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Human neutralizing antibodies against SARS-CoV-2 require intact Fc effector functions for optimal therapeutic protection
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Abstract
SARS-CoV-2 has caused the global COVID-19 pandemic. Although passively delivered neutralizing antibodies against SARS-CoV-2 show promise in clinical trials, their mechanism of action in vivo is incompletely understood. Here, we define correlates of protection of neutralizing human monoclonal antibodies (mAbs) in SARS-CoV-2-infected animals. Whereas Fc effector functions are dispensable when representative neutralizing mAbs are administered as prophylaxis, they are required for optimal protection as therapy. When given after infection, intact mAbs reduce SARS-CoV-2 burden and lung disease in mice and hamsters better than loss-of-function Fc variant mAbs. Fc engagement of neutralizing antibodies mitigates inflammation and improves respiratory mechanics, and transcriptional profiling suggests these phenotypes are associated with diminished innate immune signaling and preserved tissue repair. Immune cell depletions establish that neutralizing mAbs require monocytes and CD8+ T cells for optimal clinical and virological benefit. Thus, potently neutralizing mAbs utilize Fc effector functions during therapy to mitigate lung infection and disease.
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“Thus, residual SARS-CoV-2-specific non-neutralizing antibodies following infection may confer some protective benefit during reinfection, even when serum neutralizing activity has declined below the threshold of protection25–27.”
From Prospects for durable immune control of SARS-CoV-2 and prevention of reinfection (2021) · cites this paper as [27]
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“this measurement does not account for Fc effector functions; Fcγ receptor or complement protein engagement by non-, weakly-, or strongly- neutralizing antibodies that bind the SARS-CoV-2 spike protein on the surface of infected cells could confer substantial protection39–41.”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [39]
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Cites
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709
Robinson, M. D., McCarthy, D. J., & Smyth, G. K. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btp616 · Cited by 41,364
limma powers differential expression analyses for RNA-sequencing and microarray studies
Ritchie, M. E., Phipson, B., Wu, D., Hu, Y., Law, C. W., Shi, W., & Smyth, G. K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv007 · Cited by 40,458
featureCounts: an efficient general purpose program for assigning sequence reads to genomic features
Liao, Y., Smyth, G. K., & Shi, W. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt656 · Cited by 27,219
An interactive web-based dashboard to track COVID-19 in real time
Dong, E., Du, H., & Gardner, L. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30120-1 · Cited by 10,048
The trinity of COVID-19: immunity, inflammation and intervention
Tay, M. Z., Poh, C. M., Rénia, L., MacAry, P. A., & Ng, L. F. P. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-0311-8 · Cited by 4,360
Pathological inflammation in patients with COVID-19: a key role for monocytes and macrophages
Merad, M., & Martin, J. C. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-0331-4 · Cited by 2,472
Complex Immune Dysregulation in COVID-19 Patients with Severe Respiratory Failure
Giamarellos-Bourboulis, E. J., Netea, M. G., Rovina, N., Akinosoglou, K., Antoniadou, A., Antonakos, N., Damoraki, G., Gkavogianni, T., Adami, M.-E., Katsaounou, P., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.04.009 · Cited by 2,045
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
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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
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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
