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Development of a Thermostable and Broadly Neutralizing Pan-Sarbecovirus Vaccine Candidate
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The BP26-OMP16Es Nanoparticle Vaccine Elicits Protective Immunity against Brucella
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CELL2025_Grifoni
Grifoni, A. (2026) · ImmPort · doi:10.21430/m37vglvr69

Authors: Walls, A. C., Miranda, M. C., Schäfer, A., Pham, M. N., Greaney, A., Arunachalam, P. S., Navarro, M.-J., Tortorici, M. A., Rogers, K., O’Connor, M. A., Shirreff, L., Ferrell, D. E., Bowen, J., Brunette, N., Kepl, E., Zepeda, S. K., Starr, T., Hsieh, C.-L., Fiala, B., Wrenn, S., Pettie, D., Sydeman, C., Sprouse, K. R., Johnson, M., Blackstone, A., Ravichandran, R., Ogohara, C., Carter, L., Tilles, S. W., Rappuoli, R., Leist, S. R., Martinez, D. R., Clark, M., Tisch, R., O’Hagan, D. T., Van Der Most, R., Van Voorhis, W. C., Corti, D., McLellan, J. S., Kleanthous, H., Sheahan, T. P., Smith, K. D., Fuller, D. H., Villinger, F., Bloom, J., Pulendran, B., Baric, R. S., King, N. P., & Veesler, D.
Affiliations: University of Washington (US)
University of North Carolina at Chapel Hill (US)
Stanford University (US)
Centre National de la Recherche Scientifique (FR)
University of Louisiana at Lafayette (US)
Fred Hutch Cancer Center (US)
The University of Texas at Austin (US)
GlaxoSmithKline (Italy) (IT)
Vir Biotechnology (Switzerland) (CH)
Gates Foundation (US)
Corresponding author: King, Neil P.
Veesler, David
ORCID: Walls, Alexandra C.
Miranda, Marcos C.
Schäfer, Alexandra
Pham, Minh N.
Greaney, Allison
Arunachalam, Prabhu S.
Navarro, Mary-Jane
Tortorici, M. Alejandra
Rogers, Kenneth
O’Connor, Megan A.
Shirreff, Lisa
Ferrell, Douglas E.
Bowen, John
Brunette, Natalie
Kepl, Elizabeth
Zepeda, Samantha K.
Starr, Tyler
Hsieh, Ching-Lin
Fiala, Brooke
Wrenn, Samuel
Pettie, Deleah
Sprouse, Kaitlin R.
Johnson, Max
Ravichandran, Rashmi
Carter, Lauren
Tilles, Sasha W.
Rappuoli, Rino
Leist, Sarah R.
Martinez, David R.
Clark, Matthew
Tisch, Roland
Corti, Davide
McLellan, Jason S.
Kleanthous, Harry
Sheahan, Timothy P.
Smith, Kelly D.
Fuller, Deborah H.
Villinger, Francois
Bloom, Jesse
Pulendran, Bali
Baric, Ralph S.
King, Neil P.
Veesler, David
Venue: Cell
Publisher: Elsevier BV
Published: 2021-10
Volume: 184
Issue: 21
Pages: 5432-5447.e16
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2021.09.015
PMC: PMC7986998
OpenAlex: W3199882158
Cited by: 185
References: 116
Citations by year: 2026: 15 · 2025: 24 · 2024: 27 · 2023: 35 · 2022: 59 · 2021: 25
FWCI: 11.55
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 378 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, cc-by)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
PubMed Central (submittedVersion, cc-by-nc-nd)
Funders: Burroughs Wellcome Fund (U01 AI149644, HHSN272201700036I-75N93020F00001)
Howard Hughes Medical Institute
Defense Threat Reduction Agency (HDTRA1-18-1-0001)
National Institute of General Medical Sciences (R01GM120553)
Bill and Melinda Gates Foundation (017592, OPP1156262, INV\u2013017592)
Pfizer
University of Washington
Gilead Sciences
GlaxoSmithKline (63/032,502)
North Carolina General Assembly
National Institute of Allergy and Infectious Diseases (DP1AI158186, F32 AI152296, T32 AI007151, R01-AI127521, 5T32GM008268-32, HHSN272201700059C)
Office of Research Infrastructure Programs, National Institutes of Health (P51-OD010425)
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Keywords: Sarbecovirus, SARS-CoV-2, receptor binding domain, nanoparticle vaccine, multivalent vaccine, heterologous protection, neutralizing antibodies, SARS-CoV, spike protein mutations, mosaic vaccine, dose sparing, non-human primates

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Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines

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