Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines
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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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Prototypes of multivalent nanoparticle vaccines induce broad reactivity against different sarbecoviruses.
“For example, prototypes of multivalent nanoparticle vaccines have been reported to induce broad reactivity against different sarbecoviruses7.”
From Efficacy of an unmodified bivalent mRNA vaccine against SARS-CoV-2 variants in female small animal models (2023) · cites this paper as [7]
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Self-citationN-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
Self-citationSARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo
Hou, Y. J., Chiba, S., Halfmann, P., Ehre, C., Kuroda, M., Dinnon, K. H., Leist, S. R., Schäfer, A., Nakajima, N., Takahashi, K., et al. (2020) · Science · doi:10.1126/science.abe8499 · Cited by 900 · cited 1× · see citing works
“The SARS-CoV-2 S D614G mutation has become globally dominant and is associated with enhanced viral transmission and replication but does not significantly affect Abmediated neutralization (Hou et al., 2020; Korber et al., 2020; Plante et al., 2020; Yurkovetskiy et al., 2020).”
BackgroundSelf-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 · cited 1× · see citing works
“As a result, SARS-CoV-2 S is the focus of nucleic acid, vectored, and protein subunit vaccines currently being developed and deployed (Corbett et al., 2020a, 2020b; Jackson et al., 2020; Mercado et al., 2020; Polack et al., 2020; Tostanoski et al., 2020; Yu et al., 2020).”
Self-citationStructural Basis for RNA Replication by the SARS-CoV-2 Polymerase
Wang, Q., Wu, J., Wang, H., Gao, Y., Liu, Q., Mu, A., Ji, W., Yan, L., Zhu, Y., Zhu, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.034 · Cited by 779 · see citing works
Structural insights into coronavirus entry
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“Although the S fusion machinery (S2 subunit) has higher sequence conservation than the RBD (Pinto et al., 2021; Sauer et al., 2021; Tortorici and Veesler, 2019; Walls et al., 2016, 2020a), the breadth of neutralization and protection provided by RBD-based vaccines remains unknown.”
Self-citationProspective mapping of viral mutations that escape antibodies used to treat COVID-19
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M. C., Dingens, A. S., Li, J. Z., & Bloom, J. D. (2021) · Science · doi:10.1126/science.abf9302 · Cited by 743 · see citing works
Self-citationSARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies
Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R., Walls, A. C., Kemp S, S. A., Bassi, J., Pinto, D., Fregni, C. S., et al. (2021) · doi:10.1101/2021.01.19.21249840 · Cited by 729 · see citing works
Self-citationSensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies
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Self-citationCrawford, K. H. D., Eguia, R. T., Dingens, A. S., Loes, A. N., Malone, K. D., Wolf, C. R., Chu, H. Y., Tortorici, M. A., Veesler, D., Murphy, M., et al. (2020) · Viruses · doi:10.3390/v12050513 · Cited by 727 · cited 2× · see citing works
“HIV-based pseudotypes were prepared as previously described (Crawford et al., 2020).”
Self-citationLiu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.01.014 · Cited by 725 · cited 1× · see citing works
“These findings show that, as is the case for many convalescent individuals (Greaney et al., 2021b; Liu et al., 2021; Piccoli et al., 2020), an important fraction of vaccine-elicited neutralizing Abs in NHPs and humans is focused on the RBM (specifically around position 484), independently of the immunogen (RBD-NP, Hex…”
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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-citationTransmission, infectivity, and neutralization of a spike L452R SARS-CoV-2 variant
Deng, X., Garcia-Knight, M. A., Khalid, M. M., Servellita, V., Wang, C., Morris, M. K., Sotomayor-González, A., Glasner, D. R., Reyes, K. R., Gliwa, A. S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.025 · Cited by 651 · cited 2× · see citing works
“2 (delta) that originated in the UK, South Africa, the USA, Brazil, and India, respectively (Davies et al., 2020; Deng et al., 2021; Faria et al., 2021; McCallum et al., 2021b; Tegally et al., 2020).”
InfluentialProspective mapping of viral mutations that escape antibodies used to treat COVID-19Preprint
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M., Dingens, A. S., Li, J. Z., & Bloom, J. (2020) · bioRxiv · doi:10.1101/2020.11.30.405472 · Cited by 633 · cited 6× · see citing works
“The 16-nucleotide barcode sequences identifying each RBD variant were amplified by PCR and sequenced on an Illumina HiSeq 2500 with 50 bp single-end reads as described in Greaney et al. (2020 and Starr et al. (2020a).”
InfluentialSelf-citationA Mouse-Adapted SARS-CoV-2 Induces Acute Lung Injury and Mortality in Standard Laboratory Mice
Leist, S. R., Dinnon, K. H., Schäfer, A., Tse, L. V., Okuda, K., Hou, Y. J., West, A., Edwards, C. E., Sanders, W., Fritch, E. J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.050 · Cited by 613 · cited 10× · see citing works
“These results indicate that one or two immunizations with 1 mg RBD-NPs results in protection against SARS-CoV-2 MA10-induced disease.”
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Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582 · see citing works
Self-citationAccurate design of megadalton-scale two-component icosahedral protein complexes
Bale, J. B., Gonen, S., Liu, Y., Sheffler, W., Ellis, D., Thomas, C. P., Cascio, D., Yeates, T. O., Gonen, T., King, N. P., et al. (2016) · Science · doi:10.1126/science.aaf8818 · Cited by 563 · cited 2× · see citing works
“We recently described a multivalent subunit vaccine displaying the SARS-CoV-2 RBD nanoparticle (RBD-NP) in a highly immunogenic array using a computationally designed selfassembling protein nanoparticle (Bale et al., 2016; Walls et al., 2020b).”