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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
Self-citationVanBlargan, L. A., Errico, J. M., Halfmann, P., Zost, S. J., Crowe, J. E., Purcell, L. A., Kawaoka, Y., Corti, D., Fremont, D. H., & Diamond, M. (2022) · Nature Medicine · doi:10.1038/s41591-021-01678-y · Cited by 690
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Pinto, D., Sauer, M. M., Czudnochowski, N., Low, J. S., Tortorici, M. A., Housley, M. P., Noack, J., Walls, A. C., Bowen, J. E., Guarino, B., et al. (2021) · Science · doi:10.1126/science.abj3321 · Cited by 385
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Abani, O., Abbas, A., Abbas, F., Abbas, M. A., Abbasi, S., Abbass, H., Abbott, A., Abdallah, N., Abdelaziz, A., Abdelfattah, M., et al. (2022) · The Lancet · doi:10.1016/s0140-6736(22)00163-5 · Cited by 392
Heinz, F. X., & Stiasny, K. (2021) · npj Vaccines · doi:10.1038/s41541-021-00369-6 · Cited by 378
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Correlates of protection against SARS ‐ CoV ‐2 infection and COVID‐19 disease
Goldblatt, D., Alter, G., Crotty, S., & Plotkin, S. A. (2022) · Immunological Reviews · doi:10.1111/imr.13091 · Cited by 301
Hoepel, W., Chen, H., Geyer, C. E., Allahverdiyeva, S., Manz, X. D., de Taeye, S. W., Aman, J., Mes, L., Steenhuis, M., Griffith, G. R., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf8654 · Cited by 282
Antibodies to combat viral infections: development strategies and progress
Pantaleo, G., Correia, B. E., Fenwick, C. W., Joo, V., & Perez, L. H. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00495-3 · Cited by 298
Avidity in antibody effector functions and biotherapeutic drug design
Oostindie, S. C., Lazar, G. A., Schuurman, J., & Parren, P. W. H. I. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00501-8 · Cited by 290
Broad sarbecovirus neutralization by a human monoclonal antibody
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · Nature · doi:10.1038/s41586-021-03817-4 · Cited by 255
Prospects for durable immune control of SARS-CoV-2 and prevention of reinfection
Cromer, D., Juno, J. A., Khoury, D., Reynaldi, A., Wheatley, A. K., Kent, S. J., & Davenport, M. P. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00550-x · Cited by 265
Bégin, P., Callum, J., Jamula, E., Cook, R. J., Heddle, N. M., Tinmouth, A. T., Zeller, M. P., Beaudoin-Bussières, G., Amorim, L., Bazin, R., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01488-2 · Cited by 258
Infection- and vaccine-induced antibody binding and neutralization of the B.1.351 SARS-CoV-2 variant
Edara, V. V., Norwood, C., Floyd, K., Lai, L., Davis-Gardner, M. E., Hudson, W. H., Mantus, G., Nyhoff, L. E., Adelman, M. W., Fineman, R., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.009 · Cited by 224
Dittmar, M., Lee, J. S., Whig, K., Segrist, E., Li, M., Kamalia, B., Castellana, L., Ayyanathan, K., Cardenas‐Diaz, F. L., Morrisey, E. E., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108959 · Cited by 230
Cathcart, A. L., Havenar‐Daughton, C., Lempp, F. A., Ma, D., Schmid, M., Agostini, M. L., Guarino, B., di Iulio, J., Rosen, L. E., Tucker, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.09.434607 · Cited by 210
In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains
Chen, R. E., Winkler, E. S., Case, J. B., Aziati, I. D., Bricker, T. L., Joshi, A., Darling, T. L., Ying, B., Errico, J. M., Shrihari, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03720-y · Cited by 209
Self-citationBeyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection
Zhang, A., Stacey, H. D., D’Agostino, M. R., Tugg, Y., Marzok, A., & Miller, M. S. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00813-1 · Cited by 225
Loo, Y., McTamney, P. M., Arends, R. H., Gasser, R. A., Abram, M. E., Cheng, L., Diallo, S., Flores, D. J., Bond, N. J., Ren, K., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abl8124 · Cited by 221
