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Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite
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Abstract
Numerous antibodies that neutralize SARS-CoV-2 have been identified, and these generally target either the receptor-binding domain (RBD) or the N-terminal domain (NTD) of the viral spike. While RBD-directed antibodies have been extensively studied, far less is known about NTD-directed antibodies. Here, we report cryo-EM and crystal structures for seven potent NTD-directed neutralizing antibodies in complex with spike or isolated NTD. These structures defined several antibody classes, with at least one observed in multiple convalescent donors. The structures revealed that all seven antibodies target a common surface, bordered by glycans N17, N74, N122, and N149. This site-formed primarily by a mobile β-hairpin and several flexible loops-was highly electropositive, located at the periphery of the spike, and the largest glycan-free surface of NTD facing away from the viral membrane. Thus, in contrast to neutralizing RBD-directed antibodies that recognize multiple non-overlapping epitopes, potent NTD-directed neutralizing antibodies appear to target a single supersite.
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“Neutralizing mAbs that bind regions of the viral spike have also been identified (24, 33, 38–42).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [40]
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“that would be predicted to disrupt the so-called “super site” on the NTD mediating neutralization (Cerutti et al., 2021; Figure S2)”
From Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum (2021) · cites this paper as Cerutti et al., 2021
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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 45,882
MUSCLE: multiple sequence alignment with high accuracy and high throughput
Edgar, R. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh340 · Cited by 44,662
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
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
MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
Katoh, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf436 · Cited by 17,027
SWISS-MODEL: homology modelling of protein structures and complexes
Waterhouse, A. M., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., de Beer, T., Rempfer, C., Bordoli, L., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky427 · Cited by 13,248
Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
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
An interactive web-based dashboard to track COVID-19 in real time
Dong, E., Du, H., & Gardner, L. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30120-1 · Cited by 10,048
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
UCSF ChimeraX : Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,521
CHARMM‐GUI: A web‐based graphical user interface for CHARMM
Jo, S., Kim, T., Iyer, V. G., & Im, W. (2008) · Journal of Computational Chemistry · doi:10.1002/jcc.20945 · Cited by 9,284
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
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
WHO Declares COVID-19 a Pandemic.
Cucinotta, D., & Vanelli, M. (2020) · Acta bio-medica dell'Ateneo parmense/Acta biomedica · doi:10.23750/abm.v91i1.9397 · Cited by 8,022
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
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q. (2020) · Science · doi:10.1126/science.abb2762 · Cited by 5,036
Self-citationHow 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 4,713
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
Integration, scaling, space-group assignment and post-refinement
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047374 · Cited by 2,554
Bio3d: an R package for the comparative analysis of protein structures
Grant, B. J., Rodrigues, A. P. C., ElSawy, K. M., McCammon, J. A., & Caves, L. S. D. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl461 · Cited by 2,005
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
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853
Automated molecular microscopy: The new Leginon system
Suloway, C. J. M., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J. D., Stagg, S. M., Potter, C. S., & Carragher, B. O. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,695
Solving structures of protein complexes by molecular replacement with Phaser
McCoy, A. (2006) · Acta Crystallographica Section D: Biological Crystallography · doi:10.1107/s0907444906045975 · Cited by 1,672
