Genetic and structural basis for recognition of SARS-CoV-2 spike protein by a two-antibody cocktail
Open accessAbstract
The SARS-CoV-2 pandemic has led to an urgent need to understand the molecular basis for immune recognition of SARS-CoV-2 spike (S) glycoprotein antigenic sites. To define the genetic and structural basis for SARS-CoV-2 neutralization, we determined the structures of two human monoclonal antibodies COV2-2196 and COV2-2130 1 , which form the basis of the investigational antibody cocktail AZD7442, in complex with the receptor binding domain (RBD) of SARS-CoV-2. COV2-2196 forms an “aromatic cage” at the heavy/light chain interface using germline-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 1–4 . The structure of COV2-2130 reveals that an unusually long LCDR1 and HCDR3 make interactions with the opposite face of the RBD from that of COV2-2196. Using deep mutational scanning and neutralization escape selection experiments, we comprehensively mapped the critical residues of both antibodies and identified positions of concern for possible viral escape. Nonetheless, both COV2-2196 and COV2-2130 showed strong neutralizing activity against SARS-CoV-2 strain with recent variations of concern including E484K, N501Y, and D614G substitutions. These studies reveal germline-encoded antibody features enabling recognition of the RBD and demonstrate the activity of a cocktail like AZD7442 in preventing escape from emerging variant viruses.
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
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Earlier work using Vero E6-produced viruses carrying some or all South African spike changes found only 1.2- to 2.7-fold drops in neutralization by human sera after BNT162b2 vaccination.
“As an example, recent studies with Vero E6 cell-derived SARS-CoV-2 with spike proteins containing some (E484K, N501Y, and D614G) or all of the South African mutations showed smaller 1.2 to 2.7-fold decreases in neutralization potency by BNT162b2 mRNA vaccine-elicited human immune sera22,46.”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [46]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
<i>Coot</i> : 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 · see citing works
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 · see citing works
<i>PHENIX</i> : 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 · see citing works
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 · see citing works
<i>Phaser</i> 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 · see citing works
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 · see citing works
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works
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 · see citing works
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 12,433 · see citing works
Overview of the <i>CCP</i> 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 · see citing works
MUSCLE: a multiple sequence alignment method with reduced time and space complexity
Edgar, R. (2004) · BMC Bioinformatics · doi:10.1186/1471-2105-5-113 · Cited by 8,948 · see citing works
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 · see citing works
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · see citing works
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 · see citing works
Self-citationTegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2020) · doi:10.1101/2020.12.21.20248640 · Cited by 2,535 · see citing works
Detection 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 · see citing works
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) · doi:10.1101/2021.01.25.428137 · Cited by 2,328
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationGreaney, 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 · see citing works
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 · see citing works
Self-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 · see citing works
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 · see citing works
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 1,132 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Chen, 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 · see citing works
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 785 · see citing works
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 763 · see citing works
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 · see citing works
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 · see citing works
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Cele, S., Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., Wilkinson, E., Naidoo, Y., et al. (2021) · doi:10.1101/2021.01.26.21250224 · Cited by 651 · see citing works
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 · see citing works
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 · see citing works
Self-citationProspective mapping of viral mutations that escape antibodies used to treat COVID-19Preprint
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M., Dingens, A. S., Li, J. Z., & Bloom, J. (2020) · bioRxiv · doi:10.1101/2020.11.30.405472 · Cited by 633 · see citing works
