Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein
Open accessPreprint — published as 10.1016/j.cell.2021.03.029
Abstract
Summary: Most human monoclonal antibodies (mAbs) neutralizing SARS-CoV-2 recognize the spike (S) protein receptor-binding domain and block virus interactions with the cellular receptor angiotensin-converting enzyme 2. We describe a panel of human mAbs binding to diverse epitopes on the N-terminal domain (NTD) of S protein from SARS-CoV-2 convalescent donors and found a minority of these possessed neutralizing activity. Two mAbs (COV2-2676 and COV2-2489) inhibited infection of authentic SARS-CoV-2 and recombinant VSV/SARS-CoV-2 viruses. We mapped their binding epitopes by alanine-scanning mutagenesis and selection of functional SARS-CoV-2 S neutralization escape variants. Mechanistic studies showed that these antibodies neutralize in part by inhibiting a post-attachment step in the infection cycle. COV2-2676 and COV2-2489 offered protection either as prophylaxis or therapy, and Fc effector functions were required for optimal protection. Thus, natural infection induces a subset of potent NTD-specific mAbs that leverage neutralizing and Fc-mediated activities to protect against SARS-CoV-2 infection using multiple functional attributes.
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The lentiviral pseudotyping system gives results correlating with replication competent authentic virus.
“This system has been shown to give results correlating with replication competent authentic virus20,21.”
From Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies (2021) · cites this paper as [20]
Spike pseudotype assays have been shown to have similar characteristics as neutralisation testing using fully infectious wild type SARS-CoV-2.
“Spike pseudotype assays have been shown to have similar characteristics as neutralisation testing using fully infectious wild type SARS-CoV-220.”
From Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies (2021) · cites this paper as [20]
Loss of COV2-2489 activity against B.1.1.7 may be due to NTD deletions 69-70 and 144-145.
“possibly due to the deletions present in the NTD (69–70 and 144–145)21.”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [21]
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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
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
A dynamic nomenclature proposal for SARS-CoV-2 lineages to assist genomic epidemiology
Rambaut, A., Holmes, E. C., O’Toole, Á., Hill, V., McCrone, J. T., Ruis, C., du Plessis, L., & Pybus, O. G. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0770-5 · Cited by 2,543 · see citing works
Tegally, 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
Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity
Cantuti-Castelvetri, L., Ojha, R., Pedro, L. D., Djannatian, M., Franz, J., Kuivanen, S., van der Meer, F., Kallio, K., Kaya, T., Anastasina, M., et al. (2020) · Science · doi:10.1126/science.abd2985 · Cited by 1,925 · see citing works
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885 · 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 · cited 2× · see citing works
“Most neutralizing SARS-CoV-2 mAbs block RBD interactions with ACE2 (Brouwer et al., 2020; Cao et al., 2020; Ju et al., 2020; Liu et al., 2020a; Rogers et al., 2020; Seydoux et al., 2020; Wec et al., 2020; Wu et al., 2020; Zost et al., 2020a; Zost et al., 2020b).”