Self-citationUllah, I., Prévost, J., Ladinsky, M. S., Stone, H., Lu, M., Anand, S. P., Beaudoin-Bussières, G., Symmes, K., Benlarbi, M., Ding, S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.015 · Cited by 212
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Walls, A. C., Sprouse, K. R., Bowen, J. E., Joshi, A., Franko, N., Navarro, M. J., Stewart, C., Cameroni, E., McCallum, M., Goecker, E. A., et al. (2022) · Cell · doi:10.1016/j.cell.2022.01.011 · Cited by 188
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Sadler, K. E., Mogil, J. S., & Stucky, C. L. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00536-7 · Cited by 199
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Qi, H., Liu, B., Wang, X., & Zhang, L. (2022) · Nature Immunology · doi:10.1038/s41590-022-01248-5 · Cited by 195
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DeGrace, M. M., Ghedin, E., Frieman, M. B., Krammer, F., Grifoni, A., Alisoltani, A., Alter, G., Amara, R. R., Baric, R. S., Barouch, D. H., et al. (2022) · Nature · doi:10.1038/s41586-022-04690-5 · Cited by 168
Self-citationAntiviral neutralizing antibodies: from in vitro to in vivo activity
Burton, D. R. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00858-w · Cited by 168
Antibody-mediated neutralization of SARS-CoV-2
Gruell, H., Vanshylla, K., Weber, T., Barnes, C. O., Kreer, C., & Klein, F. (2022) · Immunity · doi:10.1016/j.immuni.2022.05.005 · Cited by 150
Bartsch, Y. C., Tong, X., Kang, J., Avendaño, M. J., Serrano, E. F., García‐Salum, T., Pardo‐Roa, C., Riquelme, A. J., Cai, Y., Renzi, I., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn9243 · Cited by 138
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Delannoy-Bruno, O., Desai, C., Raman, A. S., Chen, R. Y., Hibberd, M. C., Cheng, J., Han, N., Castillo, J. J., Couture, G., Lebrilla, C. B., et al. (2021) · Nature · doi:10.1038/s41586-021-03671-4 · Cited by 142
Self-citationRECOVERY Collaborative Group, Horby, P., Mafham, M. M., Peto, L., Campbell, M. R., Pessoa-Amorim, G., Spata, E., Staplin, N., Emberson, J., Prudon, B., et al. (2021) · medRxiv · doi:10.1101/2021.06.15.21258542 · Cited by 170
SARS-CoV-2 Neutralizing Antibodies for COVID-19 Prevention and Treatment
Li, D., Sempowski, G. D., Saunders, K. O., Acharya, P., & Haynes, B. F. (2021) · Annual Review of Medicine · doi:10.1146/annurev-med-042420-113838 · Cited by 134
Moriyama, S., Adachi, Y., Sato, T., Tonouchi, K., Sun, L., Fukushi, S., Yamada, S., Kinoshita, H., Nojima, K., Kanno, T., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.06.015 · Cited by 140
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Higuchi, Y., Suzuki, T., Arimori, T., Ikemura, N., Mihara, E., Kirita, Y., Ohgitani, E., Mazda, O., Motooka, D., Nakamura, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24013-y · Cited by 129
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Du, L., Yang, Y., & Zhang, X. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00752-2 · Cited by 133
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SARS-CoV-2 in immunocompromised individuals
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Self-citationBeaudoin-Bussières, G., Chen, Y., Ullah, I., Prévost, J., Tolbert, W. D., Symmes, K., Ding, S., Benlarbi, M., Gong, S. Y., Tauzin, A., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110368 · Cited by 122
Guo, Y., Han, J., Zhang, Y., He, J., Yu, W., Zhang, X., Wu, J., Zhang, S., Kong, Y., Guo, Y., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.877101 · Cited by 118
Mackin, S., Desai, P., Whitener, B. M., Karl, C. E., Liu, M., Baric, R. S., Edwards, D. K., Chicz, T. M., McNamara, R. P., Alter, G., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01359-1 · Cited by 123
Self-citationKeeton, R., Richardson, S. I., Moyo-Gwete, T., Hermanus, T., Tincho, M. B., Benede, N., Manamela, N. P., Baguma, R., Makhado, Z., Ngomti, A., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.10.003 · Cited by 109