Self-citationEmergence 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 · see citing works
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 · see citing works
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 · see citing works
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 539 · see citing works
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 · see citing works
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 · see citing works
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 438 · see citing works
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 423 · see citing works
Self-citationCase, 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 · see citing works
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 · see citing works
Genomic 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 · see citing works
Human 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 · see citing works
Vaccine-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 · see citing works
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 313 · see citing works
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 · see citing works
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 · see citing works
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 287 · see citing works
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 · see citing works
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 · see citing works
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 236 · see citing works
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 · see citing works
SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2103154118 · Cited by 187 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationWheatley, 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 · see citing works
Algaissi, A., Alfaleh, M. A., Hala, S., Abujamel, T. S., Alamri, S. S., Almahboub, S., Alluhaybi, K., Hobani, H. I., Alsulaiman, R. M., Alharbi, R. H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-73491-5 · Cited by 87 · see citing works
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 · see citing works
Self-citationWahba, 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 60 · see citing works
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 · see citing works
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 · see citing works
Ferrets not infected by SARS-CoV-2 in a high-exposure domestic settingPreprint
Sawatzki, K., Hill, N. J., Puryear, W. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.21.254995 · Cited by 13 · see citing works
SARS-CoV-2 escape <i>in vitro</i> 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
SARS-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) · doi:10.1101/2021.01.18.427166
Flagged first, then by citations
Research works printed but not linked: 6
- which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
- which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
- which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
- which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
- which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
- which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
Cited by
Sorted by citations
Chen, 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 · see citing works
Self-citationThe biological and clinical significance of emerging SARS-CoV-2 variants
Tao, K., Tzou, P. L., Nouhin, J., Gupta, R. K., de Oliveira, T., Kosakovsky Pond, S. L., Fera, D., & Shafer, R. W. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-021-00408-x · Cited by 1,009 · see citing works
Starr, T. N., Greaney, A. J., Dingens, A. S., & Bloom, J. D. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100255 · Cited by 470 · see citing works
Self-citationSARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 495 · see citing works
Self-citationThe 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 · see citing works
Self-citationMapping 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 · see citing works
Self-citationTackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.05.005 · Cited by 375 · see citing works
Greaney, A. J., Loes, A. N., Gentles, L. E., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9915 · Cited by 244 · see citing works
Self-citationCopin, R., Baum, A., Wloga, E., Pascal, K. E., Giordano, S., Fulton, B. O., Zhou, A., Negron, N., Lanza, K., Chan, N., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.002 · Cited by 212 · see citing works
Loo, Y., McTamney, P. M., Arends, R. H., Gasser, R. A., Abram, M. E., Cheng, L., Diallo, S., Flores, D. J., Bond, N. J., Ren, K., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abl8124 · Cited by 217 · see citing works
Self-citationUltrapotent antibodies against diverse and highly transmissible SARS-CoV-2 variants
Wang, L., Zhou, T., Zhang, Y., Yang, E. S., Schramm, C. A., Shi, W., Pegu, A., Oloniniyi, O. K., Henry, A. R., Darko, S. W., et al. (2021) · Science · doi:10.1126/science.abh1766 · Cited by 191 · see citing works