Mulligan, M. J., Lyke, K. E., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Neuzil, K., Raabe, V., Bailey, R., Swanson, K. A., et al. (2020) · doi:10.1101/2020.06.30.20142570 · Cited by 1,569 · 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
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
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
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
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
Structure-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 · see citing works
SARS-CoV-2 Neutralizing Antibody LY-CoV555 in Outpatients with Covid-19
Chen, P., Nirula, A., Heller, B., Gottlieb, R. L., Boscia, J., Morris, J., Huhn, G., Cardona, J., Mocherla, B., Stosor, V., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2029849 · Cited by 1,282 · 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
Persistence and Evolution of SARS-CoV-2 in an Immunocompromised Host
Choi, B., Choudhary, M. C., Regan, J., Sparks, J. A., Padera, R. F., Qiu, X., Solomon, I. H., Kuo, H.-H., Boucau, J., Bowman, K., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmc2031364 · Cited by 1,246 · 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
Cao, 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
SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2
Clausen, T. M., Sandoval, D. R., Spliid, C. B., Pihl, J., Perrett, H. R., Painter, C. D., Narayanan, A., Majowicz, S. A., Kwong, E. M., McVicar, R. N., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.033 · Cited by 1,162 · 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
A human monoclonal antibody blocking SARS-CoV-2 infection
Wang, C., Li, W., Drabek, D., Okba, N. M. A., van Haperen, R., Osterhaus, A. D. M. E., van Kuppeveld, F. J. M., Haagmans, B. L., Grosveld, F. G., & Bosch, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16256-y · Cited by 1,115 · see citing works
Transmission of SARS-CoV-2 on mink farms between humans and mink and back to humans
Munnink, B. B. O., Sikkema, R. S., Nieuwenhuijse, D. F., Molenaar, R. J., Münger, E., Molenkamp, R., van der Spek, A. N., Tolsma, P., Rietveld, A., Brouwer, M., et al. (2020) · Science · doi:10.1126/science.abe5901 · Cited by 1,087 · 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-citationDNA vaccine protection against SARS-CoV-2 in rhesus macaques
Yu, J., Tostanoski, L. H., Peter, L., Mercado, N. B., McMahan, K., Mahrokhian, S. H., Nkolola, J. P., Liu, J., Li, Z., Chandrashekar, A., et al. (2020) · Science · doi:10.1126/science.abc6284 · Cited by 997 · see citing works
Winkler, E. S., Bailey, A. L., Kafai, N. M., Nair, S., McCune, B. T., Yu, J., Fox, J. M., Chen, R. E., Earnest, J. T., Keeler, S. P., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0778-2 · Cited by 901 · see citing works
Self-citationN-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works
SARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo
Hou, Y. J., Chiba, S., Halfmann, P., Ehre, C., Kuroda, M., Dinnon, K. H., Leist, S. R., Schäfer, A., Nakajima, N., Takahashi, K., et al. (2020) · Science · doi:10.1126/science.abe8499 · Cited by 900 · see citing works
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795 · see citing works
DiLillo, D. J., Tan, G. S., Palese, P., & Ravetch, J. V. (2014) · Nature Medicine · doi:10.1038/nm.3443 · Cited by 749 · 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
Avanzato, V. A., Matson, M. J., Seifert, S. N., Pryce, R., Williamson, B. N., Anzick, S. L., Barbian, K., Judson, S. D., Fischer, E. R., Martens, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.049 · Cited by 703 · see citing works
Negative staining and image classification — powerful tools in modern electron microscopy
Ohi, M. D., Li, Y., Cheng, Y., & Walz, T. (2004) · Biological Procedures Online · doi:10.1251/bpo70 · Cited by 685 · see citing works
Prospective 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
ter Meulen, J., van den Brink, E. N., Poon, L. L. M., Marissen, W. E., Leung, C. S.-W., Cox, F., Cheung, C. Y., Bakker, A. Q., Bogaards, J. A., van Deventer, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030237 · Cited by 599 · see citing works
Angiotensin I converting enzyme.