Self-citationZhou, H., Chen, X., Hu, T., Li, J., Song, H., Liu, Y., Wang, P., Liu, D., Yang, J., Holmes, E. C., et al. (2020) · Current Biology · doi:10.1016/j.cub.2020.05.023 · Cited by 562 · cited 3× · see citing works
“…viruses harboring the S glycoprotein of the Pangolin-GD isolate (GMT 6.6 3 102 and 7.7 3 102 VSV) and RaTG13 (GMT VSV 6 3 102) (Figures 3E and 3F) (Lam et al., 2020; Zhou et al., 2020b), in agreement with the close phylogenetic relationship of their RBDs with that of SARS-CoV-2 S (Figure S2B).”
InfluentialmRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · Science · doi:10.1126/science.abg9175 · Cited by 557 · see citing works
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
Walls, A. C., Tortorici, M. A., Bosch, B., Frenz, B., Rottier, P. J. M., DiMaio, F., Rey, F. A., & Veesler, D. (2016) · Nature · doi:10.1038/nature16988 · Cited by 539 · see citing works
Self-citationRecurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape
McCarthy, K. R., Rennick, L. J., Nambulli, S., Robinson-McCarthy, L. R., Bain, W. G., Haidar, G., & Duprex, W. P. (2021) · Science · doi:10.1126/science.abf6950 · Cited by 535 · cited 4× · see citing works
“To understand the impact of the full constellation of mutations present in the S proteins of the aforementioned VOCs, we evaluated RBD-NP- andHexaPro S-elicited serum neutralizing activity against corresponding HIV and VSV pseudotyped variants (D614G GMT RBD-NP HIV 5 3 103 and VSV RBD-NP 6 3 102, respectively, and D61…”
BackgroundInfluentialWalls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532 · see citing works
Self-citationBroad neutralization of SARS-related viruses by human monoclonal antibodies
Wec, A. Z., Wrapp, D., Herbert, A. S., Maurer, D. P., Haslwanter, D., Sakharkar, M., Jangra, R. K., Dieterle, M. E., Lilov, A., Huang, D., et al. (2020) · Science · doi:10.1126/science.abc7424 · Cited by 520 · cited 2× · see citing works
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
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
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510 · cited 1× · see citing works
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
Self-citationSARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 495 · cited 13× · see citing works
“The isolation of RBD-specific cross-reactive mAbs neutralizing SARS-CoV-2 and SARS-CoV suggests that RBD-based vaccines could, in principle, elicit Abs that neutralize distantly related sarbecoviruses, which have future pandemic potential (Cathcart et al., 2021; Jette et al., 2021; Martinez et al., 2021a; Pinto et al.…”
InfluentialSelf-citationBolles, M., Deming, D., Long, K., Agnihothram, S., Whitmore, A., Ferris, M., Funkhouser, W., Gralinski, L., Totura, A., Heise, M., et al. (2011) · Journal of Virology · doi:10.1128/jvi.06048-11 · Cited by 477 · cited 2× · see citing works
“Previous studies showed that double-inactivated SARS-CoV vaccines could lead to eosinophil infiltration in the lungs and subsequent immune pathology (Bolles et al., 2011).”
BackgroundSelf-citationA Mouse-Adapted SARS-Coronavirus Causes Disease and Mortality in BALB/c Mice
Roberts, A., Deming, D., Paddock, C. D., Cheng, A., Yount, B. L., Vogel, L., Herman, B. D., Sheahan, T., Heise, M. T., Genrich, G. L., et al. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030005 · Cited by 447 · see citing works
Self-citationSARS-like WIV1-CoV poised for human emergence
Menachery, V. D., Yount, B. L., Sims, A. C., Debbink, K., Agnihothram, S. S., Gralinski, L. E., Graham, R. L., Scobey, T., Plante, J. A., Royal, S. R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517719113 · Cited by 418 · see citing works
Self-citationSARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412 · see citing works
Self-citationSerum Neutralizing Activity Elicited by mRNA-1273 Vaccine
Wu, K., Werner, A. P., Koch, M., Choi, A., Narayanan, E., Stewart-Jones, G. B. E., Colpitts, T., Bennett, H., Boyoglu-Barnum, S., Shi, W., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmc2102179 · Cited by 409 · see citing works
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“However, we note that neutralization assays may underestimate the contribution of NTD-specific or non-RBM RBD-targeted neutralizing Abs (Lempp et al., 2021; McCallum et al., 2021a; Suryadevara et al., 2021), and protection from challenge will be the ultimate readout.”
Broad betacoronavirus neutralization by a stem helix–specific human antibody
Pinto, D., Sauer, M. M., Czudnochowski, N., Low, J. S., Tortorici, M. A., Housley, M. P., Noack, J., Walls, A. C., Bowen, J. E., Guarino, B., et al. (2021) · Science · doi:10.1126/science.abj3321 · Cited by 381 · cited 1× · see citing works
“Although the S fusion machinery (S2 subunit) has higher sequence conservation than the RBD (Pinto et al., 2021; Sauer et al., 2021; Tortorici and Veesler, 2019; Walls et al., 2016, 2020a), the breadth of neutralization and protection provided by RBD-based vaccines remains unknown.”
Self-citationThe 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
Adjuvanting a subunit COVID-19 vaccine to induce protective immunity
Arunachalam, P. S., Walls, A. C., Golden, N., Atyeo, C. G., Fischinger, S., Li, C., Aye, P. P., Navarro, M. J., Lai, L., Edara, V. V., et al. (2021) · Nature · doi:10.1038/s41586-021-03530-2 · Cited by 326 · cited 8× · see citing works
“5 mg of AS03-adjuvanted prefusion-stabilized HexaPro S trimer (RBD EC50 1 3 10 (4)) and followed for 42 days (Arunachalam et al., 2021; Hsieh et al., 2020), as well as a panel of COVID-19 HCP (Table S2) (RBD EC50 2 3 10 (4)) (Figures 2A and S2A).”