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 · see citing works
Self-citationStructural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529
Zhou, T., Wang, L., Misasi, J., Pegu, A., Zhang, Y., Harris, D. R., Olia, A. S., Talana, C. A., Yang, E. S., Chen, M., et al. (2022) · Science · doi:10.1126/science.abn8897 · Cited by 160 · see citing works
SARS-CoV-2-neutralising monoclonal antibodies for treatment of COVID-19
Kreuzberger, N., Hirsch, C., Chai, K. L., Tomlinson, E., Khosravi, Z., Popp, M., Neidhardt, M., Piechotta, V., Salomon, S., Valk, S. J., et al. (2021) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd013825.pub2 · Cited by 149 · see citing works
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
Pymm, P., Adair, A., Chan, L., Cooney, J. P., Mordant, F., Allison, C., Lopez, E., Haycroft, E., O, Neill, M., et al. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2101918118 · Cited by 134 · see citing works
Chen, E. C., Gilchuk, P., Zost, S. J., Suryadevara, N., Winkler, E. S., Cabel, C. R., Binshtein, E., Chen, R. E., Sutton, R. E., Rodriguez, J. L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109604 · Cited by 76 · see citing works
Self-citationCurrent status of therapeutic monoclonal antibodies against SARS-CoV-2
Kumar, S., Chandele, A., & Sharma, A. K. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009885 · Cited by 103 · see citing works
VanBlargan, L. A., Adams, L., Liu, Z.-M., Chen, R. E., Gilchuk, P., Raju, S., Smith, B. K., Zhao, H.-Y., Case, J., Winkler, E. S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.016 · Cited by 95 · see citing works
Self-citationTackling 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 · see citing works
“However, some clinical mAbs are not sensitive in vitro and in vivo to themutations present in the current VOCs/VOIs due to targeting of highly conserved epitopes, as is the case for VIR-7831, COV22196, and other mAbs (Chen et al., 2021b; Dong et al., 2021; McCallum et al., 2021a; Pinto et al., 2020; Starr et al., 2021…”
InfluentialACTIV-3/TICO Bamlanivimab Study Group*, Lundgren, J. D., Grund, B., Barkauskas, C. E., Holland, T. L., Gottlieb, R., Sandkovsky, U., Brown, S. M., Knowlton, K. U., Self, W. H., et al. (2021) · Annals of Internal Medicine · doi:10.7326/m21-3507 · Cited by 78 · see citing works
A public vaccine-induced human antibody protects against SARS-CoV-2 and emerging variants
Schmitz, A. J., Turner, J. S., Liu, Z., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T. L., Darling, T. L., Adelsberg, D. C., Alsoussi, W. B., et al. (2021) · doi:10.1101/2021.03.24.436864 · Cited by 72 · see citing works
Self-citationA vaccine-induced public antibody protects against SARS-CoV-2 and emerging variants
Schmitz, A. J., Turner, J. S., Liu, Z., Zhou, J. Q., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T. L., Darling, T. L., Adelsberg, D. C., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.013 · Cited by 63 · see citing works
Self-citationOmicron-B.1.1.529 leads to widespread escape from neutralizing antibody responsesPreprint
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. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.03.471045 · Cited by 69 · see citing works
Landscape of human antibody recognition of the SARS-CoV-2 receptor binding domain
Wheatley, A., Pymm, P., Esterbauer, R., Dietrich, M., Lee, W., Drew, D., Kelly, H. G., Chan, L., Mordant, F., Black, K. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109822 · Cited by 48 · see citing works
A broadly neutralizing humanized ACE2-targeting antibody against SARS-CoV-2 variants
Du, Y., Shi, R., Zhang, Y., Duan, X., Li, L., Zhang, J., Wang, F., Zhang, R., Shen, H., Wang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25331-x · Cited by 61 · see citing works
The ins and outs of SARS-CoV-2 variants of concern (VOCs)
Salehi-Vaziri, ., Fazlalipour, M., Khorrami, S. M. S., Azadmanesh, K., Pouriayevali, M. H., Jalali, T., Shoja, Z., & Maleki, A. (2022) · Archives of Virology · doi:10.1007/s00705-022-05365-2 · Cited by 58 · see citing works
Rapid escape of new SARS-CoV-2 Omicron variants from BA.2-directed antibody responses
Dijokaite-Guraliuc, A., Das, R., Zhou, D., Ginn, H. M., Liu, C., Duyvesteyn, H. M. E., Huo, J., Nutalai, R., Supasa, P., Selvaraj, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112271 · Cited by 45 · see citing works
The 15-Months Clinical Experience of SARS-CoV-2: A Literature Review of Therapies and Adjuvants
Inchingolo, A. D., Dipalma, G., Inchingolo, A. M., Malcangi, G., Santacroce, L., D’Oria, M. T., Isacco, C. G., Bordea, I. R., Candrea, S., Scarano, A., et al. (2021) · Antioxidants · doi:10.3390/antiox10060881 · Cited by 40 · see citing works
Strohl, W. R., Ku, Z., An, Z., Carroll, S. F., Keyt, B. A., & Strohl, L. M. (2022) · BioDrugs · doi:10.1007/s40259-022-00529-7 · Cited by 34 · see citing works
Baral, P. K., Yin, J., & James, M. N. G. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.07.013 · Cited by 36 · see citing works
Monoclonal antibodies for the treatment of COVID-19 patients: An umbrella to overcome the storm?