Human neutralizing antibodies elicited by SARS-CoV-2 infection
Ju, B., Zhang, Q., Ge, J., Wang, R., Sun, J., Ge, X., Yu, J., Shan, S., Zhou, B., Song, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2380-z · Cited by 1,667
Self-citationPositive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs
Bepler, T., Morin, A., Rapp, M., Brasch, J., Shapiro, L. S., Noble, A. J., & Berger, B. (2019) · Nature Methods · doi:10.1038/s41592-019-0575-8 · Cited by 1,620
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
A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., So, R. T. Y., Lv, H., Mok, C. K. P., & Wilson, I. A. (2020) · Science · doi:10.1126/science.abb7269 · Cited by 1,429
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385
Self-citationPotent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349
Self-citationStructure-based design of prefusion-stabilized SARS-CoV-2 spikes
Hsieh, C.-L., Goldsmith, J. A., Schaub, J. M., DiVenere, A. M., Kuo, H.-C., Javanmardi, K., Le, K. C., Wrapp, D., Lee, A. G., Liu, Y., et al. (2020) · Science · doi:10.1126/science.abd0826 · Cited by 1,303
Rogers, T. F., Zhao, F., Huang, D., Beutler, N., Burns, A., He, W.-T., Limbo, O., Smith, C., Song, G., Woehl, J., et al. (2020) · Science · doi:10.1126/science.abc7520 · Cited by 1,230
Brochet, X., Lefranc, M., & Giudicelli, V. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn316 · Cited by 1,220
Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
Hansen, J., Baum, A., Pascal, K. E., Russo, V., Giordano, S., Wloga, E., Fulton, B. O., Yan, Y., Koon, K., Patel, K., et al. (2020) · Science · doi:10.1126/science.abd0827 · Cited by 1,210
Self-citationCao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.025 · Cited by 1,188
IgBLAST: an immunoglobulin variable domain sequence analysis tool
Ye, J., Ma, N., Madden, T., & Ostell, J. M. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt382 · Cited by 1,161
Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
Brouwer, P. J. M., Caniels, T. G., van der Straten, K., Snitselaar, J. L., Aldon, Y., Bangaru, S., Torres, J. L., Okba, N. M. A., Claireaux, M., Kerster, G., et al. (2020) · Science · doi:10.1126/science.abc5902 · Cited by 1,140
A human monoclonal antibody blocking SARS-CoV-2 infection
Wang, C., Li, W., Drabek, D., Okba, N. M. A., van Haperen, R., Osterhaus, A. D. M. E., van Kuppeveld, F. J. M., Haagmans, B. L., Grosveld, F. G., & Bosch, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16256-y · Cited by 1,128
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
MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes
Davis, I., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh398 · Cited by 1,032
Wu, Y., Wang, F., Shen, C., Peng, W., Li, D., Zhao, C., Li, Z., Li, S., Bi, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc2241 · Cited by 963
Self-citationBeyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein
Casalino, L., Gaieb, Z., Goldsmith, J. A., Hjorth, C. K., Dommer, A. C., Harbison, A. M., Fogarty, C. A., de Barros, E. P., Taylor, B. C., McLellan, J. S., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c01056 · Cited by 925
Addressing Preferred Specimen Orientation in Single-Particle Cryo-EM through Tilting
Tan, Y.-Z., Baldwin, P. R., Davis, J., Williamson, J., Potter, C., Carragher, B., & Lyumkis, D. (2017) · Nature Methods · doi:10.1038/nmeth.4347 · Cited by 920
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
Barad, B. A., Echols, N., Wang, R. Y.-R., Cheng, Y., DiMaio, F., Adams, P. D., & Fraser, J. S. (2015) · Nature Methods · doi:10.1038/nmeth.3541 · Cited by 886
The PDB_REDO server for macromolecular structure model optimization
Joosten, R. P., Long, F., Murshudov, G. N., & Anastassis Perrakis, A. (2014) · IUCrJ · doi:10.1107/s2052252514009324 · Cited by 847
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
Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
Benton, D. J., Wrobel, A. G., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature · doi:10.1038/s41586-020-2772-0 · Cited by 781
Structural 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 773
Self-citationStructural 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
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589
FreeSASA: An open source C library for solvent accessible surface area calculations
Mitternacht, S. (2016) · F1000Research · doi:10.12688/f1000research.7931.1 · Cited by 560
Wrobel, A. G., Benton, D. J., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0468-7 · Cited by 544
