Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells
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The COVID-19 pandemic urgently needs therapeutic and prophylactic interventions. Here, we report the rapid identification of SARS-CoV-2-neutralizing antibodies by high-throughput single-cell RNA and VDJ sequencing of antigen-enriched B cells from 60 convalescent patients. From 8,558 antigen-binding IgG1+ clonotypes, 14 potent neutralizing antibodies were identified, with the most potent one, BD-368-2, exhibiting an IC 50 of 1.2 and 15 ng/mL against pseudotyped and authentic SARS-CoV-2, respectively. BD-368-2 also displayed strong therapeutic and prophylactic efficacy in SARS-CoV-2-infected hACE2-transgenic mice. Additionally, the 3.8 Å cryo-EM structure of a neutralizing antibody in complex with the spike-ectodomain trimer revealed the antibody's epitope overlaps with the ACE2 binding site. Moreover, we demonstrated that SARS-CoV-2-neutralizing antibodies could be directly selected based on similarities of their predicted CDR3 H structures to those of SARS-CoV-neutralizing antibodies. Altogether, we showed that human neutralizing antibodies could be efficiently discovered by high-throughput single B cell sequencing in response to pandemic infectious diseases.
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Most of the strongest neutralizing antibodies against SARS-CoV-2 identified so far bind the RBD.
“We focused on the RBD since it is the target of the majority of the more potent SARS-CoV-2 neutralizing antibodies discovered to date21–26.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [23]
mRNA vaccines induce antibodies to RBD, the main target of neutralizing antibodies, in a way that resembles natural infection.
“The vaccines elicit antibody responses against the RBD, the major target of neutralizing antibodies21–26, in a manner that resembles natural infection.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [23]
Plasma RBD antibodies are strongly correlated with neutralizing activity.
“We limited our analysis to RBD because plasma RBD antibodies are strongly correlated with neutralizing activity3,10–12.”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [11]
Numerous neutralizing anti-RBD monoclonal antibodies have been characterized, the most potent of which block the RBD-ACE2 interaction.
“Numerous neutralizing anti-RBD monoclonal antibodies (mAbs) have been characterized, the most potent of which block the RBD-ACE2 interaction (16, 17, 22–24, 32–37).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [36]
Analyses of B cell responses to spike generally focus on the RBD and on cells sorted with RBD baits, introducing a bias by omitting non-RBD targets.
“Analyses of the B cell responses to the spike generally focus on the RBD and on cells sorted with RBD baits introducing an inherent bias by omitting non-RBD targets”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Cao et al., 2020
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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 45,260 · see citing works
Cutadapt removes adapter sequences from high-throughput sequencing reads
Martin, M. (2011) · EMBnet.journal · doi:10.14806/ej.17.1.200 · Cited by 33,889 · see citing works
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · 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
Self-citationHoffmann, 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
A new coronavirus associated with human respiratory disease in China
Wu, F., Zhao, S., Yu, B., Chen, Y.-M., Wang, W., Song, Z.-G., Hu, Y., Tao, Z.-W., Tian, J.-H., Pei, Y.-Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2008-3 · Cited by 11,688 · see citing works
The Phyre2 web portal for protein modeling, prediction and analysis
Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., & Sternberg, M. J. E. (2015) · Nature Protocols · doi:10.1038/nprot.2015.053 · Cited by 9,652 · 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
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 · see citing works
MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works
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 · see citing works
Spatial reconstruction of single-cell gene expression data
Satija, R., Farrell, J. A., Gennert, D., Schier, A. F., & Regev, A. (2015) · Nature Biotechnology · doi:10.1038/nbt.3192 · Cited by 7,055 · cited 1× · see citing works
“Clusters of cells were visualized using T-distributed stochastic neighbor embedding (t-SNE) in Seurat (Satija et al., 2015).”
Liebschner, D. C., Afonine, P. V., Baker, M. L., Bunkòczi, G., Chen, V. B., Croll, T. I., Hintze, B. J., Hung, L., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 6,709 · see citing works
Automated electron microscope tomography using robust prediction of specimen movements.