InfluentialSelf-citationNeutralization of SARS-CoV-2 by Destruction of the Prefusion Spike
Huo, J., Zhao, Y., Ren, J., Zhou, D., Duyvesteyn, H. M. E., Ginn, H. M., Carrique, L., Malinauskas, T., Ruza, R. R., Shah, P. N. M., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.010 · Cited by 317 · see citing works
Quadrivalent influenza nanoparticle vaccines induce broad protection
Boyoglu-Barnum, S., Ellis, D., Gillespie, R. A., Hutchinson, G. B., Park, Y., Moin, S. M., Acton, O. J., Ravichandran, R., Murphy, M., Pettie, D., et al. (2021) · Nature · doi:10.1038/s41586-021-03365-x · Cited by 306 · cited 2× · see citing works
“, 2021b) and recent results obtained with influenza virus hemagglutinin nanoparticle vaccines (Boyoglu-Barnum et al., 2021).”
Self-citationBroad and potent activity against SARS-like viruses by an engineered human monoclonal antibody
Rappazzo, C. G., Tse, L. V., Kaku, C. I., Wrapp, D., Sakharkar, M., Huang, D., Deveau, L. M., Yockachonis, T. J., Herbert, A. S., Battles, M. B., et al. (2021) · Science · doi:10.1126/science.abf4830 · Cited by 304 · cited 1× · see citing works
“The isolation of RBD-specific cross-reactive mAbs neutralizing SARS-CoV-2 and SARS-CoV suggests that RBD-based vaccines could, in principle, elicit Abs that neutralize distantly related sarbecoviruses, which have future pandemic potential (Cathcart et al., 2021; Jette et al., 2021; Martinez et al., 2021a; Pinto et al.…”
Self-citationLectins enhance SARS-CoV-2 infection and influence neutralizing antibodies
Lempp, F. A., Soriaga, L. B., Montiel-Ruiz, M., Benigni, F., Noack, J., Park, Y., Bianchi, S., Walls, A. C., Bowen, J. E., Zhou, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03925-1 · Cited by 292 · see citing works
Self-citationMosaic nanoparticle display of diverse influenza virus hemagglutinins elicits broad B cell responses
Kanekiyo, M., Joyce, M. G., Gillespie, R. A., Gallagher, J. R., Andrews, S. F., Yassine, H. M., Wheatley, A. K., Fisher, B. E., Ambrozak, D. R., Creanga, A., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0305-x · Cited by 290 · cited 1× · see citing works
“5438 Cell 184, 5432–5447, October 14, 2021 Design, assembly, and characterization of mosaic and cocktail sarbecovirus RBD-NPs We and others have recently evaluated nanoparticle immunogens that display multiple antigenic variants of viral glycoproteins as a potential route toward broadly protective vaccines (Boyoglu-Ba…”
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285 · see citing works
Self-citationAbu Jabal, K., Ben-Amram, H., Beiruti, K., Batheesh, Y., Sussan, C., Zarka, S., & Edelstein, M. (2021) · Eurosurveillance · doi:10.2807/1560-7917.es.2021.26.6.2100096 · Cited by 271 · see citing works
Ad26 vaccine protects against SARS-CoV-2 severe clinical disease in hamsters
Tostanoski, L. H., Wegmann, F., Martinot, A. J., Loos, C., McMahan, K., Mercado, N. B., Yu, J., Chan, C. N., Bondoc, S., Starke, C. E., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1070-6 · Cited by 269 · cited 1× · see citing works
“As a result, SARS-CoV-2 S is the focus of nucleic acid, vectored, and protein subunit vaccines currently being developed and deployed (Corbett et al., 2020a, 2020b; Jackson et al., 2020; Mercado et al., 2020; Polack et al., 2020; Tostanoski et al., 2020; Yu et al., 2020).”
Broad sarbecovirus neutralization by a human monoclonal antibody
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · Nature · doi:10.1038/s41586-021-03817-4 · Cited by 251 · cited 2× · see citing works
“5 3 10(1)) (Figures 2D and 2E; Data S1), which comprise conserved sarbecovirus epitopes recognized by broadly neutralizing sarbecovirus mAbs such as S2X259 (site II) and S309 (site IV) (Piccoli et al., 2020; Pinto et al., 2020; Tortorici et al., 2021).”
Self-citationGreaney, A. J., Loes, A. N., Gentles, L. E., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9915 · Cited by 244 · see citing works
Self-citationInferring the shape of global epistasis
Otwinowski, J., McCandlish, D. M., & Plotkin, J. B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804015115 · Cited by 243 · cited 1× · see citing works
“We next deconvolved variant-level escape scores into escape fraction estimates for singlemutations using global epistasismodels (Otwinowski et al., 2018) implemented in the dms_variants package, as detailed at (https://jbloomlab.”
Cathcart, A. L., Havenar‐Daughton, C., Lempp, F. A., Ma, D., Schmid, M., Agostini, M. L., Guarino, B., di Iulio, J., Rosen, L. E., Tucker, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.09.434607 · Cited by 206 · cited 2× · see citing works
“As a result, formulation of mAb cocktails or the use of mAbs targeting conserved epitopes and neutralizing a broader spectrum of circulating SARS-CoV-2 variants emerged as a promising strategy to overcome this issue (Baum et al., 2020b; Cathcart et al., 2021; Dong et al., 2021; Greaney et al., 2020; Jette et al., 2021…”
BackgroundSelf-citationStructural basis for broad coronavirus neutralization
Sauer, M. M., Tortorici, M., Park, Y.-J., Walls, A., Homad, L. J., Acton, O., Bowen, J., Wang, C., Xiong, X., de van der Schueren, W. J., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00596-4 · Cited by 199 · cited 2× · see citing works
“Although the S fusion machinery (S2 subunit) has higher sequence conservation than the RBD (Pinto et al., 2021; Sauer et al., 2021; Tortorici and Veesler, 2019; Walls et al., 2016, 2020a), the breadth of neutralization and protection provided by RBD-based vaccines remains unknown.”