Pinna, S. M., Lupia, T., Scabini, S., Vita, D., Benedetto, I. D., Gaviraghi, A., Colasanto, I., Varese, A., Cattel, F., Rosa, F. G. D., et al. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108200 · Cited by 32 · see citing works
Wu, J., Chen, Z., Gao, Y., Wang, Z., Wang, J., Chiang, B., Zhou, Y., Han, Y., Zhan, W., Xie, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112503 · Cited by 28 · see citing works
Self-citationGreaney, A. J., Eguia, R. T., Starr, T. N., Khan, K., Franko, N., Logue, J. K., Lord, S. M., Speake, C., Chu, H. Y., Sigal, A., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010592 · Cited by 27 · see citing works
Self-citationKramer, K. J., Johnson, N., Shiakolas, A. R., Suryadevara, N., Periasamy, S., Raju, N., Williams, J. K., Wrapp, D., Zost, S. J., Walker, L. M., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109784 · Cited by 26 · see citing works
Self-citationStarr, T. N., Czudnochowski, N., Zatta, F., Park, Y., Liu, Z., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.06.438709 · Cited by 24 · see citing works
Self-citationAntibody cocktail effective against variants of SARS-CoV-2
Liang, K.-H., Chiang, P.-Y., Ko, S.-H., Chou, Y., Lu, R., Lin, H.-T., Wy, C., Lin, Y., Tao, M., Jan, J., et al. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00777-9 · Cited by 19 · see citing works
Anti-human ACE2 antibody neutralizes and inhibits virus production of SARS-CoV-2 variants of concern
Chaouat, A. E., Brizić, I., Brlić, P. K., Atari, N., Kliker, L., Alfi, O., Mandelboim, M., Wolf, D. G., Tafish, L., Kol, I., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104935 · Cited by 17 · see citing works
Antibody sequence determinants of viral antigen specificity
Abu-Shmais, A. A., Vukovich, M. J., Wasdin, P. T., Suresh, Y. P., Marinov, T. M., Rush, S. A., Gillespie, R. A., Sankhala, R. S., Choe, M., Joyce, M. G., et al. (2024) · mBio · doi:10.1128/mbio.01560-24 · Cited by 19 · see citing works
Kovačech, B., Fialova, L., Filipcik, P., Škrabana, R., Zilkova, M., Paulenka-Ivanovova, N., Kováč, A., Palova, D., Rolkova, G., Tomková, K., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.103818 · Cited by 16 · see citing works
van der Straten, K., van Gils, M. V., de Taeye, S. D., & de Bree, G. D. (2022) · Frontiers in Medical Technology · doi:10.3389/fmedt.2022.867982 · Cited by 14 · see citing works
Analysis of the molecular mechanism of SARS-CoV-2 antibodies
Jin, D., Wei, J., & Sun, J. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.06.001 · Cited by 16 · see citing works
Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
Hendy, M. A., Kaufman, S., & Ponga, M. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-01081-0 · Cited by 16 · see citing works
Engelhart, E., Lopez, R. M., Emerson, R., Lin, C., Shikany, C., Guion, D., Kelley, M., & Younger, D. A. (2022) · Antibody Therapeutics · doi:10.1093/abt/tbac011 · Cited by 15 · see citing works
Monoclonal Antibodies as Potential COVID-19 Therapeutic Agents
Plichta, J., Kuna, P., & Panek, M. (2022) · COVID · doi:10.3390/covid2050045 · Cited by 13 · see citing works
REGEN-COV protects against viral escape in preclinical and human studiesPreprint
Copin, R., Baum, A., Wloga, E. H., Pascal, K. E., Giordano, S., Fulton, B. O., Zhou, A., Negron, N., Lanza, K., Chan, N., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.10.434834 · Cited by 10 · see citing works
SARS-CoV-2 Spike receptor-binding domain with a G485R mutation in complex with human ACE2Preprint
Weekley, C. M., Purcell, D. F. J., & Parker, M. W. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.16.434488 · Cited by 6 · see citing works
An elite broadly neutralizing antibody protects SARS-CoV-2 Omicron variant challengePreprint
Zhou, B., Zhou, R., Chan, J. F., Luo, M., Peng, Q., Yuan, S., Mok, B. W.-Y., Chen, B., Wang, P., Poon, V. K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.05.475037 · Cited by 5 · see citing works
Yoon, E.-H., Kim, D., Jeon, H., Kwon, Y., Jang, Y., Kim, S., & Hwang, K. Y. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.06.043 · Cited by 4 · see citing works