Mastronarde, D. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,446 · see citing works
Aran, D., Looney, A. P., Liu, L., Wu, E., Fong, V., Hsu, A., Chak, S., Naikawadi, R. P., Wolters, P. J., Abate, A. R., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0276-y · Cited by 4,984 · see citing works
New tools for automated high-resolution cryo-EM structure determination in RELION-3
Zivanov, J., Nakane, T., Forsberg, B., Kimanius, D., Hagen, W., Lindahl, E., & Scheres, S. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,377 · see citing works
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · see citing works
Chan, J. F., Kok, K., Zhu, Z., Chu, H., To, K. K., Yuan, S., & Yuen, K. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1719902 · Cited by 3,063 · see citing works
IgG Subclasses and Allotypes: From Structure to Effector Functions
Vidarsson, G., Dekkers, G., & Rispens, T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00520 · Cited by 2,667 · see citing works
Treatment of 5 Critically Ill Patients With COVID-19 With Convalescent Plasma
Shen, C., Wang, Z., Zhao, F., Yang, Y., Li, J., Yuan, J., Wang, F., Li, D., Yang, M., Xing, L., et al. (2020) · JAMA · doi:10.1001/jama.2020.4783 · Cited by 2,278 · see citing works
Predominant Autoantibody Production by Early Human B Cell Precursors
Wardemann, H., Yurasov, S., Schaefer, A., Young, J. W., Meffre, E., & Nussenzweig, M. C. (2003) · Science · doi:10.1126/science.1086907 · Cited by 2,088 · see citing works
Broad and Potent Neutralizing Antibodies from an African Donor Reveal a New HIV-1 Vaccine Target
Walker, L., Phogat, S., Chan-hui, P., Wagner, D., Pham, P., Goss, J. L., Wrin, T., Simek, M., Fling, S., Mitcham, J., et al. (2009) · Science · doi:10.1126/science.1178746 · Cited by 1,849 · see citing works
Quantifying the local resolution of cryo-EM density maps
Kucukelbir, A., Sigworth, F. J., & Tagare, H. D. (2013) · Nature Methods · doi:10.1038/nmeth.2727 · Cited by 1,763 · see citing works
COVID-19: immunopathology and its implications for therapy
Cao, X. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-0308-3 · Cited by 1,609 · see citing works
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 1,405 · see citing works
Antibody Recognition of a Highly Conserved Influenza Virus Epitope
Ekiert, D. C., Bhabha, G., Elsliger, M.-A., Friesen, R. H. E., Jongeneelen, M., Throsby, M., Goudsmit, J., & Wilson, I. A. (2009) · Science · doi:10.1126/science.1171491 · Cited by 1,326 · see citing works
Tian, X., Li, C., Huang, A., Xia, S., Lu, S., Shi, Z., Lu, L., Jiang, S., Yang, Z., Wu, Y., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1729069 · Cited by 1,239 · see citing works
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 · see citing works
The pathogenicity of SARS-CoV-2 in hACE2 transgenic mice
Bao, L., Deng, W., Huang, B., Gao, H., Liu, J., Ren, L., Wei, Q., Yu, P., Xu, Y., Qi, F., et al. (2020) · Nature · doi:10.1038/s41586-020-2312-y · Cited by 1,126 · see citing works
Self-citationA 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 1,115 · see citing works
Tiller, T., Meffre, E., Yurasov, S., Tsuiji, M., Nussenzweig, M. C., & Wardemann, H. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.09.017 · Cited by 1,078 · see citing works
Convalescent plasma as a potential therapy for COVID-19
Chen, L., Xiong, J., Bao, L., & Shi, Y. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30141-9 · Cited by 1,038 · see citing works
Self-citationRapid cloning of high-affinity human monoclonal antibodies against influenza virus
Wrammert, J., Smith, K., Miller, J., Langley, W. A., Kokko, K. E., Larsen, C. P., Zheng, N., Mays, I., Garman, L., Helms, C., et al. (2008) · Nature · doi:10.1038/nature06890 · Cited by 1,026 · see citing works
McCray, P. B., Pewe, L., Wohlford-Lenane, C., Hickey, M., Manzel, L., Shi, L., Netland, J., Jia, H. P., Halabi, C., Sigmund, C. D., et al. (2007) · Journal of Virology · doi:10.1128/jvi.02012-06 · Cited by 1,010 · see citing works
The Mechanism and Regulation of Chromosomal V(D)J Recombination
Bassing, C. H., Swat, W., & Alt, F. W. (2002) · Cell · doi:10.1016/s0092-8674(02)00675-x · Cited by 968 · see citing works
Monaco, G., Lee, B., Xu, W., Mustafah, S., Hwang, Y. Y., Carré, C., Burdin, N., Visan, L., Ceccarelli, M., Poidinger, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.041 · Cited by 958 · see citing works
Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
Scheid, J. F., Mouquet, H., Feldhahn, N., Seaman, M. S., Velinzon, K., Pietzsch, J., Ott, R. G., Anthony, R. M., Zebroski, H. A., Hurley, A., et al. (2009) · Nature · doi:10.1038/nature07930 · Cited by 855 · see citing works
Establishment and validation of a pseudovirus neutralization assay for SARS-CoV-2
Nie, J., Li, Q., Wu, J., Zhao, C., Hao, H., Liu, H., Zhang, L., Nie, L., Qin, H., Wang, M., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1743767 · Cited by 711 · see citing works
Self-citationAntibody 10-1074 suppresses viremia in HIV-1-infected individuals
Caskey, M. F., Schoofs, T., Gruell, H., Settler, A., Karagounis, T. K., Kreider, E. F., Murrell, B., Pfeifer, N., Nogueira, L., Oliveira, T. Y., et al. (2017) · Nature Medicine · doi:10.1038/nm.4268 · Cited by 487 · see citing works
Guidelines for Plaque-Reduction Neutralization Testing of Human Antibodies to Dengue Viruses
Roehrig, J. T., Hombach, J., & Barrett, A. D. T. (2008) · Viral Immunology · doi:10.1089/vim.2008.0007 · Cited by 450 · see citing works
Cross-reactive Antibody Response between SARS-CoV-2 and SARS-CoV Infections
Lv, H., Wu, N. C., Tsang, O. T.-Y., Yuan, M., Perera, R. A. P. M., Leung, W.-S., So, R. T. Y., Chan, J. M. C., Yip, G. K., Chik, T. S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107725 · Cited by 401 · see citing works
Self-citationProtective monotherapy against lethal Ebola virus infection by a potently neutralizing antibody
Corti, D., Misasi, J., Mulangu, S., Stanley, D. A., Kanekiyo, M., Wollen-Roberts, S. E., Ploquin, A., Doria‐Rose, N. A., Staupe, R. P., Bailey, M., et al. (2016) · Science · doi:10.1126/science.aad5224 · Cited by 398 · see citing works
High-Throughput Mapping of B Cell Receptor Sequences to Antigen Specificity
Setliff, I., Shiakolas, A. R., Pilewski, K. A., Murji, A. A., Mapengo, R. E., Janowska, K., Richardson, S., Oosthuysen, C., Raju, N., Ronsard, L., et al. (2019) · Cell · doi:10.1016/j.cell.2019.11.003 · Cited by 314 · see citing works
Irani, V., Guy, A. J., Andrew, D. W., Beeson, J. G., Ramsland, P. A., & Richards, J. S. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.03.255 · Cited by 302 · see citing works
Giudicelli, V. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj088 · Cited by 301 · see citing works
Potent cross-reactive neutralization of SARS coronavirus isolates by human monoclonal antibodies
Zhu, Z., Chakraborti, S., He, Y., Roberts, A., Sheahan, T., Xiao, X., Hensley, L. E., Prabakaran, P., Rockx, B., Sidorov, I. A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701000104 · Cited by 284 · see citing works
Self-citationFunctional single-cell hybridoma screening using droplet-based microfluidics
el Debs, B., Utharala, R., Balyasnikova, I., Griffiths, A., & Merten, C. (2012) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1204514109 · Cited by 273 · see citing works
Molecular Mechanisms of Somatic Hypermutation and Class Switch Recombination
Methot, S. P., & Noia, J. M. D. (2016) · Advances in immunology · doi:10.1016/bs.ai.2016.11.002 · Cited by 253 · see citing works
Yang, X. H., Deng, W., Tong, Z., Liu, Y., Zhang, L. F., Zhu, H., Gao, H., Huang, L., Liu, Y. I., Ma, C. M., et al. (2007) · PubMed · Cited by 252 · see citing works
Self-citationLiao, H., Levesque, M. C., Nagel, A., Dixon, A., Zhang, R., Walter, E. B., Parks, R., Whitesides, J. F., Marshall, D. J., Hwang, K., et al. (2009) · Journal of Virological Methods · doi:10.1016/j.jviromet.2009.02.014 · Cited by 249 · see citing works
Seifert, M., & Küppers, R. (2016) · Leukemia · doi:10.1038/leu.2016.226 · Cited by 249 · see citing works
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 · see citing works
Prabakaran, P., Gan, J., Feng, Y., Zhu, Z., Choudhry, V., Xiao, X., Ji, X., & Dimitrov, D. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600697200 · Cited by 232 · see citing works
Self-citationZhang, T., Cui, X., Zhao, X., Wang, J., Zheng, J., Zheng, G., Guo, W., Cai, C., He, S., & Xu, Y. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25795 · Cited by 227 · see citing works
Self-citationHigh-affinity allergen-specific human antibodies cloned from single IgE B cell transcriptomes