Self-citationChimeric spike mRNA vaccines protect against Sarbecovirus challenge in mice
Martinez, D. R., Schäfer, A., Leist, S. R., la Cruz, G. D., West, A., Atochina‐Vasserman, E. N., Lindesmith, L. C., Pardi, N., Parks, R., Barr, M., et al. (2021) · Science · doi:10.1126/science.abi4506 · Cited by 189 · see citing works
Self-citationSARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2103154118 · Cited by 187 · see citing works
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“REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies CR3022 ter Meulen et al., 2006 N/A S309 Pinto et al., 2020 N/A S2X259 Tortorici et al., 2021 N/A S2H14 Piccoli et al., 2020 N/A S230 Rockx et al., 2008 N/A Goat anti-mouse HRP Invitrogen Cat #626520; Lot #TG275230; AB_2533947 Goat anti-human HRP Invitrogen Cat #A18817;…”
InfluentialSelf-citationKrammer, F., Srivastava, K., the PARIS team, & Simon, V. (2021) · doi:10.1101/2021.01.29.21250653 · Cited by 116 · cited 2× · see citing works
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“Pseudovirus production MLV-based D614G SARS-CoV-2 S and SARS-CoV S pseudotypes were prepared as previously described (Millet and Whittaker, 2016; Walls et al., 2020a, 2020b).”
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Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y., Hoffman, P. R., Ou, S., Kakutani, L. M., Keeffe, J., Wu, H.-J., Howarth, M., West, A. P., et al. (2021) · Science · doi:10.1126/science.abf6840 · Cited by 60 · see citing works
Genetic and structural basis for recognition of SARS-CoV-2 spike protein by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · doi:10.1101/2021.01.27.428529 · Cited by 55 · see citing works
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Self-citationAn Engineered Antibody with Broad Protective Efficacy in Murine Models of SARS and COVID-19Preprint
Rappazzo, C. G., Tse, L. V., Kaku, C. I., Wrapp, D., Sakharkar, M., Huang, D., Deveau, L. M., Yockachonis, T. J., Herbert, A. S., Battles, M. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.17.385500 · Cited by 16 · see citing works
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Self-citationSARS-CoV-2 escape <i>in vitro</i> from a highly neutralizing COVID-19 convalescent plasma
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BackgroundInfluentialSelf-citationSARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
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Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
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Self-citationStructural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
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“The identification of broadly reactive mAbs that neutralize multiple distinct sarbecoviruses, including SARS-CoV-2 variants, pave the way for designing vaccines eliciting broad sarbecovirus immunity ( 52 – 56 ).”
Self-citationSARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 495 · see citing works
Self-citationBroad betacoronavirus neutralization by a stem helix–specific human antibody
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Self-citationUnadjuvanted intranasal spike vaccine elicits protective mucosal immunity against sarbecoviruses
Mao, T., Israelow, B., Peña-Hernández, M. A., Suberi, A., Zhou, L., Luyten, S., Reschke, M., Dong, H., Homer, R. J., Saltzman, W., et al. (2022) · Science · doi:10.1126/science.abo2523 · Cited by 288 · see citing works
“Although some recent studies have successfully reported the development of systemic pan-sarbecovirus vaccines (37, 38), P&Sx induces both systemic andmucosal immunity against both SARS-CoV-1 and SARS-CoV-2.”
ResultMolecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants
McCallum, M., Walls, A. C., Sprouse, K. R., Bowen, J. E., Rosen, L. E., Dang, H. V., Marco, A. D., Franko, N., Tilles, S. W., Logue, J. K., et al. (2021) · Science · doi:10.1126/science.abl8506 · Cited by 273 · see citing works
Self-citationBroad sarbecovirus neutralization by a human monoclonal antibody
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · Nature · doi:10.1038/s41586-021-03817-4 · Cited by 251 · see citing works
Self-citationMosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J. R., Fan, C., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · Science · doi:10.1126/science.abq0839 · Cited by 259 · see citing works
“Target list [bead region] were as follows: T helper: GM-CSF [44], IFN gamma [43], IL-1 beta [18], IL-2 [19], IL-4 [20], IL-5 [21], IL-6 [25], IL-8 (CXCL8) [27], IL-10 [28], IL12p70 [34], IL-13 [35], IL-17A (CTLA-8) [36], IL-18 [66], IL-23 [63], TNF alpha [45] Cytokines: CD40L [74], G-CSF (CSF-3) [42], IFN alpha [48],…”
Self-citationBroadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
Cameroni, E., Bowen, J. E., Rosen, L. E., Saliba, C., Zepeda, S. K., Culap, K., Pinto, D., VanBlargan, L. A., Marco, A. D., di Iulio, J., et al. (2021) · Nature · doi:10.1038/d41586-021-03825-4 · Cited by 247 · see citing works
Self-citationImprinted antibody responses against SARS-CoV-2 Omicron sublineages
Park, Y., Pinto, D., Walls, A. C., Liu, Z., Marco, A. D., Benigni, F., Zatta, F., Silacci-Fregni, C., Bassi, J., Sprouse, K. R., et al. (2022) · Science · doi:10.1126/science.adc9127 · Cited by 225 · see citing works
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-citationThe humoral response and antibodies against SARS-CoV-2 infection
Qi, H., Liu, B., Wang, X.-Q., & Zhang, L.-Q. (2022) · Nature Immunology · doi:10.1038/s41590-022-01248-5 · Cited by 169 · see citing works
Protein Cages: From Fundamentals to Advanced Applications
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Targeted modulation of immune cells and tissues using engineered biomaterials
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Omicron spike function and neutralizing activity elicited by a comprehensive panel of vaccines
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Nanotechnology-based strategies against SARS-CoV-2 variants
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Scientific rationale for developing potent RBD-based vaccines targeting COVID-19
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Self-citationAntibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry
Park, Y., Marco, A. D., Starr, T. N., Liu, Z., Pinto, D., Walls, A. C., Zatta, F., Zepeda, S. K., Bowen, J. E., Sprouse, K. R., et al. (2022) · Science · doi:10.1126/science.abm8143 · Cited by 132 · see citing works
Self-citationSARS-CoV-2 immune evasion by variant B.1.427/B.1.429Preprint
McCallum, M., Bassi, J., Marco, A. D., Chen, A., Walls, A. C., di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.31.437925 · Cited by 128 · see citing works
“429 S pseudotypes were prepared as previously 528 described (62, 63).”
