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Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model
Open accessPublished version of a preprint
Abstract
Protective neutralizing antibodies: Antibodies produced by survivors of coronavirus disease 2019 (COVID-19) may be leveraged to develop therapies. A first step is identifying neutralizing antibodies, which confer strong protection against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Rogers et al. used a high-throughput pipeline to isolate and characterize monoclonal antibodies from convalescent donors. Antibodies were selected for binding to the viral spike protein, which facilitates entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor. Most isolated antibodies bound to regions of the spike outside of the receptor binding domain (RBD); however, a larger proportion of the RBD-binding antibodies were neutralizing, with the most potent binding at a site that overlaps the ACE2 binding site. Two of the neutralizing antibodies were tested in Syrian hamsters and provided protection against SARS-CoV-2 infection. Science , this issue p. 956
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“A polyclonal antibody against multiple epitopes of the S protein beyond the RBD might, for example, inhibit viral attachment156–160, provide additional neutralizing activity161 and/or prevent post-attachment fusion162.”
From Immunological mechanisms of vaccine-induced protection against COVID-19 in humans (2021) · cites this paper as [159]
In the citing paper
“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 [26]
In the citing paper
“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 [26]
In the citing paper
“Although antibodies to the N-terminal domain and other parts of S can also be neutralizing, we limited our analysis to memory B cells that produce anti-RBD antibodies because they are the most numerous and potent18,19.”
From Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection (2021) · cites this paper as [18]
In the citing paper
“passive transfer of nAbs limits respiratory tract infection and protects against infection in animal models (16–20)”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [16]
In the citing paper
“SARS-CoV-2 infection rapidly elicits nAbs (16, 21–24) that decline, but remain detectable, over several months (25–29).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [16]
In the citing paper
“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 [16]
In the citing paper
“Several studies have now shown that authentic virus and pseudovirus neutralization correlate quite well (16, 86, 87).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [16]
In the citing paper
“The neutralizing antibodies are produced by B cells with a wide range of heavy chain and light chain V genes (Robbiani et al., 2020; Rogers et al., 2020). SARS-CoV-2 neutralizing antibodies also exhibit little to no somatic hypermutation (Gaebler et al., 2020; Robbiani et al., 2020; Rogers et al., 2020).”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Rogers et al., 2020
In the citing paper
“passive transfer of neutralizing antibodies in advance of SARS-CoV-2 infection (mimicking the conditions of 2° infection) can effectively prevent or limit URT infection, lung infection, and symptomatic disease in animal models”
From Adaptive immunity to SARS-CoV-2 and COVID-19 (2021) · cites this paper as Rogers et al., 2020
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“Similar to the SARS-CoV S protein that generated neutralizing antibodies in mouse models [55,217], convalescent plasma from recovered SARS-CoV-2 patients contained neutralizing antibodies specific to the S protein (full length S, S1, RBD, and S2) [114,218,219].”
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“Prophylactic and therapeutic efficacy of anti-SmAbs has been demonstrated in vivo in murine, hamster, and non-human primate models of SARS-CoV-2 pathogenesis (Alsoussi et al., 2020; Baum et al., 2020; Fagre et al., 2020; Hansen et al., 2020; Hassan et al., 2020; Kreye et al., 2020; Rogers et al., 2020; Shi et al., 202…”
BackgroundMethodResultInfluentialStructural 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
Self-citationSuryadevara, 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
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
Self-citationEvolution of enhanced innate immune evasion by SARS-CoV-2
Thorne, L., Bouhaddou, M., Reuschl, A., Zuliani‐Alvarez, L., Polacco, B. J., Pelin, A., Batra, J., Whelan, M. V. X., Hosmillo, M. D. T., Fossati, A., et al. (2021) · Nature · doi:10.1038/s41586-021-04352-y · Cited by 451
“E Voss 51 .”
Heinz, F. X., & Stiasny, K. (2021) · npj Vaccines · doi:10.1038/s41541-021-00369-6 · Cited by 378
Ma, X., Zou, F., Yu, F., Li, R., Yuan, Y., Zhang, Y., Zhang, X., Deng, J., Chen, T., Song, Z., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.11.015 · Cited by 336
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166
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
Barton, M. I., MacGowan, S. A., Kutuzov, M. A., Dushek, O., Barton, G. J., & van der Merwe, P. A. (2021) · eLife · doi:10.7554/elife.70658 · Cited by 346
“RBD mutations that abrogate antibody neutralisation, Beta and Gamma, became dominant in regions with very high levels of prior SARS- CoV-2 infection ( Cele et al., 2021 ; Dejnirattisai et al., 2021 ; Hoffmann et al., 2021 ; Sabino et al., 2021 ; Tegally et al., 2021 ; Zhou et al., 2021b ).”