Erdös, E. G. (1975) · Circulation Research · doi:10.1161/01.res.36.2.247 · Cited by 555 · see citing works
Severe Acute Respiratory Syndrome Coronavirus 2 from Patient with Coronavirus Disease, United States
Harcourt, J. L., Tamin, A., Lu, X., Kamili, S., Sakthivel, S. K., Murray, J., Queen, K. J., Tao, Y., Paden, C. R., Zhang, J., et al. (2020) · Emerging infectious diseases · doi:10.3201/eid2606.200516 · Cited by 524 · see citing works
Broad neutralization of SARS-related viruses by human monoclonal antibodies
Wec, A. Z., Wrapp, D., Herbert, A. S., Maurer, D. P., Haslwanter, D., Sakharkar, M., Jangra, R. K., Dieterle, M. E., Lilov, A., Huang, D., et al. (2020) · Science · doi:10.1126/science.abc7424 · Cited by 520 · 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
A SARS-CoV-2 Infection Model in Mice Demonstrates Protection by Neutralizing Antibodies
Hassan, A. O., Case, J. B., Winkler, E. S., Thackray, L. B., Kafai, N. M., Bailey, A. L., McCune, B. T., Fox, J. M., Chen, R. E., Alsoussi, W. B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.011 · Cited by 477 · see citing works
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 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-citationLethality of SARS-CoV-2 infection in K18 human angiotensin-converting enzyme 2 transgenic mice
Oladunni, F. S., Park, J.-G., Pino, P., Gonzalez, O., Akhter, A., Allué-Guardia, A., Olmo-Fontánez, A. M., Gautam, S., Garcia-Vilanova, A., Ye, C.-J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19891-7 · Cited by 394 · see citing works
Halper-Stromberg, A., Lu, C.-L., Klein, F., Horwitz, J. A., Bournazos, S., Nogueira, L., Eisenreich, T., Liu, C., Gazumyan, A., Schaefer, U., et al. (2014) · Cell · doi:10.1016/j.cell.2014.07.043 · Cited by 378 · see citing works
Laczko, D. I., Hogan, M. J., Toulmin, S. A., Hicks, P. D., Lederer, K., Gaudette, B. T., Castaño, D., Amanat, F., Muramatsu, H., Oguin, T. H., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.019 · Cited by 366 · see citing works
Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.001 · Cited by 364 · see citing works
Distinct Early Serological Signatures Track with SARS-CoV-2 Survival
Atyeo, C., Fischinger, S., Zohar, T., Slein, M. D., Burke, J., Loos, C., McCulloch, D. J., Newman, K. L., Wolf, C., Yu, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.020 · Cited by 349 · see citing works
Enhanced clearance of HIV-1–infected cells by broadly neutralizing antibodies against HIV-1 in vivo
Lu, C.-L., Murakowski, D. K., Bournazos, S., Schoofs, T., Sarkar, D., Halper-Stromberg, A., Horwitz, J. A., Nogueira, L., Golijanin, J., Gazumyan, A., et al. (2016) · Science · doi:10.1126/science.aaf1279 · Cited by 348 · 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
Potent human neutralizing antibodies elicited by SARS-CoV-2 infectionPreprint
Ju, B., Zhang, Q., Ge, X., et al. (2020) · bioRxiv · doi:10.1101/2020.03.21.990770 · Cited by 256 · see citing works
Recurrent emergence and transmission of a SARS-CoV-2 spike deletion H69/V70
Kemp, S. A., Meng, B., Ferriera, I. A., Datir, R., Harvey, W. T., Papa, G., Lytras, S., Collier, D. A., Mohamed, A., Gallo, G., et al. (2020) · doi:10.1101/2020.12.14.422555 · Cited by 252 · see citing works
Growth, detection, quantification, and inactivation of SARS-CoV-2
Case, J. B., Bailey, A. L., Kim, A. S., Chen, R. E., & Diamond, M. (2020) · Virology · doi:10.1016/j.virol.2020.05.015 · Cited by 230 · see citing works
Self-citationHuman Fc gamma RI and Fc gamma RII interact with distinct but overlapping sites on human IgG
Lund, J., Winter, G., Jones, P., Pound, J. D., Tanaka, T., Walker, M. R., Artymiuk, P. J., Arata, Y., Burton, D. R., Jefferis, R., et al. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.8.2657 · Cited by 212 · see citing works