MethodSelf-citation“World in motion” – emulsion adjuvants rising to meet the pandemic challenges
O’Hagan, D. T., der Most, R. G. V., Lodaya, R. N., Coccia, M., & Lofano, G. (2021) · npj Vaccines · doi:10.1038/s41541-021-00418-0 · Cited by 121 · see citing works
Self-citationA broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice
Martinez, D. R., Schäfer, A., Gobeil, S., Li, D., la Cruz, G. D., Parks, R., Lu, X., Barr, M., Stalls, V., Janowska, K., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abj7125 · Cited by 136 · see citing works
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“Towards this goal, nanoparticles co-displaying multiple distinct RBDs from beta-coronaviruses could induce cross-nAbs in mice, providing a strategy for simultaneous protection against SARS-CoV-2 and some zoonotic sarbecovirus infections.(67,68) Similarly, nanoparticles displaying the SARS-CoV-2 RBD formulated with 3M-…”
BackgroundRETRACTED: SARS-CoV-2 S2–targeted vaccination elicits broadly neutralizing antibodies
Ng, K. W., Faulkner, N., Finsterbusch, K., Wu, M., Harvey, R., Hussain, S., Greco, M., Liu, Y., Kjær, S., Swanton, C., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn3715 · Cited by 95 · see citing works
RetractedCurrent and future nanoparticle vaccines for COVID-19
Vu, M. N., Kelly, H. G., Kent, S. J., & Wheatley, A. K. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103699 · Cited by 97 · see citing works
“In another approach, the two-component computationally designed protein scaffold I53-50 was constructed to deliver RBDs from four distinct sarbecoviruses - SARS-CoV-1, SARS-CoV-2 and two bat coronaviruses WIV1 and RaTG13 [72].”
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Self-citationArchitecture and antigenicity of the Nipah virus attachment glycoprotein
Wang, Z., Amaya, M., Addetia, A., Dang, H. V., Reggiano, G., Yan, L., Hickey, A. C., DiMaio, F., Broder, C. C., & Veesler, D. (2022) · Science · doi:10.1126/science.abm5561 · Cited by 96 · see citing works
Self-citationTortorici, M. A., Walls, A. C., Joshi, A., Park, Y., Eguia, R. T., Miranda, M. C., Kepl, E., Dosey, A. M., Stevens‐Ayers, T., Boeckh, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.019 · Cited by 87 · see citing works
“…of therapeutics and vaccine development, including monoclonal antibody therapies and vaccines (Baum et al., 2020; Corbett et al., 2020; Corti et al., 2021; Hansen et al., 2020; McCallum et al., 2021a; Piccoli et al., 2020; Pinto et al., 2020; Polack et al., 2020; Walls et al., 2019, 2020b, 2021).”
Self-citationEngineering Self-Assembling Protein Nanoparticles for Therapeutic Delivery
Olshefsky, A., Richardson, C., Pun, S. H., & King, N. P. (2022) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.2c00030 · Cited by 91 · see citing works
Self-citationIn search of a pan-coronavirus vaccine: next-generation vaccine design and immune mechanisms
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“Serum from RBD-NP-immunized nonhuman primates strongly cross-reacted with Pangolin-GD and RaTG13 RBDs but had weaker binding to distantly related RmYN02, SARS-CoV-1, WIV16, and ZXC21 RBDs [146].”
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Self-citationAdvanced technologies for the development of infectious disease vaccines
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Self-citationChallenges and developments in universal vaccine design against SARS-CoV-2 variants
Zhao, F., Zai, X., Zhang, Z., Xu, J., & Chen, W. (2022) · npj Vaccines · doi:10.1038/s41541-022-00597-4 · Cited by 81 · see citing works
Immune imprinting and next-generation coronavirus vaccines
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“A Delta–Omicron chimaeric RBD dimer was also shown to protect against matched VOCs 127 .”
BackgroundInfluentialAdenovirus-based vaccines—a platform for pandemic preparedness against emerging viral pathogens
Coughlan, L., Kremer, E. J., & Shayakhmetov, D. M. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.01.034 · Cited by 66 · see citing works
“Another innovative vaccine platform is the use of naturally occurring, self-assembling nanoparticles or computationally designed vaccine scaffolds.(34,35) Similar to VLPs, these particles allow for a structurally ordered display of antigen, which, along with their small size, allows them to mimic viruses.”
Proactive vaccination using multiviral Quartet Nanocages to elicit broad anti-coronavirus responses
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“RBDs can be multimerized on VLPs through genetic fusion 15 or isopeptide coupling 12 .”
Imprinted antibody responses against SARS-CoV-2 Omicron sublineages
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An ultrapotent RBD-targeted biparatopic nanobody neutralizes broad SARS-CoV-2 variants
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The quest for nanoparticle-powered vaccines in cancer immunotherapy
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“60 While these results are promising and consistent with an approach that has worked with seasonal in fl u-enza vaccines, concerns include the large number of antigens required to provide broad protection as well as the plasticity of RBD domain and the possible emergence of new vaccine-evading RBD…”
Self-citationCurrent progress in the development of prophylactic and therapeutic vaccines
Li, T., Qian, C., Gu, Y., Zhang, J., Li, S., & Xia, N. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2230-4 · Cited by 57 · see citing works
“(Walls et al., 2021) and is thus currently undergoing clinical trials (NCT04742738, NCT05007951).”
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“1 (for Omicron) and our previous work (33).”
BackgroundSelf-citationHierarchical design of pseudosymmetric protein nanocages
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Self-citationAntigen- and scaffold-specific antibody responses to protein nanoparticle immunogens
Kraft, J. C., Pham, M. N., Shehata, L., Brinkkemper, M., Boyoglu-Barnum, S., Sprouse, K. R., Walls, A. C., Cheng, S., Murphy, M., Pettie, D., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100780 · Cited by 51 · see citing works
Self-citationAn antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses
Liu, L., Iketani, S., Guo, Y., Reddem, E. R., Casner, R. G., Nair, M. S., Yu, J., Chan, J. F., Wang, M., Cerutti, G., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn6859 · Cited by 51 · see citing works
Ellis, D., Brunette, N., Crawford, K. H. D., Walls, A. C., Pham, M. N., Chen, C., Herpoldt, K., Fiala, B., Murphy, M., Pettie, D., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.710263 · Cited by 50 · see citing works
“MLV-Based Pseudovirus Neutralization Assays MLV-based SARS-CoV-2 S pseudotypes were prepared as previously described (10, 25, 50, 70).”
