Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
Open accessAbstract
An antibody cocktail against SARS-CoV-2: There is an urgent focus on antibodies that target the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viral spike and prevent the virus from entering host cells. Hansen et al. generated a large panel of antibodies against the spike protein from humanized mice and recovered patients. From this panel, they identified several neutralizing antibodies, including pairs that do not compete for binding to the receptor binding domain. Baum et al. focused in on four of these antibodies. All four are effective against known spike variants. However, by growing a pseudovirus that expresses the spike in the presence of individual antibodies, the authors were able to select for spike mutants resistant to that antibody. In contrast, escape mutants are not selected when pseudovirus is grown in the presence of pairs of antibodies that either do not compete or only partially compete for binding to the RBD. Such a pair might be used in a therapeutic antibody cocktail. Science , this issue p. 1010 , p. 1014
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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 [34]
REGN-10987 was included as a positive control during experimental evaluation.
“During experimental evaluation, we also included REGN-10987 (44), an ultrapotent antibody approved for emergency use authorization, as the positive control.”
From Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization (2022) · cites this paper as [44]
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cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · 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
Combined Nivolumab and Ipilimumab or Monotherapy in Untreated Melanoma
Larkin, J., Chiarion-Sileni, V., Gonzalez, R., Grob, J. J., Cowey, C. L., Lao, C. D., Schadendorf, D., Dummer, R., Smylie, M., Rutkowski, P., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1504030 · Cited by 8,157 · see citing works
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983 · see citing works
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q. (2020) · Science · doi:10.1126/science.abb2762 · Cited by 4,950 · 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
Johnsson, B., Löfås, S., & Lindquist, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90424-r · Cited by 1,272 · see citing works
A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum
Shaner, N. C., Lambert, G. G., Chammas, A., Ni, Y., Cranfill, P. J. C., Baird, M. A., Sell, B., Allen, J. R., Day, R. N., Israelsson, M., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2413 · Cited by 1,260 · 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
Self-citationRogers, 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
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
Wu, Y., Wang, F., Shen, C., Peng, W., Li, D., Zhao, C., Li, Z., Li, S., Bi, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc2241 · Cited by 955 · 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
Recombinant vesicular stomatitis viruses from DNA.
Lawson, N. D., Stillman, E. A., Whitt, M. A., & Rose, J. K. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4477 · Cited by 617 · see citing works
A system for functional analysis of Ebola virus glycoprotein
Takada, A., Robison, C. S., Goto, H., Sanchez, A., Murti, K. G., Whitt, M. A., & Kawaoka, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14764 · Cited by 575 · see citing works
Murphy, A. J., Macdonald, L. E., Stevens, S. G., Karow, M. L., Dore, A. T., Pobursky, K. J., Huang, T. T., Poueymirou, W. T., Esau, L., Meola, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324022111 · Cited by 454 · see citing works
Self-citationNeutralization of SARS-CoV-2 spike pseudotyped virus by recombinant ACE2-Ig
Lei, C., Qian, K., Tian, L., Zhang, S., Fu, W., Ding, M., & Hu, S. (2020) · Nature Communications · doi:10.1038/s41467-020-16048-4 · Cited by 450 · see citing works
Whitt, M. A. (2010) · Journal of Virological Methods · doi:10.1016/j.jviromet.2010.08.006 · Cited by 431 · see citing works
Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
DiLillo, D. J., Palese, P., Wilson, P. C., & Ravetch, J. V. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84428 · Cited by 409 · see citing works
Protective 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
Precise and in situ genetic humanization of 6 Mb of mouse immunoglobulin genes
Macdonald, L. E., Karow, M. L., Stevens, S. G., Auerbach, W., Poueymirou, W. T., Yasenchak, J., Frendewey, D. A., Valenzuela, D. M., Giallourakis, C. C., Alt, F. W., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323896111 · Cited by 390 · see citing works
Self-citationAttenuated SARS-CoV-2 variants with deletions at the S1/S2 junction