Cleavage efficient 2A peptides for high level monoclonal antibody expression in CHO cells
Chng, J., Wang, T., Nian, R., Lau, A., Hoi, K. M., Ho, S. C., Gagnon, P., Bi, X., & Yang, Y. (2015) · mAbs · doi:10.1080/19420862.2015.1008351 · Cited by 196 · see citing works
Golden, J. W., Cline, C. R., Zeng, X., Garrison, A. R., Carey, B. D., Mucker, E. M., White, L. E., Shamblin, J. D., Brocato, R. L., Liu, J., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.142032 · Cited by 195 · see citing works
A 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
Self-citationLiu, Z., Zheng, H., Lin, H., Li, M., Yuan, R., Peng, J., Xiong, Q., Sun, J., Li, B., Wu, J., et al. (2020) · Journal of Virology · doi:10.1128/jvi.00790-20 · Cited by 162 · see citing works
An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain
Wu, N. C., Yuan, M., Liu, H., Lee, C.-C. D., Zhu, X., Bangaru, S., Torres, J. L., Caniels, T. G., Brouwer, P. J. M., van Gils, M. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108274 · Cited by 157 · see citing works
A high‐throughput shotgun mutagenesis approach to mapping B‐cell antibody epitopes
Davidson, E., & Doranz, B. J. (2014) · Immunology · doi:10.1111/imm.12323 · Cited by 154 · see citing works
Self-citationWines, B. D., Powell, M. S., Parren, P. W. H. I., Barnes, N. C., & Hogarth, P. M. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.10.5313 · Cited by 152 · see citing works
Zhou, H., Chen, Y., Zhang, S., Niu, P., Qin, K., Jia, W., Huang, B., Zhang, S., Lan, J., Zhang, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10897-4 · Cited by 142 · see citing works
Isolation and characterization of SARS-CoV-2 from the first US COVID-19 patientPreprint
Harcourt, J. L., Tamin, A., Lu, X., Kamili, S., Sakthivel, S. K., Murray, J., Queen, K. J., Tao, Y., Paden, C. R., Zhang, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.02.972935 · Cited by 141 · see citing works
Jones, B. E., Brown-Augsburger, P., Corbett, K., Westendorf, K., Davies, J., Cujec, T., Wiethoff, C. M., Blackbourne, J., Heinz, B., Foster, D., et al. (2020) · bioRxiv · doi:10.1101/2020.09.30.318972 · Cited by 140 · see citing works
Gilchuk, P., Murin, C. D., Milligan, J. C., Cross, R. W., Mire, C. E., Ilinykh, P. A., Huang, K., Kuzmina, N. A., Altman, P. X., Hui, S., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.01.001 · Cited by 86 · see citing works
Self-citationEnhancing dengue virus maturation using a stable furin over-expressing cell line
Mukherjee, S., Sirohi, D., Dowd, K. A., Chen, Z., Diamond, M. S., Kuhn, R. J., & Pierson, T. C. (2016) · Virology · doi:10.1016/j.virol.2016.06.022 · Cited by 82 · see citing works
Self-citationFox, J. M., Roy, V., Gunn, B. M., Huang, L., Edeling, M. A., Mack, M., Fremont, D. H., Doranz, B. J., Johnson, S., Alter, G., et al. (2019) · Science Immunology · doi:10.1126/sciimmunol.aav5062 · Cited by 79 · see citing works
Self-citationChiodo, F., Bruijns, S. C. M., Rodríguez, E., Li, R. J. E., Molinaro, A., Silipo, A., Lorenzo, F. D., García-Rivera, D., Valdés-Balbín, Y., Vérez-Bencomo, V. G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.13.092478 · Cited by 73 · see citing works
Voss, W. N., Hou, Y., Johnson, N., Kim, J. E., Delidakis, G., Horton, A. P., Bartzoka, F., Paresi, C. J., Tanno, Y., Abbasi, S. A., et al. (2020) · bioRxiv · doi:10.1101/2020.12.20.423708 · Cited by 57 · see citing works
Integrated pipeline for the accelerated discovery of antiviral antibody therapeutics
Gilchuk, P., Bombardi, R. G., Erasmus, J. H., Tan, Q., Nargi, R. S., Soto, C. S., Abbink, P., Suscovich, T. J., Durnell, L. A., Khandhar, A. P., et al. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-0594-x · Cited by 54 · see citing works
Self-citationLandscape and Selection of Vaccine Epitopes in SARS-CoV-2Preprint
