The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
Open accessAbstract
The tremendous pandemic potential of coronaviruses was demonstrated twice in the past few decades by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor-binding and membrane fusion functions. S also contains the principal antigenic determinants and is the target of neutralizing antibodies. Here we present the structure of a mouse coronavirus S trimer ectodomain determined at 4.0 Å resolution by single particle cryo-electron microscopy. It reveals the metastable pre-fusion architecture of S and highlights key interactions stabilizing it. The structure shares a common core with paramyxovirus F proteins, implicating mechanistic similarities and an evolutionary connection between these viral fusion proteins. The accessibility of the highly conserved fusion peptide at the periphery of the trimer indicates potential vaccinology strategies to elicit broadly neutralizing antibodies against coronaviruses. Finally, comparison with crystal structures of human coronavirus S domains allows rationalization of the molecular basis for species specificity based on the use of spatially contiguous but distinct domains.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489
Self-citationStructure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody
McLellan, J. S., Chen, M., Leung, S., Graepel, K. W., Du, X., Yang, Y., Zhou, T., Baxa, U., Yasuda, E., Beaumont, T., et al. (2013) · Science · doi:10.1126/science.1234914 · Cited by 883
Proof of principle for epitope-focused vaccine design
Correia, B. E., Bates, J. T., Loomis, R. J., Baneyx, G., Carrico, C., Jardine, J. G., Rupert, P., Correnti, C., Kalyuzhniy, O., Vittal, V., et al. (2014) · Nature · doi:10.1038/nature12966 · Cited by 555
Cited by
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
Self-citationStructure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Self-citationStructural and functional analysis of a potent sarbecovirus neutralizing antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · doi:10.1101/2020.04.07.023903 · Cited by 1,752
Self-citationSARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599
SARS-CoV-2 mRNA Vaccine Design Enabled by Prototype Pathogen Preparedness
Corbett, K. S., Edwards, D. K., Leist, S. R., Abiona, O. M., Boyoglu-Barnum, S., Gillespie, R. A., Himansu, S., Schäfer, A., Ziwawo, C. T., DiPiazza, A. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2622-0 · Cited by 1,615
Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
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., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795
Structural insights into coronavirus entry
(2019) · Advances in Virus Research · doi:10.1016/bs.aivir.2019.08.002 · Cited by 769
TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells
Bestle, D., Heindl, M. R., Limburg, H., Van Lam van, T., Pilgram, O., Moulton, H., Stein, D. A., Hardes, K., Eickmann, M., Dolnik, O., et al. (2020) · Life Science Alliance · doi:10.26508/lsa.202000786 · Cited by 815
Casagrande, M., Favieri, F., Tambelli, R., & Forte, G. (2020) · Sleep Medicine · doi:10.1016/j.sleep.2020.05.011 · Cited by 735
Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
Wrapp, D., De Vlieger, D., Corbett, K. S., Torres, G. M., Wang, N., Van Breedam, W., Roose, K., van Schie, L., Hoffmann, M., Pöhlmann, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.031 · Cited by 610
Advances in COVID-19 mRNA vaccine development
Fang, E., Liu, X., Li, M., Zhang, Z., Song, L., Zhu, B., Wu, X., Liu, J., Zhao, D., & Li, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00950-y · Cited by 601
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
Self-citationStructural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535
“2) ( 16 , 17 ).”
Self-citationWalls, 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
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
Self-citationKirchdoerfer, R. N., Wang, N., Pallesen, J., Wrapp, D., Turner, H. L., Cottrell, C. A., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2018) · Scientific Reports · doi:10.1038/s41598-018-34171-7 · Cited by 466
Domains and Functions of Spike Protein in SARS-Cov-2 in the Context of Vaccine Design
Xia, X. (2021) · Viruses · doi:10.3390/v13010109 · Cited by 319
A thermostable, closed SARS-CoV-2 spike protein trimer
Xiong, X., Qu, K., Ciazynska, K. A., Hosmillo, M., Carter, A. P., Ebrahimi, S., Ke, Z., Scheres, S. H. W., Bergamaschi, L., Grice, G. L., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0478-5 · Cited by 313
Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0334-7 · Cited by 260
Self-citationNext‐Generation Vaccines: Nanoparticle‐Mediated DNA and mRNA Delivery
Ho, W., Gao, M., Li, F., Li, Z., Zhang, X., & Xu, X. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202001812 · Cited by 261
Structure-Based Vaccine Antigen Design
Graham, B. S., Gilman, M. S. A., & McLellan, J. S. (2019) · Annual Review of Medicine · doi:10.1146/annurev-med-121217-094234 · Cited by 234
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., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.015 · Cited by 185
Self-citationA Comprehensive Review About SARS-CoV-2
Haque, S. M., Ashwaq, O., Sarief, A., & Azad John Mohamed, A. K. (2020) · Future Virology · doi:10.2217/fvl-2020-0124 · Cited by 121
Widjaja, I., Wang, C., van Haperen, R., Gutiérrez-Álvarez, J., van Dieren, B., Okba, N. M. A., Raj, V. S., Li, W., Fernandez-Delgado, R., Grosveld, F., et al. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1597644 · Cited by 115
Self-citationStructural Definition of a Neutralization-sensitive Epitope on the MERS-CoV S1-NTD
Wang, N., Rosen, O., Wang, L., Turner, H. L., Stevens, L. J., Corbett, K. S., Bowman, C. A., Pallesen, J., Shi, W., Zhang, Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.052 · Cited by 86
Immunogenicity and efficacy of mRNA COVID-19 vaccine MRT5500 in preclinical animal models
Kalnin, K. V., Plitnik, T., Kishko, M., Zhang, J., Zhang, D., Beauvais, A., Anosova, N. G., Tibbitts, T., DiNapoli, J., Ulinski, G., et al. (2021) · npj Vaccines · doi:10.1038/s41541-021-00324-5 · Cited by 82
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.07.027 · Cited by 78
“…mediate host cell attachment (S1 subunit, formed by four domains, the most relevant being the N-terminal domain [NTD] and receptor-binding domain [RBD]) and fusion of the viral and cellular membranes (S2 subunit) (Tortorici and Veesler, 2019; Walls et al., 2016, 2020b; Wrapp et al., 2020).”
