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Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Open accessAbstract
Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.
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“Protection is thought to be mediated by neutralizing antibodies against the S protein (7, 8)”
From An Alphavirus -derived replicon RNA vaccine induces SARS-CoV-2 neutralizing antibody and T cell responses in mice and nonhuman primates (2020) · cites this paper as [7]
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Cites
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
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
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
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
Inference of Macromolecular Assemblies from Crystalline State
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,007
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
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Items 201–300 of 587
Zeng, X. W., Li, L., Lin, J., Li, X., Liu, B., Kong, Y., Zeng, S., Du, J., Xiao, H., Zhang, T., et al. (2020) · Antibody Therapeutics · doi:10.1093/abt/tbaa008 · Cited by 53
In silico trial to test COVID-19 candidate vaccines: a case study with UISS platform
Russo, G. L., Pennisi, M. A., Fichera, E., Motta, S., Raciti, G., Viceconti, M., & Pappalardo, F. (2020) · BMC Bioinformatics · doi:10.1186/s12859-020-03872-0 · Cited by 56
Spike Glycoprotein-Mediated Entry of SARS Coronaviruses
Wang, L., & Xiang, Y. (2020) · Viruses · doi:10.3390/v12111289 · Cited by 51
Glycans on the SARS-CoV-2 Spike Control the Receptor Binding Domain ConformationPreprint
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
Minireview of progress in the structural study of SARS-CoV-2 proteins
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
COVID-19 during Pregnancy and Postpartum:
Naidu, S. A. G., Clemens, R., Pressman, P., Zaigham, M., Kadkhoda, K., Davies, K. J. A., & Naidu, A. S. (2020) · Journal of Dietary Supplements · doi:10.1080/19390211.2020.1834049 · Cited by 57
Inter-domain communication in SARS-CoV-2 spike proteins controls protease-triggered cell entry
Qing, E., Li, P., Cooper, L. M., Schulz, S. R., Jäck, H., Rong, L., Perlman, S. M., & Gallagher, T. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110786 · Cited by 45
Somasundaram, R., Choraria, A., & Antonysamy, M. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106654 · Cited by 51
Biparatopic sybodies neutralize SARS‐CoV‐2 variants of concern and mitigate drug resistance
Walter, J. D., Hutter, C. A. J., Garaeva, A. A., Scherer, M., Zimmermann, I., Wyss, M., Rheinberger, J., Ruedin, Y., Earp, J. C., Egloff, P., et al. (2022) · EMBO Reports · doi:10.15252/embr.202154199 · Cited by 49
Liu, T., Wu, S., Tao, H., Zeng, G., Zhou, F., Guo, F., & Wang, X. (2020) · medRxiv · doi:10.1101/2020.06.13.20130252 · Cited by 51
Human coronavirus HKU1 recognition of the TMPRSS2 host receptor
McCallum, M., Park, Y., Stewart, C., Sprouse, K. R., Addetia, A., Brown, J. T., Tortorici, M. A., Gibson, C. A., Wong, E., Ieven, M. M., et al. (2024) · Cell · doi:10.1016/j.cell.2024.06.006 · Cited by 51
Self-citationVashi, Y., Jagrit, V., & Kumar, S. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104382 · Cited by 48
Cao, L., & Liu, Q. (2024) · ACM Computing Surveys · doi:10.1145/3686150 · Cited by 52
Knyazev, E. N., Nersisyan, S. A., & Tonevitsky, A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636966 · Cited by 47
Maeda, R., Fujita, J., Konishi, Y., Kazuma, Y., Yamazaki, H., Anzai, I., Watanabe, T., Yamaguchi, K., Kasai, K., Nagata, K., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03630-3 · Cited by 47
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 47