Smith, C. C., Entwistle, S., Willis, C., Vensko, S. P., Beck, W., Garness, J. A., Sambade, M., Routh, E. D., Olsen, K. S., Kodysh, J., et al. (2020) · bioRxiv · doi:10.1101/2020.06.04.135004 · Cited by 51 · see citing works
Convalescent plasma to treat COVID-19
Bloch, E. M. (2020) · Blood · doi:10.1182/blood.2020007714 · Cited by 37 · see citing works
ACE2 partially dictates the host range and tropism of SARS-CoV-2
Gao, S., & Zhang, L. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.11.032 · Cited by 34 · see citing works
A proof of concept for neutralizing antibody-guided vaccine design against SARS-CoV-2Preprint
Zhang, L., Cao, L., Gao, X., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.23.309294 · Cited by 27 · see citing works
Ying, X. (2020) · Virology & Mycology · doi:10.35248/2161-0517.20.09.191 · Cited by 20 · see citing works
Virus load and virus shedding of SARS-CoV-2 and their impact on patient outcomes
Chen, P., Yu, X., Liu, Y.-P., et al. (2020) · World Journal of Clinical Cases · doi:10.12998/wjcc.v8.i24.6252 · Cited by 12 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- N gene (Log 10 copies/mg) bioRxiv preprint doi: https://doi.org/10.1101/2021.01.19.427324; this version posted January 20, 2021. The copyright holder for this preprint
Cited by
Sorted by citations
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) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147 · 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-citationSARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies
Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R., Walls, A. C., Kemp S, S. A., Bassi, J., Pinto, D., Fregni, C. S., et al. (2021) · doi:10.1101/2021.01.19.21249840 · Cited by 729 · see citing works
Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies
Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R. P., Walls, A. C., Kemp, S. A., Bassi, J., Pinto, D., Silacci-Fregni, C., et al. (2021) · Nature · doi:10.1038/s41586-021-03412-7 · Cited by 728 · see citing works
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera
Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.033 · Cited by 460 · see citing works
Suryadevara, 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) · Cell · doi:10.1016/j.cell.2021.03.029 · Cited by 397 · 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) · doi:10.1101/2021.01.18.427166
Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants
McCallum, M., Walls, A. C., Sprouse, K. R., Bowen, J. E., Rosen, L. E., Dang, H. V., Marco, A. D., Franko, N., Tilles, S. W., Logue, J. K., et al. (2021) · Science · doi:10.1126/science.abl8506 · Cited by 273 · see citing works
“Abs that bind to specific sites on the RBD (15– 22), the NTD (23–26), or the fusion machinery stem helix (27–31) interfere with receptor attachment or membrane fusion.”
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
“) that measures virus-induced cytopathic effect (CPE) (Gilchuk et al., 2020; Suryadevara et al., 2021; Zost et al., 2020b).”
InfluentialSelf-citationMarkers of Polyfunctional SARS-CoV-2 Antibodies in Convalescent Plasma
Natarajan, H., Crowley, A. R., Butler, S. E., Xu, S., Weiner, J. A., Bloch, E. M., Littlefield, K. E., Wieland‐Alter, W., Connor, R. I., Wright, P. F., et al. (2021) · mBio · doi:10.1128/mbio.00765-21 · Cited by 98 · see citing works
Crowley, A. R., Natarajan, H., Hederman, A. P., Bobak, C. A., Weiner, J. A., Wieland-Alter, W., Lee, J., Bloch, E. M., Tobian, A. A. R., Redd, A. D., et al. (2022) · eLife · doi:10.7554/elife.75228 · Cited by 49 · see citing works
“This evidence extends beyond correlative observations 45,48 to include mechanistic 1 evidence of in vivo contributions via Fc sequence engineering to knockout or enhance these activities 44,46 , as well as on the basis of depletion of effector cells 46 .”