Croote, D., Darmanis, S., Nadeau, K. C., & Quake, S. R. (2018) · Science · doi:10.1126/science.aau2599 · Cited by 223 · see citing works
Corti, D., Zhao, J., Pedotti, M., Simonelli, L., Agnihothram, S., Fett, C., Fernandez-Rodriguez, B., Foglierini, M., Agatic, G., Vanzetta, F., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510199112 · Cited by 216 · see citing works
Hwang, W. C., Lin, Y., Santelli, E., Sui, J., Jaroszewski, L., Stec, B., Farzan, M., Marasco, W. A., & Liddington, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603275200 · Cited by 203 · see citing works
Dieterle, M. E., Haslwanter, D., Bortz, R. H., Wirchnianski, A. S., Lasso, G., Vergnolle, O., Abbasi, S. A., Fels, J. M., Laudermilch, E., Florez, C., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.020 · Cited by 202 · see citing works
DeKosky, B. J., Lungu, O. I., Park, D., Johnson, E. L., Charab, W., Chrysostomou, C., Kuroda, D., Ellington, A. D., Ippolito, G. C., Gray, J. J., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525510113 · Cited by 189 · see citing works
Clinical characteristics of recovered COVID-19 patients with re-detectable positive RNA test
An, J., Liao, X., Xiao, T., Qian, S., Yuan, J., Ye, H., Qi, F., Shen, C., Wang, L., Liu, Y., et al. (2020) · Annals of Translational Medicine · doi:10.21037/atm-20-5602 · Cited by 187 · see citing works
Self-citationImproving B-cell epitope prediction and its application to global antibody–antigen docking
Krawczyk, K., Liu, X., Baker, T., Shi, J., & Deane, C. M. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu190 · Cited by 174 · see citing works
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 · see citing works
Goldstein, L. D., Chen, Y.-J. J., Wu, J., Chaudhuri, S., Hsiao, Y.-C., Schneider, K., Hoi, K. H., Lin, Z., Guerrero, S., Jaiswal, B. S., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0551-y · Cited by 162 · see citing works
FREAD revisited: accurate loop structure prediction using a database search algorithm
Choi, Y., & Deane, C. M. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22658 · Cited by 161 · see citing works
Horns, F., Dekker, C. L., & Quake, S. R. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.063 · Cited by 157 · see citing works
Marasca, R., Vaccari, P., Luppi, M., et al. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61691-4 · Cited by 154 · see citing works
Clonal selection drives protective memory B cell responses in controlled human malaria infection
Murugan, R., Buchauer, L., Triller, G., Kreschel, C., Costa, G., Pidelaserra-Martí, G., Imkeller, K., Busse, C. E., Chakravarty, S., Sim, B. K. L., et al. (2018) · Science Immunology · doi:10.1126/sciimmunol.aap8029 · Cited by 136 · see citing works
B-cell exhaustion in HIV infection
Moir, S. L., & Fauci, A. S. (2014) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0000000000000092 · Cited by 116 · see citing works
Passive antibody therapy in COVID-19
Abraham, J. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-0365-7 · Cited by 110 · see citing works
Cross-reactive antibody response between SARS-CoV-2 and SARS-CoV infectionsPreprint
Lv, H., Wu, N. C., Tsang, O. T., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.15.993097 · Cited by 101 · see citing works
Górny, M. K., Wang, X., Williams, C. A. U., Volsky, B., Revesz, K., Witover, B., Burda, S. T., Urbanski, M. M., Nyambi, P. N., Krachmarov, C. P., et al. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.09.005 · Cited by 100 · see citing works
Clinical characteristics of the recovered COVID-19 patients with re-detectable positive RNA testPreprint
An, J., Liao, X., Xiao, T., et al. (2020) · medRxiv · doi:10.1101/2020.03.26.20044222 · Cited by 98 · see citing works
Antibodies and vaccines against Middle East respiratory syndrome coronavirus
Xu, J., Jia, W., Wang, P., Zhang, S., Shi, X., Wang, X., & Zhang, L. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1624482 · Cited by 84 · see citing works
Shinde, 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 · see citing works
Matsuyama, S., Shirato, K., Kawase, M., et al. (2018) · Journal of Virology · doi:10.1128/jvi.00683-18 · Cited by 70 · see citing works
Using a combined computational-experimental approach to predict antibody-specific B cell epitopes