Self-citationJia, X., Liu, Y., Wagner, A. M., Chen, M. M., Zhao, Y., Smith, K. J., Some, D., Abend, A. M., & Pennington, J. P. (2021) · Journal of Chromatography B · doi:10.1016/j.jchromb.2021.123015 · Cited by 45
Structure‐guided envelope trimer design in HIV‐1 vaccine development: a narrative review
Derking, R., & Sanders, R. W. (2021) · Journal of the International AIDS Society · doi:10.1002/jia2.25797 · Cited by 46
Balkrishna, A., Solleti, S. K., Verma, S., & Varshney, A. (2020) · Molecules · doi:10.3390/molecules25215091 · Cited by 42
Song, X., Shi, Y., Ding, W., Niu, T., Sun, L., Tan, Y., Chen, Y., Shi, J., Xiong, Q., Huang, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20401-y · Cited by 42
Conformational flexibility and structural variability of SARS-CoV2 S protein
Pramanick, I., Sengupta, N., Mishra, S., Pandey, S., Girish, N., Das, A., & Dutta, S. (2021) · Structure · doi:10.1016/j.str.2021.04.006 · Cited by 43
Zhou, T., Tsybovsky, Y., Olia, A. S., Gorman, J., Rapp, M., Cerutti, G., Chuang, G., Katsamba, P. S., Nazzari, A. F., Sampson, J. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.04.187989 · Cited by 48
SARS-CoV-2 spike protein: flexibility as a new target for fighting infection
Pierri, C. L. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00369-3 · Cited by 42
Hanna, R., Dalvi, S., Sălăgean, T., Pop, I., Bordea, I. R., & Benedicenti, S. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s282213 · Cited by 42
Pan, Y., Du, J., Liu, J., Wu, H., Gui, F., Zhang, N., Deng, X., Song, G., Li, Y., Lu, J., et al. (2021) · Cell Discovery · doi:10.1038/s41421-021-00295-w · Cited by 44
Spike protein binding prediction with neutralizing antibodies of SARS-CoV-2Preprint
Park, T., Lee, S.-Y., Kim, S., Kim, M. J., Kim, H. G., Jun, S., Kim, S. I., Kim, B., Park, E. C., & Park, D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.22.951178 · Cited by 42
Neutralizing antibodies against SARS-CoV-2: current understanding, challenge and perspective
Huang, Y., Sun, H., Yu, H. J., Li, S., Zheng, Q., & Xia, N. (2020) · Antibody Therapeutics · doi:10.1093/abt/tbaa028 · Cited by 40
Wyganowska‐Świątkowska, M., Nohawica, M., Grocholewicz, K., & Nowak, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134639 · Cited by 40
Primed for global coronavirus pandemic: Emerging research and clinical outcome
Ahamad, S., Branch, S., Harrelson, S., Hussain, M. K., Saquib, M., & Khan, S. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112862 · Cited by 39
Beaudoin, C. A., Jamasb, A. R., Alsulami, A. F., Copoiu, L., van Tonder, A. J., Hala, S. M., Bannerman, B. P., Thomas, S. E., Vedithi, S. C., Torres, P. H. M., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.06.041 · Cited by 36
Glycan shield of the ebolavirus envelope glycoprotein GP
Peng, W., Rayaprolu, V., Parvate, A. D., Pronker, M. F., Hui, S., Parekh, D. V., Shaffer, K. C. L., Yu, X., Saphire, E. O., & Snijder, J. (2022) · Communications Biology · doi:10.1038/s42003-022-03767-1 · Cited by 42
Self-citationYu, S., Wang, J., & Shen, H. (2020) · Annals of Palliative Medicine · doi:10.21037/apm.2020.03.27 · Cited by 38
Potent monoclonal antibody–mediated neutralization of a divergent Hendra virus variant
Wang, Z., Dang, H. V., Amaya, M., Xu, Y., Yin, R., Yan, L., Hickey, A. C., Annand, E. J., Horsburgh, B. A., Reid, P. A., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122769119 · Cited by 37
Self-citationStructure-based neutralizing mechanisms for SARS-CoV-2 antibodies
Huang, Q., Han, X., & Yan, J. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2125348 · Cited by 37
Zhao, X., Ma, X., Guo, J., Mi, M., Wang, K., Zhang, C., Tang, X., Chang, L., Huang, Y., & Tong, D. (2019) · International Journal of Biological Sciences · doi:10.7150/ijbs.36532 · Cited by 35
Konwarh, R. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01531 · Cited by 36
Review of COVID-19 Antibody Therapies