Lau, S.-Y., Wang, P., Mok, B. W.-Y., Zhang, J., Chu, H., Lee, A. C.-Y., Deng, S., Chen, P., Chan, K., Song, W., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1756700 · Cited by 291 · see citing works
Saphire, E. O., Schendel, S. L., Fusco, M. L., Gangavarapu, K., Gunn, B. M., Wec, A. Z., Halfmann, P. J., Brannan, J. M., Herbert, A. S., Qiu, X., et al. (2018) · Cell · doi:10.1016/j.cell.2018.07.033 · Cited by 212 · see citing works
Self-citationPascal, K. E., Dudgeon, D., Trefry, J. C., Anantpadma, M., Sakurai, Y., Murin, C. D., Turner, H. L., Fairhurst, J. L., Torres, M., Rafique, A., et al. (2018) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiy285 · Cited by 173 · see citing works
Self-citationAntibody-mediated protection against Ebola virus
Saphire, E. O., Schendel, S. L., Gunn, B. M., Milligan, J. C., & Alter, G. (2018) · Nature Immunology · doi:10.1038/s41590-018-0233-9 · Cited by 134 · see citing works
Fukushi, S., Mizutani, T., Saijo, M., Matsuyama, S., Miyajima, N., Taguchi, F., Itamura, S., Kurane, I., & Morikawa, S. (2005) · Journal of General Virology · doi:10.1099/vir.0.80955-0 · Cited by 132 · see citing works
Exploring blocking assays using Octet, ProteOn, and Biacore biosensors
Abdiche, Y. N., Malashock, D., Pinkerton, A., et al. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.11.038 · Cited by 88 · see citing works
Yasui, F., Kohara, M., Kitabatake, M., Nishiwaki, T., Fujii, H., Tateno, C., Yoneda, M., Morita, K., Matsushima, K., Koyasu, S., et al. (2014) · Virology · doi:10.1016/j.virol.2014.02.005 · Cited by 83 · see citing works
Human immunoglobulin variable region gene analysis by single cell RT-PCR
Wang, X., & Stollar, B. D. (2000) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00260-x · Cited by 80 · see citing works
Stillman, E. A., Rose, J. K., & Whitt, M. A. (1995) · Journal of Virology · doi:10.1128/jvi.69.5.2946-2953.1995 · Cited by 52 · see citing works
Immunoglobulin genes in transgenic mice
Alt, F. W., Blackwell, T. K., & Yancopoulos, G. D. (1985) · Trends in Genetics · doi:10.1016/0168-9525(85)90089-7 · Cited by 41 · see citing works
Self-citationMyszka, D. G. (1999) · Journal of Molecular Recognition · doi:10.1002/(sici)1099-1352(199909/10)12:5
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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
Self-citationOmicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04385-3 · Cited by 2,006 · see citing works
REGN-COV2, a Neutralizing Antibody Cocktail, in Outpatients with Covid-19
Weinreich, D. M., Sivapalasingam, S., Norton, T., Ali, S., Gao, H., Bhore, R., Musser, B. J., Soo, Y., Rofail, D., Im, J., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2035002 · Cited by 1,642 · 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
SARS-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
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
Self-citationEscape 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
Greaney, 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
Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
Liu, L., Iketani, S., Guo, Y., Chan, J. F.-W., Wang, M., Liu, L., Luo, Y., Chu, H., Huang, Y., Nair, M. S., et al. (2022) · Nature · doi:10.1038/s41586-021-04388-0 · Cited by 1,290 · 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
Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
Yurkovetskiy, L., Wang, X., Pascal, K. E., Tomkins-Tinch, C., Nyalile, T. P., Wang, Y., Baum, A., Diehl, W. E., Dauphin, A., Carbone, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.032 · Cited by 1,025 · see citing works
Self-citationSARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies
Hoffmann, M., Arora, P., Groß, R., Seidel, A., Hörnich, B. F., Hahn, A. S., Krüger, N., Graichen, L., Hofmann-Winkler, H., Kempf, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.036 · Cited by 897 · see citing works
N-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
“Several RBD-specific mAbs capable of protecting small animals and non-human primates from SARSCoV-2 challenge are able to neutralize viral infection by targeting multiple distinct antigenic sites (Baum et al., 2020a; Hansen et al., 2020; Jones et al., 2020; Pinto et al., 2020; Rogers et al., 2020; Tortorici et al., 20…”
The 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
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
Hoffmann, M., Krüger, N., Schulz, S., Cossmann, A., Rocha, C., Kempf, A., Nehlmeier, I., Graichen, L., Moldenhauer, A.-S., Winkler, M. S., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.032 · Cited by 889 · 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
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
“1A), consistent with structural work showing that these antibodies target distinct epitopes in this motif ( 11 ).”
