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Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Open accessAbstract
Understanding the molecular basis for immune recognition of SARS-CoV-2 spike glycoprotein antigenic sites will inform the development of improved therapeutics. We determined the structures of two human monoclonal antibodies-AZD8895 and AZD1061-which form the basis of the investigational antibody cocktail AZD7442, in complex with the receptor-binding domain (RBD) of SARS-CoV-2 to define the genetic and structural basis of neutralization. AZD8895 forms an 'aromatic cage' at the heavy/light chain interface using germ line-encoded residues in complementarity-determining regions (CDRs) 2 and 3 of the heavy chain and CDRs 1 and 3 of the light chain. These structural features explain why highly similar antibodies (public clonotypes) have been isolated from multiple individuals. AZD1061 has an unusually long LCDR1; the HCDR3 makes interactions with the opposite face of the RBD from that of AZD8895. Using deep mutational scanning and neutralization escape selection experiments, we comprehensively mapped the crucial binding residues of both antibodies and identified positions of concern with regards to virus escape from antibody-mediated neutralization. Both AZD8895 and AZD1061 have strong neutralizing activity against SARS-CoV-2 and variants of concern with antigenic substitutions in the RBD. We conclude that germ line-encoded antibody features enable recognition of the SARS-CoV-2 spike RBD and demonstrate the utility of the cocktail AZD7442 in neutralizing emerging variant viruses.
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“Importantly, our spike did not contain R346K, which has been observed at relatively low frequency (<10%) within the Omicron lineage, but which is known to mediate escape from class 3 neutralizing monoclonal antibodies such as AZD1061/cilgavimab (Barnes et al., 2020; Dong et al., 2021; Greaney et al., 2021b).”
From mRNA-based COVID-19 vaccine boosters induce neutralizing immunity against SARS-CoV-2 Omicron variant (2022) · cites this paper as Dong et al., 2021
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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
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
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969
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
Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576
WebLogo: A Sequence Logo Generator: Figure 1Preprint
Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,480
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
MUSCLE: a multiple sequence alignment method with reduced time and space complexity
Edgar, R. C. (2004) · BMC Bioinformatics · doi:10.1186/1471-2105-5-113 · Cited by 9,119
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
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
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
Antibody responses to SARS-CoV-2 in patients with COVID-19
Long, Q.-X., Liu, B.-Z., Deng, H.-J., Wu, G.-C., Deng, K., Chen, Y.-K., Liao, P., Qiu, J.-F., Lin, Y., Cai, X.-F., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0897-1 · Cited by 2,876
Self-citationDetection of a SARS-CoV-2 variant of concern in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510
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
Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956
Self-citationConvergent 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
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
Spike mutation D614G alters SARS-CoV-2 fitness
Plante, J. A., Liu, Y., Liu, J., Xia, H., Johnson, B. A., Lokugamage, K. G., Zhang, X., Muruato, A. E., Zou, J., Fontes-Garfias, C. R., et al. (2021) · Nature · doi:10.1038/s41586-020-2895-3 · Cited by 1,558
Self-citationThe Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Li, Q., Wu, J., Nie, J., Zhang, L., Hao, H., Liu, S., Zhao, C., Zhang, Q., Liu, H., Nie, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.012 · Cited by 1,420
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
Potent 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
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
Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308 · cited 1×
“E484K is present in emerging lineages B.1.351 38 and B.1.1.28 39 , along with substitutions at K417, and has been demonstrated to alter the binding of some monoclonal antibodies 40,43,44 as well as human polyclonal serum antibodies 45 .”
InfluentialStructure-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
A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286
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
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
Self-citationGreaney, 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 · cited 2×
“E484K is present in emerging lineages B.1.351 38 and B.1.1.28 39 , along with substitutions at K417, and has been demonstrated to alter the binding of some monoclonal antibodies 40,43,44 as well as human polyclonal serum antibodies 45 .”