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Corbett, K. S., Gagné, M., Wagner, D. A., Connell, S. O., Narpala, S., Flebbe, D. R., Andrew, S. F., Davis, R. L., Flynn, B. J., Johnston, T. S., et al. (2021) · Science · doi:10.1126/science.abl8912 · Cited by 98
Körper, S., Weiß, M., Zickler, D., Wiesmann, T., Zacharowski, K. D., Corman, V. M., Grüner, B., Ernst, L., Spieth, P. M., Lepper, P. M., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci152264 · Cited by 97
Bertoglio, F., Fühner, V., Ruschig, M., Heine, P. A., Abassi, L., Klünemann, T., Rand, U., Meier, D., Langreder, N., Steinke, S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109433 · Cited by 98
VanBlargan, L. A., Adams, L. J., Liu, Z., Chen, R. E., Gilchuk, P., Raju, S., Smith, B. K., Zhao, H., Case, J. B., Winkler, E. S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.016 · Cited by 87
Self-citationAsymptomatic and symptomatic SARS-CoV-2 infections elicit polyfunctional antibodies
Dufloo, J., Grzelak, L., Staropoli, I., Madec, Y., Tondeur, L., Anna, F., Pelleau, S., Wiedemann, A., Planchais, C., Buchrieser, J., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100275 · Cited by 89
Fielding, C. A., Sabberwal, P., Williamson, J. C., Greenwood, E. J. D., Crozier, T. W. M., Zelek, W. M., Seow, J., Graham, C., Huettner, I., Edgeworth, J. D., et al. (2022) · eLife · doi:10.7554/elife.74489 · Cited by 87
Protective activity of mRNA vaccines against ancestral and variant SARS-CoV-2 strains
Ying, B., Whitener, B., VanBlargan, L. A., Hassan, A. O., Shrihari, S., Liang, C.-Y., Karl, C. E., Mackin, S., Chen, R. E., Kafai, N. M., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abm3302 · Cited by 85
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Kim, A. S., Kafai, N. M., Winkler, E. S., Gilliland, T. C., Cottle, E. L., Earnest, J. T., Jethva, P. N., Kapłonek, P., Shah, A. P., Fong, R. H., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.006 · Cited by 79
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Pino, M., Abid, T., Ribeiro, S. P., Edara, V. V., Floyd, K. A., Smith, J. C., Latif, M. B., Sánchez, G. P., Dutta, D., Wang, S., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abh3634 · Cited by 77
Bowen, J. E., Park, Y., Stewart, C., Brown, J. T., Sharkey, W. K., Walls, A. C., Joshi, A., Sprouse, K. R., McCallum, M., Tortorici, M. A., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.adf1421 · Cited by 81
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Kapłonek, P., Wang, C., Bartsch, Y. C., Fischinger, S., Gorman, M. J., Bowman, K. A., Kang, J., Dayal, D., Martin, P., Nowak, R. P., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abj2901 · Cited by 77
Case, J. B., Chen, R. E., Cao, L., Ying, B., Winkler, E. S., Johnson, M., Goreshnik, I., Pham, M. N., Shrihari, S., Kafai, N. M., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.008 · Cited by 73
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Richardson, S. I., Manamela, N. P., Motsoeneng, B. M., Kaldine, H., Ayres, F., Makhado, Z., Mennen, M., Skelem, S., Williams, N., Sullivan, N. J., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100510 · Cited by 73
Gagné, M., Corbett, K. S., Flynn, B. J., Foulds, K. E., Wagner, D. A., Andrew, S. F., Todd, J.-P. M., Honeycutt, C. C., McCormick, L., Nurmukhambetova, S. T., et al. (2021) · Cell · doi:10.1016/j.cell.2021.12.002 · Cited by 71
Planchais, C., Fernández, I., Bruel, T., de Melo, G. D., Prot, M., Beretta, M., Guardado‐Calvo, P., Dufloo, J., Molinos-Albert, L. M., Backović, M., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220638 · Cited by 75
Cross-reactive coronavirus antibodies with diverse epitope specificities and Fc effector functions
Shiakolas, A. R., Kramer, K. J., Wrapp, D., Richardson, S. I., Schäfer, A., Wall, S. C., Wang, N., Janowska, K., Pilewski, K. A., Venkat, R., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100313 · Cited by 75
Self-citationSchepens, B., van Schie, L., Nerinckx, W., Roose, K., Breedam, W. V., Fijałkowska, D., Devos, S., Weyts, W., Cae, S. D., Vanmarcke, S., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi7826 · Cited by 66
