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Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Open accessAbstract
Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.
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“Immune responses are improved by introducing two consecutive proline residues (2P), which are known to retain the full-length S protein in the prefusion conformation.64,65”
From COVID-19 mRNA vaccines: Platforms and current developments (2022) · cites this paper as [64]
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“Both vaccines encode the same full-length, pre-fusion stabilized severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike protein13,14 and are encapsulated in lipid nanoparticles (LNPs) with identical composition.”
From Optimization of non-coding regions for a non-modified mRNA COVID-19 vaccine (2022) · cites this paper as [13]
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“Stabilizing coronavirus spike proteins by substituting two prolines at the top of heptad repeat 1 prevents structural rearrangements of the fusion (S2) subunit.”
From An mRNA Vaccine against SARS-CoV-2 — Preliminary Report (2020) · cites this paper as [27]
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“Moreover, S-2P conformational stability translates into greater immunogenicity,27-29 based on preservation of neutralization-sensitive epitopes at the apex of the prefusion molecule, as shown for respiratory syncytial virus F glycoprotein,30 and improved protein expression,27 which is particularly advantageous for gene-based antigen delivery.”
From An mRNA Vaccine against SARS-CoV-2 — Preliminary Report (2020) · cites this paper as [27]
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UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Isolation of a Novel Coronavirus from a Man with Pneumonia in Saudi Arabia
Zaki, A. M., van Boheemen, S., Bestebroer, T. M., Osterhaus, A. D. M. E., & Fouchier, R. A. M. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1211721 · Cited by 5,677
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
How good are my data and what is the resolution?
Evans, P. R., & Murshudov, G. N. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913000061 · Cited by 4,743
Comparative Protein Structure Modeling Using MODELLER
Webb, B., & Šali, A. (2016) · Current Protocols in Bioinformatics · doi:10.1002/cpbi.3 · Cited by 4,404
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Ashkenazy, H., Abadi, S., Martz, E., Chay, O., Mayrose, I., Pupko, T., & Ben-Tal, N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw408 · Cited by 3,163
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Zhang, S., Zhou, P.-P., Wang, P., Li, Y., Jiang, L., Jia, W., Wang, H., Fan, A., Wang, D., Shi, X., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.041 · Cited by 69
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Francica, J. R., Flynn, B. J., Foulds, K. E., Noe, A. T., Werner, A. P., Moore, I. N., Gagné, M., Johnston, T. S., Tucker, C., Davis, R. L., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi4547 · Cited by 89
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Kim, M. H., Kim, H. J., & Chang, J. (2019) · PLoS ONE · doi:10.1371/journal.pone.0220196 · Cited by 63
Ismail, S., Ahmad, S., & Azam, S. S. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.113612 · Cited by 63
Kim, Y., Kim, D.-K., Yu, K.-M., Seo, H. D., Lee, S.-A., Casel, M. A. B., Jang, S., Kim, S., Jung, W., Lai, C., et al. (2021) · mBio · doi:10.1128/mbio.00230-21 · Cited by 65
Jia, Q., Bielefeldt‐Ohmann, H., Maison, R. M., Masleša-Galić, S., Cooper, S. K., Bowen, R. A., & Horwitz, M. A. (2021) · npj Vaccines · doi:10.1038/s41541-021-00321-8 · Cited by 65
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Dickey, T. H., Tang, W. K., Butler, B., Ouahes, T., Orr-Gonzalez, S., Salinas, N. D., Lambert, L., & Tolia, N. H. (2022) · Science Advances · doi:10.1126/sciadv.abq8276 · Cited by 59
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Yilmaz, I. C., İpekoğlu, E. M., Bulbul, A., Turay, N., Yıldırım, M., Evcili, İ., Yilmaz, N. S., Guvencli, N., Aydin, Y., Gungor, B., et al. (2021) · Allergy · doi:10.1111/all.15091 · Cited by 63
Goel, R. R., Painter, M. M., Apostolidis, S. A., Mathew, D., Meng, W., Rosenfeld, A. M., Lundgreen, K. A., Reynaldi, A., Khoury, D. S., Pattekar, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.23.457229 · Cited by 59
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Monrad, J. T., Sandbrink, J. B., & Cherian, N. G. (2021) · npj Vaccines · doi:10.1038/s41541-021-00290-y · Cited by 60
Rappaport, A., Hong, S., Scallan, C. D., Gitlin, L., Akoopie, A., Boucher, G. R., Egorova, M., Espinosa, J. A., Fidanza, M., Kachura, M. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31005-z · Cited by 57
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Dangi, T., Sanchez, S., Lew, M. H., Awakoaiye, B., Visvabharathy, L., Richner, J. M., Koralnik, I. J., & Penaloza‐MacMaster, P. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112167 · Cited by 55