InfluentialSelf-citationSARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147
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
Sui, J., Hwang, W. C., Perez, S., Ge, W., Aird, D. R., Chen, L., Santelli, E., Stec, B., Cadwell, G., Ali, M., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1566 · Cited by 1,128
Potently neutralizing and protective human antibodies against SARS-CoV-2
Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041
Self-citationGreaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016
Self-citationChen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881
Self-citationFocused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing
Wu, X., Zhou, T., Zhu, J., Zhang, B., Georgiev, I. S., Wang, C., Chen, X., Longo, N. S., Louder, M. K., McKee, K., et al. (2011) · Science · doi:10.1126/science.1207532 · Cited by 797
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
Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M. C., Dingens, A. S., Li, J. Z., & Bloom, J. D. (2021) · Science · doi:10.1126/science.abf9302 · Cited by 743
Self-citationLiu, 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
Self-citationLeung, K., Shum, M. H., Leung, G. M., Lam, T. T., & Wu, J. T. (2021) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.26.1.2002106 · Cited by 694
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Network for Genomic Surveillance in South Africa, Cele, S., COMMIT-KZN Team, Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03471-w · Cited by 651
Transmission, infectivity, and neutralization of a spike L452R SARS-CoV-2 variant
Deng, X., Garcia-Knight, M. A., Khalid, M. M., Servellita, V., Wang, C., Morris, M. K., Sotomayor-González, A., Glasner, D. R., Reyes, K. R., Gliwa, A. S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.025 · Cited by 651
An Infectious cDNA Clone of SARS-CoV-2
Xie, X., Muruato, A., Lokugamage, K. G., Narayanan, K., Zhang, X., Zou, J., Liu, J., Schindewolf, C., Bopp, N. E., Aguilar, P. V., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.04.004 · Cited by 647
Self-citationIncreased resistance of SARS-CoV-2 variant P.1 to antibody neutralization
Wang, P., Casner, R. G., Nair, M. S., Wang, M., Yu, J., Cerutti, G., Liu, L., Kwong, P. D., Huang, Y., Shapiro, L., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.007 · Cited by 636
Emergence of SARS-CoV-2 B.1.1.7 Lineage — United States, December 29, 2020–January 12, 2021
Galloway, S. E., Paul, P., MacCannell, D., Johansson, M. A., Brooks, J. T., MacNeil, A., Slayton, R. B., Tong, S., Silk, B. J., Armstrong, G. L., et al. (2021) · MMWR Morbidity and Mortality Weekly Report · doi:10.15585/mmwr.mm7003e2 · Cited by 609
Thomson, E. C., Rosen, L. E., Shepherd, J. G., Spreafico, R., da Silva Filipe, A., Wojcechowskyj, J. A., Davis, C., Piccoli, L., Pascall, D. J., Dillen, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.037 · Cited by 606
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
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
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
Walls, A. C., Tortorici, M. A., Snijder, J., Xiong, X., Bosch, B., Rey, F. A., & Veesler, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708727114 · Cited by 520
REGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters
Baum, A., Ajithdoss, D., Copin, R., Zhou, A., Lanza, K., Negron, N., Ni, M., Wei, Y., Mohammadi, K., Musser, B., et al. (2020) · Science · doi:10.1126/science.abe2402 · Cited by 517
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
Self-citationReverse vaccinology 2.0: Human immunology instructs vaccine antigen design
Rappuoli, R., Bottomley, M. J., D’Oro, U., Finco, O., & Gregorio, E. D. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151960 · Cited by 449
Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies
Greaney, A. J., Starr, T. N., Barnes, C. O., Weisblum, Y., Schmidt, F., Caskey, M., Gaebler, C., Cho, A., Agudelo, M., Finkin, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24435-8 · Cited by 433
Self-citationZost, 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
Self-citationSARS-CoV-2 escape 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. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103154118 · Cited by 429
Case, J. B., Rothlauf, P. W., Chen, R. E., Liu, Z., Zhao, H., Kim, A. S., Bloyet, L.-M., Zeng, Q., Tahan, S., Droit, L., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.021 · Cited by 410
Self-citationGenomic characterization of a novel SARS-CoV-2 lineage from Rio de Janeiro, Brazil
Voloch, C. M., Silva F, R. D., de Almeida, L. G. P., Cardoso, C. C., Brustolini, O. J., Gerber, A. L., Guimarães, A. P. D. C., Mariani, D., Costa, R. M. D., Ferreira, O. C., et al. (2020) · doi:10.1101/2020.12.23.20248598 · Cited by 372 · cited 3×
“Chimeric viruses expressing the spoike genes of B.1.351 or B.1.1.28 were generated in the WA1/2020 backbone and have been described previously 42 .”