Chung, D. J., Shah, G. L., Devlin, S. M., Ramanathan, L. V., Doddi, S., Pessin, M. S., Hoover, E., Marcello, L. T., Young, J. C., Boutemine, S. R., et al. (2021) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-21-0139 · Cited by 66
Ko, S., Park, S., Sohn, M. H., Jo, M., Ko, B. J., Na, J., Yoo, H., Jeong, A. L., Ha, K., Woo, J. R., et al. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00870-5 · Cited by 71
King, H. A. D., Joyce, M. G., Lakhal-Naouar, I., Ahmed, A., Cincotta, C. M., Subra, C., Peachman, K. K., Hack, H. R., Chen, R. E., Thomas, P. V., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106433118 · Cited by 65
Self-citationInstructing durable humoral immunity for COVID-19 and other vaccinable diseases
Bhattacharya, D. (2022) · Immunity · doi:10.1016/j.immuni.2022.05.004 · Cited by 64
Gu, X., Wang, S., Zhang, W., Li, C., Guo, L., Wang, Z., Li, H., Zhang, H., Zhou, Y., Liang, W., et al. (2023) · EBioMedicine · doi:10.1016/j.ebiom.2023.104851 · Cited by 68
Francica, J. R., Flynn, B. J., Foulds, K. E., Noe, A. T., Werner, A. P., Moore, I. N., Gagné, M., Johnston, T. S., Tucker, C., Davis, R. L., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi4547 · Cited by 89
Therapeutic monoclonal antibodies for COVID-19 management: an update
Chavda, V. P., Prajapati, R., Lathigara, D., Nagar, B., Kukadiya, J., Redwan, E. M. M. M., Uversky, V. N., Kher, M. N., & Patel, R. (2022) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2022.2078160 · Cited by 74
Wuertz, K. M., Barkei, E. K., Chen, W., Martinez, E. J., Lakhal-Naouar, I., Jagodzinski, L. L., Paquin‐Proulx, D., Gromowski, G. D., Swafford, I., Ganesh, A., et al. (2021) · npj Vaccines · doi:10.1038/s41541-021-00392-7 · Cited by 66
Landscape of human antibody recognition of the SARS-CoV-2 receptor binding domain
Wheatley, A. K., Pymm, P., Esterbauer, R., Dietrich, M. H., Lee, W. S., Drew, D. R., Kelly, H. G., Chan, L., Mordant, F. L., Black, K. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109822 · Cited by 62
BNT162b2 vaccine induces divergent B cell responses to SARS-CoV-2 S1 and S2
Brewer, R. C., Ramadoss, N. S., Lahey, L. J., Jahanbani, S., Robinson, W. H., & Lanz, T. V. (2021) · Nature Immunology · doi:10.1038/s41590-021-01088-9 · Cited by 62
Dussupt, V., Sankhala, R. S., Mendez-Rivera, L., Townsley, S., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G. C., Tran, U., Jackson, N. D., et al. (2021) · Nature Immunology · doi:10.1038/s41590-021-01068-z · Cited by 59
Anti-SARS-CoV-2 antibodies elicited by COVID-19 mRNA vaccine exhibit a unique glycosylation pattern
Farkash, I., Feferman, T., Saban, N. C., Avraham, Y., Morgenstern, D., Mayuni, G., Barth, N., Lustig, Y., Miller, L., Shouval, D. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110114 · Cited by 60
A public antibody class recognizes an S2 epitope exposed on open conformations of SARS-CoV-2 spike
Claireaux, M. A. F., Caniels, T. G., de Gast, M., Han, J., Guerra, D., Kerster, G., van Schaik, B. D. C., Jongejan, A., Schriek, A. I., Grobben, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32232-0 · Cited by 64
Bruel, T., Stéfic, K., Nguyen, Y., Toniutti, D., Staropoli, I., Porrot, F., Guivel‐Benhassine, F., Bolland, W., Planas, D., Hadjadj, J., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100850 · Cited by 62
Andrews, H. S., Herman, J. D., & Gandhi, R. T. (2023) · Annual Review of Medicine · doi:10.1146/annurev-med-052422-020316 · Cited by 64
Gagné, M., Flynn, B. J., Andrew, S. F., Marquez, J., Flebbe, D. R., Mychalowych, A., Lamb, E., Davis-Gardner, M. E., Burnett, M. R., Serebryannyy, L., et al. (2024) · Nature Immunology · doi:10.1038/s41590-024-01951-5 · Cited by 78
Self-citationThe role of micropeptides in biology
Vitorino, R. M. P., Guedes, S. D. M., Amado, F. M. L., Santos, M. A. S., & Akimitsu, N. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03740-3 · Cited by 60