BackgroundMethodSelf-citationMalhi, H., Homad, L. J., Wan, Y.-H., Poudel, B., Fiala, B., Borst, A. J., Wang, J. Y., Walkey, C., Price, J., Wall, A., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100658 · Cited by 48 · see citing works
Self-citationSong, J. Y., Choi, W. S., Heo, J. Y., Kim, E. J., Lee, J. S., Jung, D. S., Kim, S., Park, K., Eom, J. S., Jeong, S. J., et al. (2023) · EClinicalMedicine · doi:10.1016/j.eclinm.2023.102140 · Cited by 50 · see citing works
Self-citationResearch progress on emulsion vaccine adjuvants
Huang, Z., Gong, H., Sun, Q., Yang, J., Yan, X., & Xu, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e24662 · Cited by 47 · see citing works
“Although current preliminary data are encouraging [121], careful evaluation of the immune response induced by emulsion adjuvant vaccines relative to alternative vaccine approaches is needed.”
BackgroundZhang, J., Xu, Y., Chen, M., Huang, Y., Song, T., Yang, C. J., Yang, Y., & Song, Y. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c09229 · Cited by 46 · see citing works
Molecular basis of convergent evolution of ACE2 receptor utilization among HKU5 coronaviruses
Park, Y., Liu, C., Lee, J., Brown, J. T., Ma, C., Liu, P., Gen, R., Xiong, Q., Zepeda, S. K., Stewart, C., et al. (2025) · Cell · doi:10.1016/j.cell.2024.12.032 · Cited by 46 · see citing works
“These findings are reminiscent of the weak cross-clade neutralization observed for sarbecoviruses, 105,106 which harbor RBDs much more similar to each other than merbecovirus RBDs.”
Self-citationBroad-spectrum pan-genus and pan-family virus vaccines
Tan, C. W., Valkenburg, S., Poon, L. L. M., & Wang, L. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.05.017 · Cited by 41 · see citing works
“sarbecoviruses and protect the vaccinated animals from SARSCoV-1 infection.(124) Chimeric spike mRNA vaccine candidates, containing RBD, NTD, and S2 domains from different SARS-”
Rapid and automated design of two-component protein nanomaterials using ProteinMPNN
de Haas, R. J., Brunette, N., Goodson, A., Dauparas, J., Yi, S. Y., Yang, E. C., Dowling, Q., Nguyen, H., Kang, A., Bera, A. K., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314646121 · Cited by 42 · see citing works
“In vitro assembly has been used in the manufacturing processes for several designed protein nanoparticle vaccines in clinical trials (35, 49) (NCT05664334 and NCT04750343), including a mosaic nanoparticle vaccine for influenza that codisplays four distinct hemagglutinin antigens on the same…”
Self-citationOmicron 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 41 · see citing works
Self-citationVishwanath, S., Carnell, G., Ferrari, M., Asbach, B., Billmeier, M., George, C. L., Sans, M. S., Nadesalingam, A., Huang, C. Q., Paloniemi, M., et al. (2023) · Nature Biomedical Engineering · doi:10.1038/s41551-023-01094-2 · Cited by 37 · see citing works
“Strategies to achieve pan-sarbecovirus and pan-betacoronavirus protection include synthetic mRNAs expressing chimaeric versions of different spike proteins 29 , and mosaic or cocktail nanoparticles expressing RBDs derived from different coronaviruses 30 .”
Antigen spacing on protein nanoparticles influences antibody responses to vaccination
Ellis, D., Dosey, A. M., Boyoglu-Barnum, S., Park, Y., Gillespie, R. A., Syeda, H., Hutchinson, G. B., Tsybovsky, Y., Murphy, M., Pettie, D., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113552 · Cited by 42 · see citing works
“…include Epstein-Barr virus gp350 89 and human cytomegalovirus glycoprotein B. 90 The strategy has also been combined with antigen stabilization, 86,91,92 germline targeting, 93–95 and mosaic nanoparticle display 34,85,96,97 to further increase the potency and breadth of vaccine-elicited antibodies.”