BackgroundNeutralizing monoclonal antibodies for treatment of COVID-19
Taylor, P. C., Adams, A. C., Hufford, M. M., de la Torre, I., Winthrop, K., & Gottlieb, R. L. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00542-x · Cited by 732 · see citing works
Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis
Johnson, B. A., Xie, X., Bailey, A. L., Kalveram, B., Lokugamage, K. G., Muruato, A., Zou, J., Zhang, X., Juelich, T., Smith, J. K., et al. (2021) · Nature · doi:10.1038/s41586-021-03237-4 · Cited by 694 · 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
Self-citationThomson, E. C., Rosen, L. E., Shepherd, J. G., Spreafico, R., da Silva Filipe, A., Wojcechowskyj, J. A., Davis, C., Piccoli, L., Pascall, D. J., Dillen, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.037 · Cited by 606 · 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
mRNA 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
Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532 · see citing works
Self-citationCerutti, 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
Self-citationREGN-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
Self-citationStructural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535 · see citing works
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412 · see citing works
CoV-AbDab: the coronavirus antibody database
Raybould, M. I. J., Kovaltsuk, A., Marks, C., & Deane, C. M. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btaa739 · Cited by 383 · see citing works
Gruell, H., Vanshylla, K., Tober-Lau, P., Hillus, D., Schommers, P., Lehmann, C., Kurth, F., Sander, L. E., & Klein, F. (2022) · Nature Medicine · doi:10.1038/s41591-021-01676-0 · Cited by 410 · 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
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-citationTubiana, J., Schneidman-Duhovny, D., & Wolfson, H. J. (2022) · Nature Methods · doi:10.1038/s41592-022-01490-7 · Cited by 274 · see citing works
Cherian, S., Potdar, V., Jadhav, S., Yadav, P., Gupta, N., Das, M., Rakshit, P., Singh, S., Abraham, P., Panda, S., et al. (2021) · doi:10.1101/2021.04.22.440932 · Cited by 730 · see citing works
Neutralizing antibody vaccine for pandemic and pre-emergent coronaviruses
Saunders, K. O., Lee, E., Parks, R., Martinez, D. R., Li, D., Chen, H., Edwards, R. J., Gobeil, S., Barr, M., Mansouri, K., et al. (2021) · Nature · doi:10.1038/s41586-021-03594-0 · Cited by 253 · 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
Copin, 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
Self-citationHoffmann, M., Hofmann-Winkler, H., Krüger, N., Kempf, A., Nehlmeier, I., Graichen, L., Arora, P., Sidarovich, A., Moldenhauer, A.-S., Winkler, M. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109415 · Cited by 258 · 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
Greaney, 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
“Dilution series of the “synthetic” sera comprised of the anti-RBD antibody rREGN10987 (Hansen et al., 2020) or anti-NTD antibody 4A8 (Chi et al.”