The structural basis of antibody–antigen recognition
Sela-Culang, I., Kunik, V., & Ofran, Y. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00302 · Cited by 530
Zost, S. J., Gilchuk, P., Chen, R. E., Case, J. B., Reidy, J. X., Trivette, A., Nargi, R. S., Sutton, R. E., Suryadevara, N., Chen, E. C., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0998-x · Cited by 429
Recent developments in the PHENIX software for automated crystallographic structure determination
Adams, P. D., Gopal, K., Grosse‐Kunstleve, R. W., Hung, L., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Pai, R. K., Read, R. J., Romo, T. D., et al. (2003) · Journal of Synchrotron Radiation · doi:10.1107/s0909049503024130 · Cited by 379
Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.001 · Cited by 364
Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody
Lv, Z., Deng, Y., Ye, Q., Cao, L., Sun, C.-Y., Fan, C., Huang, W., Sun, S., Sun, Y., Zhu, L., et al. (2020) · Science · doi:10.1126/science.abc5881 · Cited by 364
Zhou, T., Tsybovsky, Y., Gorman, J., Rapp, M., Cerutti, G., Chuang, G., Katsamba, P. S., Sampson, J. M., Schön, A., Bimela, J. S., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.004 · Cited by 345
Self-citationSupersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120
Kong, L., Lee, J. H., Doores, K. J., Murin, C. D., Julien, J., McBride, R., Liu, Y., Marozsan, A. J., Cupo, A., Klasse, P.-J., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2594 · Cited by 334
Chen, X., Li, R., Pan, Z., Qian, C., Yang, Y., You, R., Zhao, J., Liu, P., Gao, L., Li, Z., et al. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0426-7 · Cited by 327
Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors
Zhou, T., Lynch, R. M., Chen, L., Acharya, P., Wu, X., Doria-Rose, N. A., Joyce, M. G., Lingwood, D., Soto, C. S., Bailer, R. T., et al. (2015) · Cell · doi:10.1016/j.cell.2015.05.007 · Cited by 311
Self-citationKreer, C., Zehner, M., Weber, T., Ercanoglu, M. S., Gieselmann, L., Rohde, C., Halwe, S., Korenkov, M., Schommers, P., Vanshylla, K., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.044 · Cited by 309
Prevalent, protective, and convergent IgG recognition of SARS-CoV-2 non-RBD spike epitopes
Voss, W. N., Hou, Y. J., Johnson, N. V., Delidakis, G., Kim, J. E., Javanmardi, K., Horton, A. P., Bartzoka, F., Paresi, C., Tanno, Y., et al. (2021) · Science · doi:10.1126/science.abg5268 · Cited by 255
The coronavirus pandemic in five powerful charts
Callaway, E., Cyranoski, D., Mallapaty, S., Stoye, E., & Tollefson, J. (2020) · Nature · doi:10.1038/d41586-020-00758-2 · Cited by 237
SAbPred: a structure-based antibody prediction server
Dunbar, J., Krawczyk, K., Leem, J., Marks, C., Nowak, J., Regep, C., Georges, G. J., Kelm, S., Popovic, B., & Deane, C. M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw361 · Cited by 202
Wang, L., Shi, W., Chappell, J. D., Joyce, M. G., Zhang, Y., Kanekiyo, M., Becker, M. M., van Doremalen, N., Fischer, R., Wang, N., et al. (2018) · Journal of Virology · doi:10.1128/jvi.02002-17 · Cited by 169
Self-citationZhou, H., Chen, Y., Zhang, S., Niu, P., Qin, K., Jia, W., Huang, B., Zhang, S., Lan, J., Zhang, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10897-4 · Cited by 148
Rational Vaccine Design in the Time of COVID-19
Burton, D., & Walker, L. (2020) · Cell Host and Microbe · doi:10.1016/j.chom.2020.04.022 · Cited by 112
Structural Characterization of Viral Epitopes Recognized by Broadly Cross-Reactive Antibodies
Lee, P. S., & Wilson, I. A. (2014) · Current topics in microbiology and immunology · doi:10.1007/82_2014_413 · Cited by 95
Chen, Y., Lu, S., Jia, H., Deng, Y., Zhou, J., Huang, B., Yu, Y., Lan, J., Wang, W., Lou, Y., et al. (2017) · Emerging Microbes & Infections · doi:10.1038/emi.2017.50 · Cited by 81
Structure-based development of human antibody cocktails against SARS-CoV-2
Wang, N., Sun, Y., Feng, R., Wang, Y., Guo, Y., Zhang, L., Deng, Y., Wang, L., Cui, Z., Cao, L., et al. (2020) · Cell Research · doi:10.1038/s41422-020-00446-w · Cited by 81
Self-citationSheng, Z., Schramm, C. A., Kong, R., Program, N. C. S., Mullikin, J. C., Mascola, J. R., Kwong, P. D., & Shapiro, L. S. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00537 · Cited by 78
Self-citationShinde, P. V., Xu, H. C., Maney, S. K., Kloetgen, A., Namineni, S., Zhuang, Y., Honke, N., Shaabani, N., Bellora, N., Doerrenberg, M., et al. (2017) · Journal of Virology · doi:10.1128/jvi.01637-17 · Cited by 76