Chen, J., Gao, K., Wang, R., Nguyen, D. D., & Wei, G. (2020) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-062920-063711 · Cited by 37
Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein
Zhang, S., Go, E. P., Ding, H., Anang, S., Kappes, J. C., Desaire, H., & Sodroski, J. (2021) · Journal of Virology · doi:10.1128/jvi.01626-21 · Cited by 39
Hurdiss, D. L., Drulyte, I., Lang, Y., Shamorkina, T. M., Pronker, M. F., van Kuppeveld, F. J. M., Snijder, J., & de Groot, R. J. (2020) · Nature Communications · doi:10.1038/s41467-020-18440-6 · Cited by 38
Self-citationTelles, C. R., Roy, A., Ajmal, M. R., Mustafa, S. K., Ahmad, M. A., de la Serna, J. M., Frigo, E. P., & Rosales, M. H. (2021) · JMIR Public Health and Surveillance · doi:10.2196/20699 · Cited by 35
Catch Me if You Can: Superspreading of COVID-19
Lakdawala, S. S., & Menachery, V. D. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.05.002 · Cited by 33
SpySwitch 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
Broad 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 33
Self-citationSohrabi, Y., dos Santos, J. C., Dorenkamp, M., Findeisen, H. M., Godfrey, R., Netea, M. G., & Joosten, L. A. B. (2020) · Clinical & Translational Immunology · doi:10.1002/cti2.1228 · Cited by 34
Site-specific N-glycosylation Characterization of Recombinant SARS-CoV-2 Spike ProteinsPreprint
Zhang, Y., Zhao, W., Mao, Y., Chen, Y., Wang, S., Zhong, Y., Su, T., Gong, M., Du, D., Lu, X., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.28.013276 · Cited by 37
Forecasting the timeframe of 2019-nCoV and human cells interaction with reverse engineering
Sohail, A., & Nutini, A. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.04.002 · Cited by 33
Patil, P., Shetty, P. K., Kuriakose, N., Gollapalli, P., Shetty, S., Bhandary, R. R., Vishwanatha, J. K., & Ghate, S. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011028 · Cited by 33
Guan, H., Wang, Y., Perčulija, V., Saeed, A. F. U. H., Liu, Y., Li, J., Jan, S. S., Li, Y., Zhu, P., & Ouyang, S. (2020) · Journal of Virology · doi:10.1128/jvi.01301-20 · Cited by 34
2020 update on human coronaviruses: One health, one world
Zhao, X., Ding, Y., Du, J., & Fan, Y. (2020) · Medicine in Novel Technology and Devices · doi:10.1016/j.medntd.2020.100043 · Cited by 36
Requena, D., Médico, A., Chacón, R. D., Ramírez, M., & Marín-Sánchez, O. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.02008 · Cited by 34
Double lock of a potent human therapeutic monoclonal antibody against SARS-CoV-2
Zhu, L., Deng, Y., Zhang, R.-R., Cui, Z., Sun, C.-Y., Fan, C., Xing, X., Huang, W., Chen, Q., Zhang, N.-N., et al. (2020) · National Science Review · doi:10.1093/nsr/nwaa297 · Cited by 34
Demers‐Mathieu, V., DaPra, C., Mathijssen, G. B., Sela, D. A., Järvinen, K. M., Seppo, A., Fels, S., & Medo, E. T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041749 · Cited by 32
Gastrointestinal implications in COVID-19
Dahiya, D. S., Kichloo, A., Albosta, M. S., Pagad, S., & Wani, F. (2020) · Journal of Investigative Medicine · doi:10.1136/jim-2020-001559 · Cited by 34
Perrella, F., Coppola, F., Petrone, A., Platella, C., Montesarchio, D., Stringaro, A., Ravagnan, G., Fuggetta, M. P., Rega, N., & Musumeci, D. (2021) · Biomolecules · doi:10.3390/biom11071048 · Cited by 32
Label-free methods for optical in vitro characterization of protein–protein interactions
Soltermann, F., Struwe, W. B., & Kukura, P. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp01072g · Cited by 32
Tian, Y., Parsons, L. M., Jankowska, E. A., & Cipollo, J. F. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.767448 · Cited by 29
Rouzbahani, A. K., Kheirandish, F., & Hosseini, S. Z. (2022) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-022-00224-w · Cited by 32
Cocherie, T., Zafilaza, K., Leducq, V., Marot, S., Cálvez, V., Marcelin, A., & Todesco, È. (2022) · Microorganisms · doi:10.3390/microorganisms11010030 · Cited by 33