Sela-Culang, I., Benhnia, M. R.-E.-I., Matho, M. H., Kaever, T., Maybeno, M., Schlossman, A., Nimrod, G., Li, S., Xiang, Y., Zajonc, D., et al. (2014) · Structure · doi:10.1016/j.str.2014.02.003 · Cited by 69 · see citing works
Setthapramote, C., Sasaki, T., Puiprom, O., et al. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.057 · Cited by 58 · see citing works
How B-Cell Receptor Repertoire Sequencing Can Be Enriched with Structural Antibody Data
Kovaltsuk, A., Krawczyk, K., Galson, J. D., Kelly, D. F., Deane, C. M., & Trück, J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01753 · Cited by 48 · see citing works
Kovaltsuk, A., Raybould, M. I. J., Wong, W. K., Marks, C., Kelm, S., Snowden, J., Trück, J., & Deane, C. M. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007636 · Cited by 39 · see citing works
Niu, X., Zhao, L., Qu, L., Yao, Z., Zhang, F., Yan, Q., Zhang, S., Liang, R., Chen, P., Luo, J. L., et al. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1614885 · Cited by 33 · see citing works
Self-citationSCALOP: sequence-based antibody canonical loop structure annotation
Wong, W. K., Georges, G. J., Ros, F., Kelm, S., Lewis, A. P., Taddese, B., Leem, J., & Deane, C. M. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty877 · Cited by 32 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
Omicron 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 · see citing works
Self-citationEvolution of antibody immunity to SARS-CoV-2
Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674 · see citing works
The 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
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 · see citing works
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 · see citing works
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 · 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
Baum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253 · 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
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
Seow, J., Graham, C., Merrick, B., Acors, S., Pickering, S., Steel, K. J. A., Hemmings, O., O’Byrne, A., Kouphou, N., Galao, R. P., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00813-8 · Cited by 1,419 · 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
Greaney, 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
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-citationCOVID-19 immune features revealed by a large-scale single-cell transcriptome atlas
Ren, X., Wen, W., Fan, X., Hou, W., Su, B., Cai, P., Li, J., Liu, Y., Tang, F., Zhang, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.053 · Cited by 865 · see citing works
Self-citationBarnes, 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 · see citing works
SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development
Wang, M.-Y., Zhao, R., Gao, L.-J., Gao, X.-F., Wang, D.-P., & Cao, J.-M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.587269 · Cited by 874 · see citing works
Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection
Wang, Z., Muecksch, F., Schaefer-Babajew, D., Finkin, S., Viant, C., Gaebler, C., Hoffmann, H. H., Barnes, C. O., Cipolla, M., Ramos, V., et al. (2021) · Nature · doi:10.1038/s41586-021-03696-9 · Cited by 721 · 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
Antibody-dependent enhancement and SARS-CoV-2 vaccines and therapies
Lee, W. S., Wheatley, A. K., Kent, S. J., & DeKosky, B. J. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00789-5 · Cited by 676 · see citing works
Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses
Schmidt, F., Weisblum, Y., Muecksch, F., Hoffmann, H.-H., Michailidis, E., Lorenzi, J. C. C., Mendoza, P., Rutkowska, M., Bednarski, E., Gaebler, C., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201181 · Cited by 572 · see citing works
Circular RNA Vaccines against SARS-CoV-2 and Emerging Variants
Qu, L., Yi, Z., Shen, Y., Lin, L., Chen, F., Xu, Y., Wu, Z., Tang, H., Zhang, X., Tian, F., et al. (2021) · doi:10.1101/2021.03.16.435594 · Cited by 636 · see citing works
Self-citationmRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · Science · doi:10.1126/science.abg9175 · Cited by 557 · see citing works
Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519 · 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