Kreer, C., Zehner, M., Weber, T., Ercanoglu, M. S., Gieselmann, L., Rohde, C., Halwe, S., Korenkov, M., Schommers, P., Vanshylla, K., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.046 · Cited by 67
Schramm, C. A., Sheng, Z., Zhang, Z., Mascola, J. R., Kwong, P. D., & Shapiro, L. S. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00372 · Cited by 65
Self-citationCharacterization of neutralizing antibodies from a SARS-CoV-2 infected individualPreprint
Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.12.091298 · Cited by 64
Transplanting Supersites of HIV-1 Vulnerability
Zhou, T., Zhu, J., Yang, Y., Gorman, J., Ofek, G., Srivatsan, S. R., Druz, A., Lees, C. R., Lu, G., Soto, C. S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099881 · Cited by 59
Self-citationVoss, W. N., Hou, Y., Johnson, N., Kim, J. E., Delidakis, G., Horton, A. P., Bartzoka, F., Paresi, C. J., Tanno, Y., Abbasi, S. A., et al. (2020) · bioRxiv · doi:10.1101/2020.12.20.423708 · Cited by 57
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
IMGT®, the International ImMunoGeneTics Information System® for Immunoinformatics
Lefranc, M. (2008) · Molecular Biotechnology · doi:10.1007/s12033-008-9062-7 · Cited by 52
Longo, N. S., Sutton, M. S., Shiakolas, A. R., Guenaga, J., Jarosinski, M. C., Georgiev, I. S., McKee, K., Bailer, R. T., Louder, M. K., O'Dell, S. J., et al. (2016) · Journal of Virology · doi:10.1128/jvi.01012-16 · Cited by 36
Kumar, S., Ju, B., Shapero, B., Lin, X., Ren, L., Zhang, L., Li, D., Zhou, Z., Feng, Y., Sou, C., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb1328 · Cited by 28
Liu, X., Gao, F., Gou, L., Chen, Y., Gu, Y., Ao, L., Shen, H., Hu, Z., Guo, X., & Gao, W. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.03.074914 · Cited by 21
Targeting the N332-supersite of the HIV-1 envelope for vaccine design
Moyo-Gwete, T., Kitchin, D., & Moore, P. L. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1752183 · Cited by 19
Flagged first, then by citations
4 of the 89 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,022
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Wang, P., Nair, M. S., Liu, L., Iketani, S., Luo, Y., Guo, Y., Wang, M., Yu, J., Zhang, B., Kwong, P. D., et al. (2021) · Nature · doi:10.1038/s41586-021-03398-2 · Cited by 2,312
Self-citationOmicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04385-3 · Cited by 2,006
Self-citationStriking antibody evasion manifested by the Omicron variant of SARS-CoV-2
Liu, L., Iketani, S., Guo, Y., Chan, J. F.-W., Wang, M., Liu, L., Luo, Y., Chu, H., Huang, Y., Nair, M. S., et al. (2022) · Nature · doi:10.1038/s41586-021-04388-0 · Cited by 1,290
Self-citationEvidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
Zhou, D., Dejnirattisai, W., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.037 · Cited by 992
Metadata
- Authors
- Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., Huang, Y., Katsamba, P. S., Liu, L., Nair, M. S., Rawi, R., Olia, A. S., Wang, P., Zhang, B., Chuang, G.-Y., Ho, D. D., Sheng, Z., Kwong, P. D., & Shapiro, L.
- Affiliations
- Mortimer B. Zuckerman Mind Brain Behavior Institute (US)
- National Institutes of Health (US)
- Aaron Diamond AIDS Research Center (US)
- Corresponding author
- Kwong, Peter D.
- Shapiro, Lawrence
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2021-05
- Volume
- 29
- Issue
- 5
- Pages
- 819-833.e7
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC7953435
- OpenAlex
- W3136437538
- Cited by
- 519
- References
- 89
- Citations by year
- 2026: 28 · 2025: 39 · 2024: 67 · 2023: 93 · 2022: 141 · 2021: 151
- FWCI
- 35.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Host & Microbe (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Simons Foundation (SF349247)
- National Institute of General Medical Sciences (GM103310, GM129539)
- National Institutes of Health (P41 GM103403, P30 GM124165)
- Vaccine Research Center
- Office of Science (W-31-109-Eng-38)
- Empire State Development's Division of Science, Technology and Innovation
- Basic Energy Sciences
- U.S. Department of Energy
- National Institute of Allergy and Infectious Diseases
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2, neutralizing antibodies, antibody-antigen complex structure, cryo-EM structure, crystal structure, glycans, beta-hairpin, epitope mapping, convalescent donors, receptor binding domain
- MeSH terms
- Protein Domains, SARS-CoV-2, Antibodies, Viral, Humans, Mutation, Protein Conformation, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
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 ›
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