MethodSelf-citationDesign of a mutation-integrated trimeric RBD with broad protection against SARS-CoV-2
Liang, Y., Zhang, J., Yuan, R. Y., Wang, M. Y., He, P., Su, J. G., Han, Z. B., Jin, Y. Q., Hou, J. W., Zhang, H., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00383-5 · Cited by 42 · see citing works
Martinez, D. R., Schaefer, A., Gobeil, S., Li, D., la Cruz, G. D., Parks, R., Lu, X., Barr, M., Manne, K., Mansouri, K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.27.441655 · Cited by 37 · see citing works
Self-citationSpySwitch enables pH- or heat-responsive capture and release for plug-and-display nanoassembly
Vester, S. K., Rahikainen, R., Anuar, I. N. A. K., Hills, R. A., Tan, T. K., & Howarth, M. R. (2022) · Nature Communications · doi:10.1038/s41467-022-31193-8 · Cited by 35 · see citing works
Host range, transmissibility and antigenicity of a pangolin coronavirus
Hou, Y. J., Chiba, S., Leist, S. R., Meganck, R. M., Martinez, D. R., Schäfer, A., Catanzaro, N., Sontake, V., West, A., Edwards, C. E., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01476-x · Cited by 34 · see citing works
Self-citationBroad receptor tropism and immunogenicity of a clade 3 sarbecovirus
Lee, J., Zepeda, S. K., Park, Y., Taylor, A. L., Quispe, J. D., Stewart, C., Leaf, E. M., Treichel, C., Corti, D., King, N. P., et al. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.10.018 · Cited by 34 · see citing works
Self-citationMaltseva, M., Keeshan, A., Cooper, C., & Langlois, M. (2024) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2024.2384192 · Cited by 33 · see citing works
Zhang, Y.-N., Paynter, J. A., Sou, C., Fourfouris, T., Wang, Y., Abraham, C., Ngo, T. A., Zhang, Y., He, L.-L., & Zhu, J. (2021) · Science Advances · doi:10.1126/sciadv.abj3107 · Cited by 24 · see citing works
Broadly neutralizing antibodies to SARS-related viruses can be readily induced in rhesus macaques
He, W.-T., Yuan, M., Callaghan, S., Musharrafieh, R., Song, G., Silva, M., Beutler, N., Lee, W., Yong, P., Torres, J., et al. (2021) · bioRxiv · doi:10.1126/scitranslmed.abl9605 · Cited by 31 · see citing works
Rationally designed immunogens enable immune focusing following SARS-CoV-2 spike imprinting
Hauser, B. M., Sangesland, M., Denis, K. S., Lam, E. C., Case, J. B., Windsor, I. W., Feldman, J. E., Caradonna, T. M., Kannegieter, T., Diamond, M., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110561 · Cited by 37 · see citing works
“Although protein- and mRNA-based immunization strategies elicit SARS-2 and broad sarbecovirus immunity (Cohen et al., 2021; Martinez et al., 2021; Walls et al., 2021), it remains unknownwhether these vaccine candidates can successfully focus immunity toward conserved crossneutralizing epitopes in the context of SARS-2…”
Wang, H., Xue, Q., Zhang, H. C., Yuan, G., Wang, X., Sheng, K., Li, C., Cai, J., Sun, Y., Zhao, J., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2249121 · Cited by 30 · see citing works
“There are also two backbones pseudovirus systems that simultaneously used in the neutralization assays for SARS-CoV-2 [38,39].”
MethodZhou, D., Cheng, R., Yao, Y., Zhang, G., Li, X., Wang, B., Wang, Y., Yu, F., Yang, S., Liu, H., et al. (2024) · npj Vaccines · doi:10.1038/s41541-024-00954-5 · Cited by 29 · see citing works
“Duetotheseadvantages,thisdeliverysystemhasbeen extensively utilized in vaccine developments against diverse infectious pathogens and tumors, including in fl uenza vaccines 35,36 , Epstein-Barr virus vaccines 37,38 , and COVID-19 vaccines 39 – 42 .”
BackgroundMethodHutchinson, G. B., Abiona, O. M., Ziwawo, C. T., Werner, A. P., Ellis, D., Tsybovsky, Y., Leist, S. R., Palandjian, C., West, A., Fritch, E. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41661-4 · Cited by 29 · see citing works
“Other studies have reported intrasubgroup cross-reactivity through natural infection 7 or via nanoparticle-based immunogens using mosaic co-display of RBDs from diverse SARS-like CoV S proteins 9,10 .”
BackgroundSelf-citationAdvances in SARS-CoV-2 receptor-binding domain-based COVID-19 vaccines
Guan, X., Yang, Y., & Du, L. (2023) · Expert Review of Vaccines · doi:10.1080/14760584.2023.2211153 · Cited by 28 · see citing works
“Such approaches have also been used to design S-based mosaic nanoparticle vaccines that target different SARS-CoV-2 variants, as well as RBD-based universal mosaic nanoparticle vaccines against both SARS-CoV-2 and other Sarbecoviruses [114,116–118].”
BackgroundMethodS glycoprotein diversity of the Omicron variantPreprint
Sarkar, R., Lo, M., Saha, R., Dutta, S., & Chawla‐Sarkar, M. (2021) · medRxiv · doi:10.1101/2021.12.04.21267284 · Cited by 27 · see citing works
“The E484Q has been shown to reduce serum neutralizing antibody titers [33-35].”
BackgroundInducing broad-based immunity against viruses with pandemic potential
Sette, A., & Saphire, E. O. (2022) · Immunity · doi:10.1016/j.immuni.2022.04.010 · Cited by 24 · see citing works
Moore, K. A., Leighton, T., Ostrowsky, J. T., Anderson, C. J., Danila, R. N., Ulrich, A. K., Lackritz, E. M., Mehr, A. J., Baric, R. S., Baylor, N. W., et al. (2023) · Vaccine · doi:10.1016/j.vaccine.2023.02.032 · Cited by 25 · see citing works
Self-citationLenart, K., Cerveira, R. A., Hellgren, F., Ols, S., Sheward, D. J., Kim, C., Cagigi, A., Gagné, M., Davis, B. J., Germosen, D., et al. (2024) · npj Vaccines · doi:10.1038/s41541-024-00806-2 · Cited by 26 · see citing works
“Elicitation of broadly neutralizing B cell responses is therefore critical for developing highly ef fi cacious vaccine immunity to past, present, and future SARS-CoV-2 variants 36,37 .”
Self-citationProtein Nanoparticles as Vaccine Platforms for Human and Zoonotic Viruses
Pandey, K. K., Sahoo, B. R., & Pattnaik, A. K. (2024) · Viruses · doi:10.3390/v16060936 · Cited by 25 · see citing works
“In these studies, either the full-length S [142], mosaic S from several variants of concern [143], the RBD [139,141], or the mosaic RBD from multiple sarbecoviruses [144] was displayed as trimeric subunits on the surface of the I53-50 through genetic fusion or tag coupling.”