DeFrancesco, L. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0697-7 · Cited by 55
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Jones, H. G., Battles, M. B., Lin, C.-C., Bianchi, S., Corti, D., & McLellan, J. S. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007944 · Cited by 57
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Shin, Y., König-Beihammer, J., Vavra, U., Schwestka, J., Kienzl, N. F., Klausberger, M., Laurent, E., Grünwald‐Gruber, C., Vierlinger, K., Hofner, M., et al. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.689104 · Cited by 55
Hoque, M. N., Chaudhury, A., Akanda, M. A. M., Hossain, M. A., & Islam, T. (2020) · PeerJ · doi:10.7717/peerj.9689 · Cited by 53
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Watterson, D., Wijesundara, D. K., Modhiran, N., Mordant, F. L., Li, Z., Avumegah, M. S., McMillan, C. L. D., Lackenby, J. A., Guilfoyle, K. A., van Amerongen, G., et al. (2021) · Clinical & Translational Immunology · doi:10.1002/cti2.1269 · Cited by 53
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Wang, L., & Xiang, Y. (2020) · Viruses · doi:10.3390/v12111289 · Cited by 51
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Dong, Y., Dai, T., Wang, B., Zhang, L., Zeng, L., Huang, J., Yan, H., Zhang, L., & Zhou, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00796-w · Cited by 53
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Henderson, R. C., Edwards, R. J., Mansouri, K., Janowska, K., Stalls, V., Kopp, M., Haynes, B. F., & Acharya, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.26.173765 · Cited by 49
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Zhu, G., Zhu, C., Zhu, Y., & Sun, F. (2020) · Current Research in Microbial Sciences · doi:10.1016/j.crmicr.2020.06.003 · Cited by 54
Otto, D. P., & de Villiers, M. M. (2020) · Molecules · doi:10.3390/molecules25153415 · Cited by 64
McLeod, B., Mabrouk, M. T., Miura, K., Ravichandran, R., Kephart, S. M., Hailemariam, S., Pham, T., Semesi, A., Kucharska, I., Kundu, P., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.07.015 · Cited by 52
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Machado, B. A. S., Hodel, K. V. S., Fonseca, L. M. D. S., Mascarenhas, L. A. B., Andrade, L. P. C. D. S., Rocha, V. P. C., Soares, M. B. P., Berglund, P., Duthie, M. S., Reed, S. G., et al. (2021) · Vaccines · doi:10.3390/vaccines9111345 · Cited by 55
Rapid characterization of spike variants via mammalian cell surface display
Javanmardi, K., Chou, C., Terrace, C. I., Annapareddy, A., Kaoud, T. S., Guo, Q., Lutgens, J., Zorkic, H., Horton, A. P., Gardner, E. C., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.024 · Cited by 54
Antigen- 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 50
Self-citationNel, A. E., & Miller, J. F. (2021) · ACS Nano · doi:10.1021/acsnano.1c01845 · Cited by 50
Mandolesi, M., Sheward, D. J., Hanke, L., Ma, J., Pushparaj, P., Vidakovics, L. P., Kim, C., Ádori, M., Lenart, K., Loré, K., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100252 · Cited by 46
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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 45
Metadata
- Authors
- Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., Kong, W.-P., Andres, E. L., Kettenbach, A. N., Denison, M. R., Chappell, J. D., Graham, B. S., Ward, A. B., & McLellan, J. S.
- Affiliations
- Scripps Research Institute (US)
- Dartmouth College (US)
- National Institute of Allergy and Infectious Diseases (US)
- Vanderbilt University Medical Center (US)
- Vanderbilt University (US)
- Corresponding author
- Pallesen, Jesper
- Wang, Nianshuang
- Corbett, Kizzmekia S.
- Ward, Andrew B.
- McLellan, Jason S.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-08-14
- Volume
- 114
- Issue
- 35
- Pages
- E7348-E7357
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5584442
- OpenAlex
- W2750464792
- Cited by
- 1,073
- References
- 89
- Citations by year
- 2026: 48 · 2025: 75 · 2024: 98 · 2023: 127 · 2022: 174 · 2021: 275 · 2020: 220 · 2019: 31 · 2018: 17 · 2017: 6
- FWCI
- 57.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (R01AI127521)
- HHS | NIH | National Institute of General Medical Sciences (P20GM113132)
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases (AI005125)
- 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
- MERS-CoV, spike protein, structure-based vaccine design, neutralizing antibodies, receptor binding domain, receptor recognition, membrane fusion mechanism, coronavirus vaccines
- MeSH terms
- Animals, Antibodies, Viral, Coronaviridae, Humans, Immunoglobulin G, Mice, Inbred BALB C, Protein Binding, Protein Conformation, Receptors, Virus, Structure-Activity Relationship, Vaccination, Viral Vaccines, Coronavirus Infections, Crystallography, X-Ray, Immunity, Humoral, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus, Middle East Respiratory Syndrome Coronavirus
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