InfluentialGenomic characterization of a novel SARS-CoV-2 lineage from Rio de Janeiro, Brazil
Voloch, C. M., da Silva Francisco, R., de Almeida, L. G. P., Cardoso, C. C., Brustolini, O. J., Gerber, A. L., Guimarães, A. P. D. C., Mariani, D., da Costa, R. M., Ferreira, O. C., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00119-21 · Cited by 372
The antigenic anatomy of SARS-CoV-2 receptor binding domain
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
Self-citationHuman broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus
Giang, E., Dorner, M., Prentoe, J. C., Dreux, M., Evans, M. J., Bukh, J., Rice, C. M., Ploß, A., Burton, D. R., & Law, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114927109 · Cited by 346
BNT162b2-elicited neutralization of B.1.617 and other SARS-CoV-2 variants
Liu, J., Liu, Y., Xia, H., Zou, J., Weaver, S. C., Swanson, K. A., Cai, H., Cutler, M., Cooper, D., Muik, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03693-y · Cited by 342
Self-citationVaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses
Joyce, M. G., Wheatley, A. K., Thomas, P. V., Chuang, G.-Y., Soto, C., Bailer, R. T., Druz, A., Georgiev, I. S., Gillespie, R. A., Kanekiyo, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.043 · Cited by 333
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
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.2020.06.044 · Cited by 309
High frequency of shared clonotypes in human B cell receptor repertoires
Soto, C., Bombardi, R. G., Branchizio, A., Kose, N., Matta, P., Sevy, A. M., Sinkovits, R. S., Gilchuk, P., Finn, J. A., & Crowe, J. E. (2019) · Nature · doi:10.1038/s41586-019-0934-8 · Cited by 294
Self-citationRapid development of broadly influenza neutralizing antibodies through redundant mutations
Pappas, L., Foglierini, M., Piccoli, L., Kallewaard, N. L., Turrini, F., Silacci, C., Fernandez-Rodriguez, B. M., Agatic, G., Giacchetto-Sasselli, I., Pellicciotta, G., et al. (2014) · Nature · doi:10.1038/nature13764 · Cited by 290
Huang, C.-C., Venturi, M., Majeed, S., Moore, M. J., Phogat, S. K., Zhang, M.-Y., Dimitrov, D. S., Hendrickson, W. A., Robinson, J. E., Sodroski, J., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308527100 · Cited by 275
Inferring the shape of global epistasis
Otwinowski, J., McCandlish, D. M., & Plotkin, J. B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804015115 · Cited by 243
Human B Cell Clonal Expansion and Convergent Antibody Responses to SARS-CoV-2
Nielsen, S. C. A., Yang, F., Jackson, K., Hoh, R. A., Röltgen, K., Jean, G. H., Stevens, B., Lee, J.-Y., Rustagi, A., Rogers, A. J., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.09.002 · Cited by 229
GlyProt: in silico glycosylation of proteins
Bohne-Lang, A., & der Lieth, C. W. V. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki385 · Cited by 207
Diversion of HIV-1 vaccine–induced immunity by gp41-microbiota cross-reactive antibodies
Williams, W. B., Liao, H., Moody, M. A., Kepler, T. B., Alam, S. M., Gao, F., Wiehe, K. J., Trama, A. M., Jones, K. L., Zhang, R., et al. (2015) · Science · doi:10.1126/science.aab1253 · Cited by 197
Broadly neutralizing antibodies with few somatic mutations and hepatitis C virus clearance
Bailey, J. R., Flyak, A. I., Cohen, V. J., Li, H., Wasilewski, L. N., Snider, A. E., Wang, S., Learn, G. H., Kose, N., Loerinc, L. B., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.92872 · Cited by 138
Self-citationKlimstra, W. B., Tilston-Lunel, N. L., Nambulli, S., Boslett, J., McMillen, C. M., Gilliland, T., Dunn, M. D., Sun, C., Wheeler, S. E., Wells, A., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001481 · Cited by 137
Wheatley, A. K., Whittle, J. R. R., Lingwood, D., Kanekiyo, M., Yassine, H. M., Steven, S., Narpala, S., Prabhakaran, M. S., Matus‐Nicodemos, R., Bailer, R. T., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402835 · Cited by 98
Algaissi, A. A., Alfaleh, M. A., Hala, S. M., Abujamel, T. S., Alamri, S. S., Almahboub, S. A., Alluhaybi, K. A., Hobani, H. I., Alsulaiman, R. M., Alharbi, R. H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-73491-5 · Cited by 93
Wahba, L., Jain, N., Fire, A. Z., Shoura, M. J., Artiles, K. L., McCoy, M. J., & Jeong, D. (2020) · mSphere · doi:10.1128/msphere.00160-20 · Cited by 86
The Measurement of Human Spermatozoan Motility
Janick, J., & Macleod, J. (1970) · Fertility and Sterility · doi:10.1016/s0015-0282(16)37327-7 · Cited by 78
Weitkamp, J.-H., Kallewaard, N. L., Kusuhara, K., Bures, E., Williams, J. V., LaFleur, B., Greenberg, H. B., & Crowe, J. E. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.9.4680 · Cited by 68
Self-citationTransmission of SARS-CoV-2 from humans to animals and potential host adaptationPreprint
Tan, C. C. S., Lam, S. D., Richard, D., Owen, C. J., Berchtold, D., Orengo, C. A., Nair, M. S., Kuchipudi, S. V., Kapur, V., van Dorp, L., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.16.384743 · Cited by 62
Tian, C., Luskin, G. K., Dischert, K. M., Higginbotham, J. N., Shepherd, B. E., & Crowe, J. E. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.5.3279 · Cited by 48
Self-citationHost barriers to SARS-CoV-2 demonstrated by ferrets in a high-exposure domestic setting
Sawatzki, K., Hill, N. J., Puryear, W. B., Foss, A. D., Stone, J. J., & Runstadler, J. A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025601118 · Cited by 43
Fitzgerald, M., & Berman, D. S. (1994) · Nature · doi:10.1038/368092b0 · Cited by 11
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 · cited 1×
“A total of 386, 193, 47, or 7 heavy chain sequences for this SARS-CoV-2 reactive public clonotype was found in each donor or cord blood repertoire, respectively (Extended Data Fig.”