Profiles of current COVID-19 vaccines
Heinz, F. X., & Stiasny, K. (2021) · Wiener klinische Wochenschrift · doi:10.1007/s00508-021-01835-w · Cited by 45 · see citing works
Nitahara, Y., Nakagama, Y., Kaku, N., Candray, K., Michimuko, Y., Tshibangu-Kabamba, E., Kaneko, A., Yamamoto, H., Mizobata, Y., Kakeya, H., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00965-21 · Cited by 26 · see citing works
Conserved Neutralizing Epitopes on the N-Terminal Domain of Variant SARS-CoV-2 Spike ProteinsPreprint
Wang, Z.-J., Muecksch, F., Cho, A., Gaebler, C., Hoffmann, H., Ramos, V. A., Zong, S., Cipolla, M., Johnson, B., Schmidt, F., et al. (2022) · bioRxiv · doi:10.1101/2022.02.01.478695 · Cited by 20 · see citing works
“…appear to target the previously defined supersite on NTD (Amanat et al., 2021; Cerutti et al., 2021b; Chi et al., 2020; Dussupt et al., 2021; Haslwanter et al., 2021; Li et al., 2021; Liu et al., 2021; McCallum et al., 2021a; Planas et al., 2021b; Suryadevara et al., 2021b; Voss et al., 2021).”
InfluentialSingh, P., Sharma, K. K., Singh, P., Bhargava, A., Negi, S. S., Sharma, P., Bhise, M. P., Tripathi, M. K., Jindal, A., & Nagarkar, N. M. (2022) · Microbial Pathogenesis · doi:10.1016/j.micpath.2022.105404 · Cited by 22 · see citing works
“T19R, G142D, E156G, and two deletions of F157 and R158 located within NTD have altered a recognized monoclonal antibody (mAb) recognition site N1 and N3 loop to helps the virus in escaping antibody response [4,11].”
Eslami, S., Glassy, M. C., & Ghafouri‐Fard, S. (2021) · Gene · doi:10.1016/j.gene.2021.146113 · Cited by 12 · see citing works
“It has been shown that Y144 deletion contribute to immune escape and mostly confers resistance to most NTD-directed monoclonal antibodies (mAbs) (Suryadevara, 2021).”
Rapid Identification of Neutralizing Antibodies against SARS-CoV-2 Variants by mRNA Display
Tanaka, S., Olson, C., Barnes, C., et al. (2021) · bioRxiv · doi:10.1101/2021.09.14.460356 · Cited by 10
Standardized Two-Step Testing of Antibody Activity in COVID-19 Convalescent Plasma
Gilchuk, P., Thomsen, I. P., Yoder, S. M., Brady, E. J., Chappell, J. D., Stevens, L. J., Denison, M. R., Sutton, R. E., Chen, R. E., VanBlargan, L. A., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103602 · Cited by 7 · see citing works
Self-citation
- Authors
- Suryadevara, 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., Fouch, M. E., Davidson, E., Doranz, B. J., Carnahan, R. H., Thackray, L. B., Diamond, M. S., & Crowe, J. E.
- Affiliations
- Vanderbilt University Medical Center (US)
- Washington University in St. Louis (US)
- Integral Molecular (United States) (US)
- Corresponding author
- Thackray, Larissa B.
- Diamond, Michael S.
- Crowe, James E.
- ORCID
- Venue
- Cell
- Publisher
- openRxiv
- Published
- 2021-01-20
- Volume
- 184
- Issue
- 9
- Pages
- 2316-2331.e15
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7836115
- OpenAlex
- W3139036184
- Cited by
- 361
- References
- 91
- Citations by year
- 2026: 10 · 2025: 17 · 2024: 58 · 2023: 45 · 2022: 119 · 2021: 111 · 2020: 1
- FWCI
- 26.42
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cell (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- George Mason University
- Vanderbilt University
- Merck KGaA
- Vanderbilt University Medical Center
- Fast Grants
- National Institutes of Health (-0001, COVID-19)
- Defense Advanced Research Projects Agency (HR0011‐18‐2‐0001)
- Mercatus Center, George Mason University
- National Institute of Allergy and Infectious Diseases (R01AI157155, COVID-19, 75N93019C00074, F30AI152327, T32AI138932, AI095202, 75N93019C00073, AI157155, T32AI007163, T32AI095202)
- Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases
- 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, spike protein, N-terminal domain, human monoclonal antibodies, neutralizing antibodies, antibody protection, Fc effector functions, epitope mapping, convalescent donors
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