Onodera, T., Kita, S., Adachi, Y., Moriyama, S., Sato, A., Nomura, T., Sakakibara, S., Inoue, T., Tadokoro, T., Anraku, Y., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.025 · Cited by 61
Brunet‐Ratnasingham, E., Anand, S. P., Gantner, P., Dyachenko, A., Moquin‐Beaudry, G., Brassard, N., Beaudoin-Bussières, G., Pagliuzza, A., Gasser, R., Benlarbi, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abj5629 · Cited by 54
High-affinity, neutralizing antibodies to SARS-CoV-2 can be made without T follicular helper cells
Chen, J., Chow, R. D.-W., Song, E., Mao, T., Israelow, B., Kamath, K., Bozekowski, J. D., Haynes, W. A., Filler, R. B., Menasché, B. L., et al. (2022) · Science Immunology · doi:10.1126/sciimmunol.abl5652 · Cited by 52
Xu, Q., Xue, J.-H., Xiao, Y., Jia, Z.-J., Wu, M., Liu, Y., Li, W.-L., Liang, X., & Yang, T. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.786554 · Cited by 53
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 51
Ullah, I., Beaudoin-Bussières, G., Symmes, K., Cloutier, M., Ducas, É., Tauzin, A., Laumaea, A., Grunst, M. W., Dionne, K., Richard, J., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100893 · Cited by 49
Ku, Z., Xie, X., Lin, J., Gao, P., Wu, B., Sahili, A. E., Su, H., Liu, Y., Ye, X., Tan, E. Y. J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33284-y · Cited by 54
Hybrid Immunity Shifts the Fc-Effector Quality of SARS-CoV-2 mRNA Vaccine-Induced Immunity
Bowman, K. A., Stein, D., Shin, S. A., Ferbas, K. G., Tobin, N. H., Mann, C. J., Fischinger, S., Saphire, E. O., Lauffenburger, D. A., Rimoin, A. W., et al. (2022) · mBio · doi:10.1128/mbio.01647-22 · Cited by 49
Engineering ACE2 decoy receptors to combat viral escapability
Arimori, T., Ikemura, N., Okamoto, T., Takagi, J., Standley, D. M., & Hoshino, A. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.06.011 · Cited by 44
Herman, J. D., Wang, C., Loos, C., Yoon, H., Rivera, J., Dieterle, M. E., Haslwanter, D., Jangra, R. K., Bortz, R. H., Bar, K. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27201-y · Cited by 39
SARS-CoV-2 and Influenza A Virus Coinfections in Ferrets
Huang, Y., Skarlupka, A. L., Jang, H., Blas-Machado, U., Holladay, N., Hogan, R. J., & Ross, T. M. (2021) · Journal of Virology · doi:10.1128/jvi.01791-21 · Cited by 43
Self-citationClark, J. J., Hoxie, I., Adelsberg, D. C., Sapse, I. A., Andreata‐Santos, R., Yong, J. S., Amanat, F., Tcheou, J., Raskin, A. J., Singh, G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114922 · Cited by 43
Evolution of Anti-SARS-CoV-2 Therapeutic Antibodies
Almagro, J. C., Mellado‐Sánchez, G., Pedraza‐Escalona, M., & Pérez‐Tapia, S. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179763 · Cited by 40
Metadata
- Authors
- 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., Case, J. B., Sutton, R. E., Carnahan, R. H., Darling, T. L., Boon, A. C. M., Mack, M., Head, R. D., Ross, T. M., Crowe, J. E., & Diamond, M. S.
- Affiliations
- Washington University in St. Louis (US)
- Vanderbilt University Medical Center (US)
- University of Georgia (US)
- University Hospital Regensburg (DE)
- Corresponding author
- Crowe, James E.
- Diamond, Michael S.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 184
- Issue
- 7
- Pages
- 1804-1820.e16
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7879018
- OpenAlex
- W3132982761
- Cited by
- 366
- References
- 101
- Citations by year
- 2026: 13 · 2025: 34 · 2024: 40 · 2023: 69 · 2022: 99 · 2021: 109
- FWCI
- 25.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 365 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- University of Regensburg Publication Server (University of Regensburg) (submittedVersion)
- Funders
- NIAID
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Keywords
- SARS-CoV-2, neutralizing monoclonal antibodies, Fc effector functions, passive immunotherapy, COVID-19 pandemic, pulmonary infection, monocytes, CD8+ T cells, innate immune signaling, tissue repair, inflammation, correlates of protection
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