Self-citationCoronavirus entry: how we arrived at SARS-CoV-2
Whittaker, G. R., Daniel, S., & Millet, J. K. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.02.006 · Cited by 67
Preclinical evaluation of a SARS-CoV-2 mRNA vaccine PTX-COVID19-B
Liu, J., Budylowski, P., Samson, R., Griffin, B. D., Babuadze, G., Rathod, B., Colwill, K., Abioye, J. A., Schwartz, J. A., Law, R., et al. (2022) · Science Advances · doi:10.1126/sciadv.abj9815 · Cited by 56
Structure and design of Langya virus glycoprotein antigens
Wang, Z., McCallum, M., Yan, L., Gibson, C. A., Sharkey, W., Park, Y.-J., Dang, H. V., Amaya, M., Person, A., Broder, C. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314990121 · Cited by 32
Self-citationMechanism of receptor assembly via the pleiotropic adipokine Leptin
Tsirigotaki, A., Dansercoer, A., Verschueren, K. H. G., Marković, I., Pollmann, C., Hafer, M., Felix, J., Birck, C., Van Putte, W., Catteeuw, D., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00941-9 · Cited by 29
A broadly generalizable stabilization strategy for sarbecovirus fusion machinery vaccines
Lee, J., Stewart, C., Schäfer, A., Leaf, E. M., Park, Y.-J., Asarnow, D., Powers, J. M., Treichel, C., Sprouse, K. R., Corti, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49656-5 · Cited by 23
Self-citationDu, W., Debski-Antoniak, O., Drabek, D., van Haperen, R., van Dortmondt, M., van der Lee, J., Drulyte, I., van Kuppeveld, F. J. M., Grosveld, F., Hurdiss, D. L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49693-0 · Cited by 19
Self-citationWang, C., van Haperen, R., Gutiérrez-Álvarez, J., Li, W., Okba, N. M. A., Albulescu, I., Widjaja, I., van Dieren, B., Fernandez-Delgado, R., Sola, I., et al. (2020) · doi:10.1101/2020.10.20.346916 · Cited by 15
Self-citationImmunogenicity of novel mRNA COVID-19 vaccine MRT5500 in mice and non-human primates
Kalnin, K. V., Plitnik, T., Kishko, M., Zhang, J., Zhang, D., Beauvais, A., Anosova, N. G., Tibbitts, T., DiNapoli, J. M., Huang, P.-W. D., et al. (2020) · doi:10.1101/2020.10.14.337535 · Cited by 18
Calcraft, T., Stanke-Scheffler, N., Nans, A., Lindemann, D., Taylor, I. A., & Rosenthal, P. B. (2024) · Cell · doi:10.1016/j.cell.2024.06.017 · Cited by 14
Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395
Self-citationMechanism of receptor assembly via the pleiotropic adipokine Leptin
Tsirigotaki, A., Dansercoer, A., Verschueren, K. H. G., Marković, I., Pollmann, C., Hafer, M., Felix, J., Birck, C., Van Putte, W., Catteeuw, D., et al. (2022) · doi:10.1101/2022.12.01.518327 · Cited by 2
Metadata
- Authors
- Walls, A. C., Tortorici, M. A., Bosch, B.-J., Frenz, B., Rottier, P. J. M., DiMaio, F., Rey, F. A., & Veesler, D.
- Venue
- Nature
- Published
- 2016-02-08
- Volume
- 531
- Issue
- 7592
- Pages
- 114-117
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2271364844
- Cited by
- 538
- References
- 5
- FWCI
- 30.52
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