BackgroundInfluentialMolecular 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
An antibody-escape estimator for mutations to the SARS-CoV-2 receptor-binding domain
Greaney, A. J., Starr, T. N., & Bloom, J. D. (2022) · Virus Evolution · doi:10.1093/ve/veac021 · Cited by 147 · 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
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · doi:10.1101/2021.01.14.426475 · Cited by 901 · see citing works
Approaches and Challenges in SARS-CoV-2 Vaccine Development
Dagotto, G., Yu, J., & Barouch, D. H. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.08.002 · Cited by 103 · see citing works
Animal models in SARS-CoV-2 research
Chu, H., Chan, J. F.-W., & Yuen, K.-Y. (2022) · Nature Methods · doi:10.1038/s41592-022-01447-w · Cited by 103 · 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
Monoclonal Antibodies to Disrupt Progression of Early Covid-19 Infection
Cohen, M. S. (2021) · New England Journal of Medicine · doi:10.1056/nejme2034495 · Cited by 80 · 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) · 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-citationZhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., Landau, N. R., & Tada, T. (2021) · mBio · doi:10.1128/mbio.01386-21 · Cited by 68 · see citing works
Muecksch, 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
Kruglova, N., Siniavin, A., Gushchin, V., & Mazurov, D. (2021) · Viruses · doi:10.3390/v13061133 · Cited by 37 · see citing works
A 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
- Authors
- Hansen, J., Baum, A., Pascal, K. E., Russo, V., Giordano, S., Wloga, E., Fulton, B. O., Yan, Y., Koon, K., Patel, K., Chung, K. M., Hermann, A., Ullman, E., Cruz, J., Rafique, A., Huang, T., Fairhurst, J., Libertiny, C., Malbec, M., Lee, W.-Y., Welsh, R., Farr, G., Pennington, S., Deshpande, D., Cheng, J., Watty, A., Bouffard, P., Babb, R., Levenkova, N., Chen, C., Zhang, B., Romero Hernandez, A., Saotome, K., Zhou, Y., Franklin, M., Sivapalasingam, S., Lye, D. C., Weston, S., Logue, J., Haupt, R., Frieman, M., Chen, G., Olson, W., Murphy, A. J., Stahl, N., Yancopoulos, G. D., & Kyratsous, C. A.
- Affiliations
- Regeneron (United States) (US)
- Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591, USA.
- Tan Tock Seng Hospital (SG)
- University of Maryland, Baltimore (US)
- Corresponding author
- Hansen, Johanna
- Baum, Alina
- Kyratsous, Christos A.
- ORCID
- Hansen, Johanna
- Baum, Alina
- Pascal, Kristen E.
- Russo, Vincenzo
- Giordano, Stephanie
- Wloga, Elzbieta
- Fulton, Benjamin O.
- Yan, Ying
- Koon, Katrina
- Patel, Krunal
- Chung, Kyung Min
- Hermann, Aynur
- Ullman, Erica
- Cruz, Jonathan
- Rafique, Ashique
- Huang, Tammy
- Fairhurst, Jeanette
- Libertiny, Christen
- Malbec, Marine
- Lee, Wen-yi
- Welsh, Richard
- Farr, Glen
- Deshpande, Dipali
- Bouffard, Pascal
- Levenkova, Natasha
- Chen, Calvin
- Zhang, Bojie
- Saotome, Kei
- Zhou, Yi
- Franklin, Matthew
- Sivapalasingam, Sumathi
- Lye, David Chien
- Weston, Stuart
- Logue, James
- Haupt, Robert
- Frieman, Matthew
- Olson, William
- Murphy, Andrew J.
- Stahl, Neil
- Kyratsous, Christos A.
- Venue
- Science
- Published
- 2020-08-21
- Volume
- 369
- Issue
- 6506
- Pages
- 1010-1014
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC7299284
- OpenAlex
- W3034202401
- Cited by
- 1,210
- References
- 33
- Citations by year
- 2026: 34 · 2025: 62 · 2024: 95 · 2023: 146 · 2022: 317 · 2021: 424 · 2020: 130
- FWCI
- 33.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Science (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Biomedical Advanced Research and Development Authority (HHSO100201700020C)
- 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, antibody cocktail, humanized mice, spike protein, receptor binding domain, antibody escape mutants, therapeutic antibodies, antibody structure
- MeSH terms
- Betacoronavirus, Broadly Neutralizing Antibodies, Receptors, Coronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, COVID-19 Serotherapy, Adolescent, Adult, Animals, Antibodies, Viral, Antibody Affinity, Antibody-Dependent Cell Cytotoxicity, Epitopes, Binding Sites, Antibody, Cell Line, Humans, Immunization, Passive, Peptidyl-Dipeptidase A, Middle Aged, Models, Molecular, Neutralization Tests, Pneumonia, Viral, Receptors, Virus, Coronavirus Infections, Severe acute respiratory syndrome-related coronavirus, Mice, Protein Interaction Domains and Motifs, Young Adult, Antibodies, Neutralizing, Cytophagocytosis, Pandemics, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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