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Cameroni, E., Bowen, J. E., Rosen, L. E., Saliba, C., Zepeda, S. K., Culap, K., Pinto, D., VanBlargan, L. A., Marco, A. D., di Iulio, J., et al. (2021) · Nature · doi:10.1038/s41586-021-04386-2 · Cited by 1,070
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Metadata
- Authors
- Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., Rodriguez, J., Armstrong, E., Gainza, C., Nargi, R. S., Binshtein, E., Xie, X., Zhang, X., Shi, P.-Y., Logue, J., Weston, S., McGrath, M. E., Frieman, M. B., Brady, T., Tuffy, K. M., Bright, H., Loo, Y.-M., McTamney, P. M., Esser, M. T., Carnahan, R. H., Diamond, M. S., Bloom, J. D., & Crowe, J. E.
- Affiliations
- Vanderbilt University Medical Center (US)
- University of Washington (US)
- Fred Hutch Cancer Center (US)
- Washington University in St. Louis (US)
- The University of Texas Medical Branch at Galveston (US)
- University of Maryland, College Park (US)
- AstraZeneca (United States) (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Crowe, James E.
- ORCID
- Dong, Jinhui
- Zost, Seth J.
- Greaney, Allison J.
- Starr, Tyler N.
- Dingens, Adam S.
- Chen, Elaine C.
- Chen, Rita E.
- Case, James Brett
- Gilchuk, Pavlo
- Rodriguez, Jessica
- Binshtein, Elad
- Xie, Xuping
- Zhang, Xianwen
- Shi, Pei-Yong
- Logue, James
- Weston, Stuart
- McGrath, Marisa E.
- Frieman, Matthew B.
- Brady, Tyler
- Tuffy, Kevin M.
- Bright, Helen
- Loo, Yueh-Ming
- Esser, Mark T.
- Carnahan, Robert H.
- Diamond, Michael S.
- Bloom, Jesse D.
- Crowe, James E.
- Venue
- Nature Microbiology
- Published
- 2021-09-21
- Volume
- 6
- Issue
- 10
- Pages
- 1233-1244
- ISSN
- 2058-5276 (ISSN-L)
- PMC
- PMC8543371
- OpenAlex
- W3199394546
- Cited by
- 285
- References
- 84
- Citations by year
- 2026: 12 · 2025: 17 · 2024: 43 · 2023: 72 · 2022: 107 · 2021: 33
- FWCI
- 20.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (AI095202, 75N93019C00062, AI157155, AI141707, 75N93019C00074, AI150739)
- U.S. Department of Health & Human Services | NIH | National Center for Advancing Translational Sciences (UL1TR001439)
- United States Department of Defense | Defense Advanced Research Projects Agency (HR0011-18-3-0001, HR0011-18-2-0001)
- Merck KGaA (Future Insight Prize 2019)
- DOE | LDRD | Argonne National Laboratory (DE-AC02-06CH11357)
- Michigan Economic Development Corporation (085P1000817)
- 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, spike protein, receptor binding domain, monoclonal antibodies, antibody neutralization, antibody-antigen complex structure, hypervariable region, HCDR3, neutralization escape, variants of concern, deep mutational scanning
- MeSH terms
- Protein Domains, COVID-19, SARS-CoV-2, Antibodies, Monoclonal, Antibodies, Viral, Antigenic Variation, Binding Sites, Humans, Mutation, Complementarity Determining Regions, 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.
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