Enhanced SARS-CoV-2 neutralization by dimeric IgA
Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Viant, C., Gaebler, C., Cipolla, M., Hoffmann, H.-H., Oliveira, T. Y., Oren, D. A., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf1555 · Cited by 475 · see citing works
Humoral and circulating follicular helper T cell responses in recovered patients with COVID-19
Juno, J. A., Tan, H.-X., Lee, W. S., Reynaldi, A., Kelly, H. G., Wragg, K., Esterbauer, R., Kent, H. E., Batten, C. J., Mordant, F. L., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0995-0 · Cited by 437 · see citing works
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 · see citing works
Winkler, E. S., Gilchuk, P., Yu, J., Bailey, A. L., Chen, R. E., Chong, Z., Zost, S. J., Jang, H., Huang, Y., Allen, J. D., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.026 · Cited by 366 · see citing works
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
Yuan, M., Huang, D., Lee, C.-C. D., Wu, N. C., Jackson, A. M., Zhu, X., Liu, H., Peng, L., van Gils, M. J., Sanders, R. W., et al. (2021) · doi:10.1101/2021.02.16.430500 · Cited by 364 · see citing works
Schäfer, A., Muecksch, F., Lorenzi, J. C. C., Leist, S. R., Cipolla, M., Bournazos, S., Schmidt, F., Maison, R. M., Gazumyan, A., Martinez, D. R., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20201993 · Cited by 305 · see citing works
Kreye, J., Reincke, S. M., Kornau, H.-C., Sánchez-Sendin, E., Corman, V. M., Liu, H., Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.049 · Cited by 347 · see citing works
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
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., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285 · see citing works
Self-citationSARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2
Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.005 · Cited by 273 · see citing works
Wang, R., Zhang, Q., Ge, J., Ren, W., Zhang, R., Lan, J., Ju, B., Su, B., Yu, F., Chen, P., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.06.003 · Cited by 240 · see citing works
Self-citationA Potently Neutralizing Antibody Protects Mice against SARS-CoV-2 Infection
Alsoussi, W. B., Turner, J. S., Case, J. B., Zhao, H., Schmitz, A. J., Zhou, J. Q., Chen, R. E., Lei, T., Rizk, A. A., McIntire, K. M., et al. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000583 · Cited by 181 · see citing works
Wang, K., Long, Q.-X., Deng, H.-J., Hu, J., Gao, Q.-Z., Zhang, G.-J., He, C.-L., Huang, L.-Y., Hu, J.-L., Chen, J., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1143 · Cited by 218 · see citing works
Molecular determinants and mechanism for antibody cocktail preventing SARS-CoV-2 escape
Ku, Z., Xie, X., Davidson, E., Ye, X., Su, H., Menachery, V. D., Li, Y., Yuan, Z., Zhang, X., Muruato, A. E., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20789-7 · Cited by 160 · see citing works
Self-citationProlonged evolution of the human B cell response to SARS-CoV-2 infection
Sakharkar, M., Rappazzo, C. G., Wieland-Alter, W. F., Hsieh, C.-L., Wrapp, D., Esterman, E. S., Kaku, C. I., Wec, A. Z., Geoghegan, J. C., McLellan, J. S., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abg6916 · Cited by 174 · see citing works
Stewart, A., Ng, J. C.-F., Wallis, G., Tsioligka, V., Fraternali, F., & Dunn-Walters, D. K. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.602539 · Cited by 161 · see citing works
Shan, S., Luo, S., Yang, Z., Hong, J., Su, Y., Ding, F., Fu, L., Li, C., Chen, P., Ma, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122954119 · Cited by 157 · see citing works
Deep geometric representations for modeling effects of mutations on protein-protein binding affinity
Liu, X., Luo, Y., Li, P., Song, S., & Peng, J. (2021) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009284 · Cited by 140 · see citing works
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · doi:10.1101/2021.02.05.21251182 · Cited by 559 · see citing works
Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain
Tan, T. J. C., Yuan, M., Kuzelka, K., Padron, G. C., Beal, J. R., Chen, X., Wang, Y., Rivera-Cardona, J., Zhu, X., Stadtmueller, B. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24123-7 · Cited by 75 · 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