Custódio, T. F., Das, H., Sheward, D. J., Hanke, L., Pažický, S., Pieprzyk, J., Sorgenfrei, M., Schroer, M. A., Gruzinov, A. Y., Jeffries, C. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.23.165415 · Cited by 32
Verkhivker, G. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218268 · Cited by 29
Kawase, M., Kataoka, M., Shirato, K., & Matsuyama, S. (2019) · Journal of Virology · doi:10.1128/jvi.00785-19 · Cited by 32
Highly potent anti-SARS-CoV-2 multivalent DARPin therapeutic candidatesPreprint
Walser, M., Rothenberger, S., Hurdiss, D. L., Schlegel, A., Calabro, V., Fontaine, S., Villemagne, D., Paladino, M., Hospodarsch, T., Neculcea, A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.25.256339 · Cited by 30
Li, Y., Wang, T., Zhang, J., Shao, B., Gong, H., Wang, Y., He, X., Liu, S., & Liu, T. (2021) · Advanced Theory and Simulations · doi:10.1002/adts.202100152 · Cited by 29
Erasmus, J. H., Khandhar, A. P., Walls, A. C., Hemann, E. A., O’Connor, M. A., Murapa, P., Archer, J. F., Leventhal, S. S., Fuller, J., Lewis, T. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.28.121640 · Cited by 30
Self-citationStructure 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-citationImpact of glycan cloud on the B-cell epitope prediction of SARS-CoV-2 Spike protein
Wintjens, R. T., Bifani, A. M., & Bifani, P. J. (2020) · npj Vaccines · doi:10.1038/s41541-020-00237-9 · Cited by 29
Thakur, N., Conceicao, C., Isaacs, A., Human, S., Modhiran, N., McLean, R. K., Pedrera, M., Tan, T. K., Rijal, P., Townsend, A., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001506 · Cited by 25
SARS-CoV-2, Early Entry Events
CHAMBERS, J. K., Yu, J., Valdés, J. J., & Arulanandam, B. P. (2020) · Journal of Pathogens · doi:10.1155/2020/9238696 · Cited by 32
Freitas, F. C., Ferreira, P. H. B., Favaro, D. C., & de Oliveira, R. J. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01320 · Cited by 29
Biagioli, M., Marchianò, S., Roselli, R., Giorgio, C. D., Bellini, R., Bordoni, M., Gidari, A., Sabbatini, S., Francisci, D., Fiorillo, B., et al. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114564 · Cited by 29
Kim, Y. S., Chung, H., Noh, S. G., Lee, B., Chung, H. Y., & Choi, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168604 · Cited by 29
Widyasari, K., & Kim, J. N. (2023) · Antibodies · doi:10.3390/antib12010005 · Cited by 29
Innate and adaptive immunity to SARS-CoV-2 and predisposing factors
Shen, J., Fan, J., Zhao, Y., Jiang, D., Niu, Z., Zhang, Z., & Cao, G. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1159326 · Cited by 38
Zhan, X.-Y., Zhang, Y., Zhou, X., Huang, K., Qian, Y., Leng, Y., Yan, L., Huang, B., & He, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.25.170688 · Cited by 29
Neutralizing Aptamers Block S/RBD‐ACE2 Interactions and Prevent Host Cell Infection
Liu, X., Wang, Y., Wu, J., Qi, J., Zeng, Z., Wan, Q., Chen, Z., Manandhar, P., Cavener, V. S., Boyle, N. R., et al. (2021) · Angewandte Chemie · doi:10.1002/ange.202100345 · Cited by 28
Hu, Y., & Buehler, M. J. (2022) · ACS Nano · doi:10.1021/acsnano.2c07681 · Cited by 26
Noman, A., Aqeel, M. A., Khalid, N., Hashem, M., Alamari, S., Zafar, S., Qasim, M. U., Irshad, M. S., & Qari, S. H. (2020) · Microbial Pathogenesis · doi:10.1016/j.micpath.2020.104719 · Cited by 28
Schön, M. P., Berking, C., Biedermann, T., Buhl, T., Erpenbeck, L., Eyerich, K., Eyerich, S., Ghoreschi, K., Goebeler, M., Ludwig, R. J., et al. (2020) · JDDG Journal der Deutschen Dermatologischen Gesellschaft · doi:10.1111/ddg.14169_g · Cited by 28
Union is strength: antiviral and anti-inflammatory drugs for COVID-19
Naveja, J. J., Madariaga‐Mazón, A., Flores‐Murrieta, F. J., Granados‐Montiel, J., Maradiaga‐Ceceña, M. A., Duarte-Alaniz, V., Maldonado-Rodriguez, M., García-Morales, J., Senosiain, J. P., & Martínez‐Mayorga, K. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.10.018 · Cited by 29