Cheng, M. H., Krieger, J., Xiang, Y., Kaynak, B., Shi, Y., Arditi, M., & Bahar, İ. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3907841 · Cited by 4 · see citing works
Activity of Tixagevimab/Cilgavimab against the Omicron variant of SARS-CoV-2 in a hamster modelPreprint
Driouich, J., Lingas, G., Lucıanı, L., Cochin, M., Villarroel, P. M. S., Moureau, G., Petit, P.-R., Touret, F., Guedj, J., de Lamballerie, X. N., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1399448/v1 · Cited by 4 · see citing works
Treatment of COVID-19 by monoclonal antibodies and the traditional Chinese medicine
Ling, Y., Dong, Y., Li, Q., Huang, D., Li, Z., & Chen, M. (2022) · Medicine in Novel Technology and Devices · doi:10.1016/j.medntd.2022.100159 · Cited by 3 · see citing works
Molecular targets in SARS-CoV-2 infection: An update on repurposed drug candidates
Rahmani, D., Jafari, A., Kesharwani, P., & Sahebkar, A. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155589 · Cited by 2 · see citing works
The Efficacy of Recombinant Drugs in COVID-19 Treatment
Norizadeh, M. (2023) · Advances in Pharmacology & Clinical Trials · doi:10.23880/apct-16000220 · Cited by 1 · see citing works
Visualizing Amino Acid Substitutions in a Physicochemical Vector SpacePreprint
Nemzer, L. R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.15.452549
Yan, Q., Gao, X., Liu, B., Hou, R., He, P., Ma, Y., Zhang, Y., Zhang, Y., Li, Z., Chen, Q., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.12.561995
Los anticuerpos monoclonales de AstraZeneca, un nuevo fármaco experimental contra la covid-19
Lopez-Munoz, F. J., & Guirao, J. (2021) · doi:10.64628/aao.4h7ms94sv
Astuti, P., Mahyarudin, M., Liana, D. F., Novianry, V., Shofiyah, S. S., Amalia, P., Faisal, M., & Reynaldi, M. A. (2025) · Infection Epidemiology and Microbiology · doi:10.61882/iem.11.3.285
- 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., Bright, H., Loo, Y.-M., McTamney, P., Esser, M., 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
- Bright, Helen
- Loo, Yueh-Ming
- Esser, Mark
- Carnahan, Robert H.
- Diamond, Michael S.
- Bloom, Jesse D.
- Crowe, James E.
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2021-01-28
- PMC
- PMC7852235
- OpenAlex
- W3121265983
- Cited by
- 55
- References
- 74
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 4 · 2022: 14 · 2021: 34
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Energy (DE‐ AC02‐06CH11357, COVID-19, AC02‐06CH11357, 085P1000817, 06CH11357, DE-AC02-)
- Damon Runyon Cancer Research Foundation (DRG-2381-19)
- Amon G. Carter Foundation
- Washington Research Foundation (DE-AC02-06CH11357)
- Eli Lilly and Company
- AstraZeneca
- GlaxoSmithKline
- Michigan Economic Development Corporation (085P1000817, DE-AC02-06CH11357)
- George Mason University
- Vanderbilt University
- John S. Dunn Foundation
- University of Washington (DE-AC02-06CH11357)
- Merck KGaA
- Robert J. Kleberg, Jr. and Helen C. Kleberg Foundation
- Vanderbilt University Medical Center
- Fast Grants
- Moderna
- National Institutes of Health (1s10od028685-01, -0001, COVID-19, 75N93019C00062, DE-AC02–06CH11357, 085P1000817, UL1TR001439)
- Defense Advanced Research Projects Agency (HR0011‐18‐2‐0001, HR00 11-18-3-0001, 75N93019C00062)
- Office of Science (AC02‐06CH11357, DE-AC02, 085P1000817, 06CH11357, DE-AC02-06CH11357)
- Advanced Research Projects Agency
- Michigan Technology Tri-Corridor (DE-AC02-06CH11357, 085P1000817)
- Mercatus Center, George Mason University
- National Institute of Allergy and Infectious Diseases (T32AI083203)
- Office of Research Infrastructure Programs, National Institutes of Health (S10OD028685)
- Argonne National Laboratory (DE- AC02-06-CH11357, DE-AC02, AC02–06CH11357, 085P1000817, 06CH11357)
- 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
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2, spike protein, receptor binding domain, monoclonal antibodies, antibody-antigen complex structure, hypervariable region, neutralization escape, deep mutational scanning, E484K, N501Y, D614G, variants of concern
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
