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Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Open accessAbstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2–6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9–12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Cryo-electron microscopy and tomography studies reveal the structures, conformations and distributions of spike protein trimers on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions and provide a basis for understanding the interactions of the spike protein with neutralizing antibodies.
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Cites
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
A novel coronavirus from patients with pneumonia in China, 2019
Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281
Structural basis of receptor recognition by SARS-CoV-2
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.045 · Cited by 2,892
Distinct conformational states of SARS-CoV-2 spike protein
Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221
Snijder, E. J., Limpens, R. W. A. L., de Wilde, A. H., de Jong, A. W. M., Zevenhoven-Dobbe, J. C., Maier, H. J., Faas, F. F. G. A., Koster, A. J., & Bárcena, M. (2020) · PLOS Biology · doi:10.1371/journal.pbio.3000715 · Cited by 477
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Evolution of antibody immunity to SARS-CoV-2
Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674
mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
Wang, Z., Schmidt, F., Weisblum, Y., Muecksch, F., Barnes, C. O., Finkin, S., Schaefer-Babajew, D., Cipolla, M., Gaebler, C., Lieberman, J. A., et al. (2021) · Nature · doi:10.1038/s41586-021-03324-6 · Cited by 1,343
Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178
Molecular Architecture of the SARS-CoV-2 Virus
Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060
“The slight dilation and lower local resolution (Figure S3A and S3B) of the NTD on the native spike against recombinant spike structures was also observed on the other cryo-ET structures (Ke et al., 2020).”
InfluentialSARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Dejnirattisai, W., Huo, J., Zhou, D., Zahradník, J., Supasa, P., Liu, C., Duyvesteyn, H. M. E., Ginn, H. M., Mentzer, A. J., Tuekprakhon, A., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.046 · Cited by 930
“Indeed, rapidly prepared virus particles tend to have RBDs closer to locked-down state (Ke et al., 2020).”
Liu, 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
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
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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
SARS-CoV-2 escape in vitro from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451
“The main target of vaccines and mAbs is the SARS-CoV-2 spike protein (S-protein), a large class I trimeric fusion protein which plays a key role in viral pathogenesis (3, 5, 6).”
Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · doi:10.1101/2020.12.31.425021 · Cited by 1,178
Liu, 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. (2020) · doi:10.1101/2020.11.06.372037 · Cited by 135
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
“…constrained access to their cognate epitope, as 50% of S trimers have all three RBDs closed, whereas the remaining half possess a single open RBD (Ke et al., 2020; Walls et al., 2020b), and the proximity of the epitopes on neighboring RBDs might not be compatible with multiple immunoglobulin G…”
Molecular architecture and dynamics of SARS-CoV-2 envelope by integrative modeling
Pezeshkian, W., Grünewald, F., Narykov, O., Lu, S., Arkhipova, V., Solodovnikov, A., Wassenaar, T. A., Marrink, S. J., & Korkin, D. (2023) · Structure · doi:10.1016/j.str.2023.02.006 · Cited by 60
Viral and host factors regulating HIV-1 envelope protein trafficking and particle incorporation
Anokhin, B., & Spearman, P. (2022) · Viruses · doi:10.3390/v14081729 · Cited by 21
Immunogenicity 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
Gonzalez-Magaldi, M., Gullapalli, A., Papoulas, O., Liu, C., Leung, A. Y.-H., Guo, L., Brilot, A. F., Marcotte, E. M., Ke, Z., & Leahy, D. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2424678122 · Cited by 17
Self-citationHastie, K. M., Salie, Z. L., Ke, Z., Halfmann, P. J., DeWald, L. E., McArdle, S., Grinyó, A., Davidson, E., Schendel, S. L., Hariharan, C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56452-2 · Cited by 9
Self-citationHigh-resolution real-space reconstruction of cryo-EM structures using a neural field network
Huang, Y., Zhu, C., Yang, X., & Liu, M. (2024) · Nature Machine Intelligence · doi:10.1038/s42256-024-00870-2 · Cited by 9
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
Borges, R. J., Salvador, G. H. M., Pimenta, D. C., dos Santos, L. D., Fontes, M. R. M., & Usón, I. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac029 · Cited by 5
Inhibition of SARS-CoV-2 3CL protease by the anti-viral chimeric protein RetroMAD1
Chan, L.-C., Mat Yassim, A. S., Ahmad Fuaad, A. A. H., Leow, T. C., Sabri, S., Radin Yahaya, R. S., & Abu Bakar, A. M. S. (2023) · Scientific Reports · doi:10.1038/s41598-023-47511-z · Cited by 5
Li, J., Xing, H., Meng, F., Liu, T., Hong, X., Han, X., Dong, Y., Li, M., Wang, Z., Zhang, S., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c01277 · Cited by 2
Kaizuka, Y., & Machida, R. (2025) · eLife · doi:10.7554/elife.101175.3 · Cited by 2
Metadata
- Authors
- Ke, Z., Oton, J., Qu, K., Cortese, M., Zila, V., McKeane, L., Nakane, T., Zivanov, J., Neufeldt, C. J., Cerikan, B., Lu, J. M., Peukes, J., Xiong, X., Kräusslich, H.-G., Scheres, S. H. W., Bartenschlager, R., & Briggs, J. A. G.
- Venue
- Nature
- Published
- 2020-08-17
- Volume
- 588
- Issue
- 7838
- Pages
- 498-502
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W3049142173
- Cited by
- 1,149
- References
- 8
- FWCI
- 25.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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