Sertraline Is an Effective SARS-CoV-2 Entry Inhibitor Targeting the Spike Protein
Chen, Y., Wu, Y., Chen, S., Zhan, Q., Wu, D., Yang, C., He, X., Qiu, M., Zhang, N., Li, Z., et al. (2022) · Journal of Virology · doi:10.1128/jvi.01245-22 · Cited by 27
Torchia, J. A., Tavares, A. H., Carstensen, L. S., Chen, D. W., Huang, J., Xiao, T., Mukherjee, S., Reeves, P. M., Tu, H., Sluder, A. E., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq6527 · Cited by 25
Cryo-EM Studies of Virus-Antibody Immune Complexes
Li, N., Li, Z., Fu, Y., & Cao, S. (2020) · Virologica Sinica · doi:10.1007/s12250-019-00190-5 · Cited by 27
El-hoshoudy, A. N. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.113968 · Cited by 26
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Lempp, F., Soriaga, L. B., Montiel-Ruiz, M., Benigni, F., Noack, J., Park, Y.-J., Bianchi, S., Walls, A., Bowen, J., Zhou, J.-Y., et al. (2021) · bioRxiv · doi:10.1101/2021.04.03.438258 · Cited by 22
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Yu, H., Liu, B., Zhang, Y., Gao, X., Wang, Q., Xiang, H., Peng, X., Xie, C., Wang, Y., Hu, P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36761-0 · Cited by 24
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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) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.15.096511 · Cited by 23
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Metadata
- Authors
- Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., Zambon, M., Rey, F. A., Corti, D., & Veesler, D.
- Affiliations
- University of Washington (US)
- Centre National de la Recherche Scientifique (FR)
- Vir Biotechnology (Switzerland) (CH)
- Public Health England (GB)
- The Francis Crick Institute (GB)
- Institute for Research in Biomedicine (CH)
- Corresponding author
- Veesler, David
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 176
- Issue
- 5
- Pages
- 1026-1039.e15
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC6751136
- OpenAlex
- W2915009278
- Cited by
- 582
- References
- 85
- Citations by year
- 2026: 7 · 2025: 25 · 2024: 30 · 2023: 40 · 2022: 79 · 2021: 173 · 2020: 214 · 2019: 14
- FWCI
- 92.33
- Type
- journal article
- Language
- en
- Update notices
- erratum (2020-12-10)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- National Institute of General Medical Sciences (R01GM120553)
- National Institute of Allergy and Infectious Diseases (HHSN272201700059C)
- Pew Biomedical Scholars Award
- Burroughs Wellcome Fund
- Netherlands Organisation for Scientific Research (Rubicon 019.2015.2.310.006)
- European Molecular Biology Organization (ALTF933-2015)
- Zoonoses Anticipation and Preparedness Initiative (IMI115760)
- Pasteur Institute
- Centre National de la Recherche Scientifique
- LabEx Integrative Biology of Emerging Infectious Diseases
- University of Washington Arnold and Mabel Beckman CryoEM Center and Proteomics Resource (UWPR95794)
- Advanced Light Source at Lawrence Berkley National Laboratory
- 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
- SARS-CoV, MERS-CoV, neutralizing antibodies, antibody-antigen complex structure, humoral immune response, viral entry, receptor binding
- MeSH terms
- Animals, Antibodies, Monoclonal, Antibodies, Viral, Chlorocebus aethiops, Humans, Protein Binding, Receptors, Virus, Vero Cells, Coronavirus, Coronavirus Infections, Molecular Mimicry, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Immunity, Humoral, Antibodies, Neutralizing, HEK293 Cells, Spike Glycoprotein, Coronavirus, Middle East Respiratory Syndrome Coronavirus
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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.
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