BackgroundAntibody-mediated immunity to SARS-CoV-2 spike
Errico, J. M., Adams, L. J., & Fremont, D. H. (2022) · Advances in immunology · doi:10.1016/bs.ai.2022.07.001 · Cited by 20 · see citing works
“Although SARS-CoV cross-reactive RBM (ACE2-blocking) antibodies exist in polyclonal settings (Walls et al., 2021; Wec et al., 2020), examples of true class 1 or 2 broad sarbecovirus neutralizing mAbs like S2K146 are rare; S2K146 is itself unlike other class I RBM antibodies in that it displays a…”
Brinkkemper, M., Veth, T. S., Brouwer, P. J. M., Turner, H. L., Poniman, M., Burger, J. A., Bouhuijs, J. H., Olijhoek, W., Bontjer, I., Snitselaar, J. L., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105649 · Cited by 24 · see citing works
“Similar approaches, using RBDs from S proteins of multiple SARS and SARS-like strains, have demonstrated potential in mice and non-human primates.(51,52) Future mosaic NP approaches may exclude SARS-CoV2 S to specifically boost cross-reactive responses.”
Self-citationAddetia, A., Piccoli, L., Case, J. B., Park, Y., Beltramello, M., Guarino, B., Dang, H. V., Pinto, D., Scheaffer, S. M., Sprouse, K. R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.17.523798 · Cited by 25 · see citing works
Self-citationMosaic RBD nanoparticle elicits immunodominant antibody responses across sarbecoviruses
Liu, C., Xu, S., Zheng, Y., Xie, Y., Xu, K., Chai, Y., Luo, T., Dai, L., & Gao, G. F. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114235 · Cited by 24 · see citing works
Lamerton, R. E., Marcial‐Juárez, E., Faustini, S. E., Pérez-Toledo, M., Goodall, M. D., Jossi, S. E., Newby, M. L., Chapple, I., Dietrich, T., Veenith, T., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.838780 · Cited by 20 · see citing works
Zhou, J., Liu, Z., Zhang, G., Xu, W., Xing, L., Lu, L., Wang, Q., & Jiang, S. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28172 · Cited by 23 · see citing works
“For example, the vaccine RBD‐NP utilized a two‐component icosahedral protein nanoparticle (I53‐50) to display the SARS‐CoV‐2 RBD protein.(113) The vaccine's efficacy in different animal models was confirmed (Table 2).”
BackgroundMethodInfluentialHendricks, G. G., Grigoryan, L., Navarro, M. J., Catanzaro, N., Hubbard, M. L., Powers, J. M., Mattocks, M. D., Treichel, C., Walls, A. C., Lee, J., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adu2085 · Cited by 22 · see citing works
“Second, as shown previously (20, 33, 44–48), multivalent display of RBDs on self-assembling protein nanoparticles improves immunogenicity, particularly post-prime, as indicated by the enhanced immunogenicity of the adjuvanted protein RBD nanoparticles compared with non-assembling RBD trimers at…”
Self-citationLee, D. B., Kim, H., Jeong, J. H., Jang, U. S., Jang, Y., Roh, S., Jeon, H., Kim, E. J., Han, S. Y., Maeng, J. Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208425120 · Cited by 22 · see citing works
“In contrast, mosaic nanoparticles achieved by mixing heterologous β-CoV RBDs provide an avidity advantage to elicit superior cross-reactive B cells than an admixture of nanoparticles (24, 25).”
BackgroundJacob-Dolan, C., Yu, J., McMahan, K., Giffin, V. M., Chandrashekar, A., Martinot, A. J., Anioke, T., Powers, O. C., Hall, K., Hope, D. L., et al. (2023) · npj Vaccines · doi:10.1038/s41541-023-00622-0 · Cited by 23 · see citing works
Self-citationWang, D., Yuan, Y., Liu, B., Epstein, N. D., & Yang, Y. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123979 · Cited by 23 · see citing works
Corleis, B., Hoffmann, D., Rauch, S., Fricke, C., Roth, N., Gergen, J., Kovacikova, K., Schlottau, K., Halwe, N. J., Ulrich, L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36110-1 · Cited by 22 · see citing works
Computational design of vaccine immunogens
Castro, K. M., Scheck, A., Xiao, S., & Correia, B. E. (2022) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2022.102821 · Cited by 22 · see citing works
Dosey, A. M., Ellis, D., Boyoglu-Barnum, S., Syeda, H., Saunders, M., Watson, M. J., Kraft, J. C., Pham, M. N., Guttman, M., Lee, K. K., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113553 · Cited by 22 · see citing works
Self-citationMartinez, D. R., Moreira, F. R., Catanzaro, N., Diefenbacher, M. V., Zweigart, M. R., Gully, K. L., la Cruz, G. D., Brown, A. J., Adams, L. E., Yount, B. L., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adj4504 · Cited by 33 · see citing works
Self-citationAddetia, A., Stewart, C., Seo, A. J., Sprouse, K. R., Asiri, A. Y., Al-Mozaini, M., Memish, Z. A., Alshukairi, A. N., & Veesler, D. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114530 · Cited by 22 · see citing works
“As such, betacoronavirus RBD-based vaccines will likely confer high neutralizing antibody titers and robust protection across this genera and could become an universal strategy to develop betacoronavirus vaccines, as successfully implemented with the SKYcovione COVID-19 vaccine 67,68 .”
Self-citationGlycosylation and Serological Reactivity of an Expression-enhanced SARS-CoV-2 Viral Spike Mimetic
Chawla, H., Jossi, S., Faustini, S., Samsudin, F., Allen, J., Watanabe, Y., Newby, M., Marcial-Juárez, E., Lamerton, R., McLellan, J., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167332 · Cited by 24 · see citing works
Self-citationStructural basis for broad sarbecovirus neutralization by a human monoclonal antibodyPreprint
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.07.438818 · Cited by 22 · see citing works
Self-citationSARS-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-citationZhang, J., Xu, Y., Chen, M., Wang, S., Lin, G., Huang, Y., Yang, C. J., Yang, Y., & Song, Y. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202412294 · Cited by 20 · see citing works
Vaccine-mediated protection against Merbecovirus and Sarbecovirus challenge in mice
Martinez, D. R., Schäfer, A., Gavitt, T. D., Mallory, M. L., Lee, E., Catanzaro, N., Chen, H., Gully, K. L., Scobey, T., Korategere, P., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113248 · Cited by 19 · see citing works
Self-citation
- 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)
- 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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