“, 2020), (2) a phase 2 study of the single RBM mAb BGB-DXP593 tested at three undisclosed doses administered intravenously (Cao et al., 2020), and (3) a phase 1/2/3 study of the single mAb ADG20 recognizing a conserved site on RBD tested as a single undisclosed dose administered either intravenously or intramuscularly…”
InfluentialSuryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · doi:10.1101/2021.01.19.427324 · Cited by 361 · see citing works
Genetic and structural basis for recognition of SARS-CoV-2 spike protein by a two-antibody cocktail
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., et al. (2021) · doi:10.1101/2021.01.27.428529 · Cited by 55 · see citing works
Self-citationDeficiency of Tfh Cells and Germinal Center in Deceased COVID-19 Patients
Duan, Y.-Q., Xia, M.-H., Ren, L., Zhang, Y.-F., Ao, Q.-L., Xu, S.-P., Kuang, D., Liu, Q., Yan, B., Zhou, Y.-W., et al. (2020) · Current Medical Science · doi:10.1007/s11596-020-2225-x · Cited by 59 · see citing works
Self-citationMuecksch, F., Weisblum, Y., Barnes, C. O., Schmidt, F., Schaefer-Babajew, D., Lorenzi, J. C. C., Flyak, A. I., DeLaitsch, A. T., Huey-Tubman, K. E., Hou, S., et al. (2021) · doi:10.1101/2021.03.07.434227 · Cited by 39 · see citing works
Guo, Y., Zhang, G., Yang, Q., Xie, X., Lu, Y., Cheng, X., Wang, H., Liang, J., Tang, J., Gao, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39267-x · Cited by 28 · see citing works
“The clonotypes featuring a frequency higher than 1, expressing IGHG1 but not IGHG2, having a somatic hypermutation (SHM) rate higher than 2% (corresponding to suf fi cient af fi nity maturation), and containing at least 1 MBC were considered to have high con fi dence in subsequent experiments 24 (Fig.”
Self-citationA Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants
Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.766821 · Cited by 21 · see citing works
de Mattos Barbosa, M. G., Liu, H., Huynh, D., Shelley, G., Keller, E. T., Emmer, B. T., Sherman, E., Ginsburg, D., Kennedy, A. A., Tai, A. W., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.147386 · Cited by 14 · see citing works
Zhou, C., Sun, M., Huang, X., Liu, P., Ouyang, Z., Wu, M., Yuan, L., Chen, J., Shu, W., Cao, T., et al. (2025) · hLife · doi:10.1016/j.hlife.2025.04.008 · Cited by 4 · see citing works
Self-citation
- Authors
- Cao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., Chai, X., He, R., Li, X., Lv, Q., Zhu, H., Deng, W., Xu, Y., Wang, Y., Qiao, L., Tan, Y., Song, L., Wang, G., Du, X., Gao, N., Liu, J., Xiao, J., Su, X.-D., Du, Z., Feng, Y., Qin, C., Qin, C., Jin, R., & Xie, X. S.
- Affiliations
- Peking University (CN)
- Capital Medical University (CN)
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- Academy of Military Medical Sciences (CN)
- Corresponding author
- Qin, Chuan
- Jin, Ronghua
- Xie, X. Sunney
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-07
- Volume
- 182
- Issue
- 1
- Pages
- 73-84.e16
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7231725
- OpenAlex
- W3024602798
- Cited by
- 1,188
- References
- 82
- Citations by year
- 2026: 25 · 2025: 58 · 2024: 74 · 2023: 116 · 2022: 204 · 2021: 468 · 2020: 242
- FWCI
- 33.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Beijing Advanced Innovation Center for Genomics
- Fundamental Research Funds for the Central Universities (A20ZX00846)
- Beijing Municipal Commission of Science and Technology (Z201100005420018)
- National Center for Protein Sciences at Peking University
- National Mega projects of China for Major Infectious Diseases (2017ZX10304402)
- Development Project of China (2016YFD0500304)
- CAMS initiative for Innovative Medicine of China (2016-12M-2-006)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- SARS-CoV-2, neutralizing antibodies, convalescent patients, B cells, single-cell RNA sequencing, antibody discovery, spike protein, ACE2 binding site, therapeutic antibodies, hACE2 transgenic mice, cryo-EM structure
- MeSH terms
- COVID-19, Animals, Antibodies, Monoclonal, B-Lymphocytes, Convalescence, Humans, Pneumonia, Viral, Sequence Analysis, RNA, Coronavirus Infections, VDJ Exons, Mice, Antibodies, Neutralizing, Pandemics, Single-Cell Analysis, High-Throughput Nucleotide Sequencing, Spike Glycoprotein, Coronavirus
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