BackgroundHartley, G. E., Edwards, E. S. J., Aui, P. M., Varese, N., Stojanovic, S., McMahon, J., Peleg, A. Y., Boo, I., Drummer, H. E., Hogarth, P. M., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abf8891 · Cited by 296
“Other studies have identified SARS-CoV-2-specific B cells in COVID-19 patients with particular focus on the RBD of the spike protein, mainly for the purpose of cloning neutralizing SARS-CoV-2-specific antibodies ( 4 , 14 , 22 , 47 , 48 ).”
Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy
Zhang, Q., Xiang, R., Huo, S., Zhou, Y., Jiang, S., Wang, Q., & Yu, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00653-w · Cited by 364
In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies
Li, D., Edwards, R. J., Manne, K., Martinez, D. R., Schäfer, A., Alam, S. M., Wiehe, K. J., Lu, X., Parks, R., Sutherland, L. L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.021 · Cited by 337
“, 2020a) or rodent models (Hassan et al., 2020; Rogers et al., 2020; Wu et al., 2020) have protected against SARS-CoV-2 infection.”
BackgroundInfluentialGenetic 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
Crawford, K. H. D., Dingens, A. S., Eguia, R., Wolf, C. R., Wilcox, N., Logue, J. K., Shuey, K., Casto, A. M., Fiala, B., Wrenn, S., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa618 · Cited by 265
SARS-CoV-2 escape in vitro from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451
“The SARS-CoV-2 S-protein is composed of two subunits: S1, which contains the receptor-binding domain (RBD) responsible for the interaction with receptors on the host cells, and S2, which mediates membrane fusion and viral entry (7, 8).”
A human coronavirus evolves antigenically to escape antibody immunity
Eguia, R., Crawford, K. H. D., Stevens-Ayers, T., Kelnhofer-Millevolte, L., Greninger, A. L., Englund, J. A., Boeckh, M. J., & Bloom, J. D. (2020) · doi:10.1101/2020.12.17.423313 · Cited by 258
A human coronavirus evolves antigenically to escape antibody immunity
(2021) · doi:10.1371/journal.ppat.1009453 · Cited by 258
“We synthesized genes encoding all five spikes, truncating the last 19 residues of the cytoplasmic tail since this improves titers of spike-pseudotyped viruses (Crawford et al., 2020a; Kawase et al., 2009; Rogers et al., 2020).”
MethodMuecksch, F., Weisblum, Y., Barnes, C. O., Schmidt, F., Schaefer-Babajew, D. J., Wang, Z., Lorenzi, J. C. C., Flyak, A. I., DeLaitsch, A. T., Huey‐Tubman, K. E., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.07.008 · Cited by 279
“The receptor-binding domains (RBDs) of the SARS-CoV-2 Spike trimer are key neutralization targets, and potent RBDspecific antibodies have been isolated from many convalescent donors (Brouwer et al., 2020; Cao et al., 2020; Chen et al., 2020; Chi et al., 2020; Hansen et al., 2020; Ju et al., 2020; Kreer et al., 2020; R…”
BackgroundNeutralizing 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
SARS-CoV-2 spreads through cell-to-cell transmission
Zeng, C., Evans, J. P., King, T., Zheng, Y.-M., Oltz, E. M., Whelan, S. P. J., Saif, L. J., Peeples, M. E., & Liu, S.-L. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111400119 · Cited by 246
Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models
Cohen, A. A., van Doremalen, N., Greaney, A. J., Andersen, H., Sharma, A., Starr, T. N., Keeffe, J. R., Fan, C., Schulz, J. E., Gnanapragasam, P. N. P., et al. (2022) · Science · doi:10.1126/science.abq0839 · Cited by 264
Broadly neutralizing antibodies target the coronavirus fusion peptide
Dacon, C., Tucker, C., Peng, L., Lee, C.-C. D., Lin, T.-H., Yuan, M., Cong, Y., Wang, L., Purser, L., Williams, J. K., et al. (2022) · Science · doi:10.1126/science.abq3773 · Cited by 250
“Pseudotyped viral neutralization assays were performed similar to a previous report (50).”
Self-citationTrougakos, I. P., Stamatelopoulos, K. S., Terpos, E., Tsitsilonis, O., Aivalioti, E., Paraskevis, D. N., Kastritis, E., Pavlakis, G. N., & Dimopoulos, M. A. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-020-00703-5 · Cited by 305
Prevalent, protective, and convergent IgG recognition of SARS-CoV-2 non-RBD spike epitopes
Voss, W. N., Hou, Y. J., Johnson, N. V., Delidakis, G., Kim, J. E., Javanmardi, K., Horton, A. P., Bartzoka, F., Paresi, C., Tanno, Y., et al. (2021) · Science · doi:10.1126/science.abg5268 · Cited by 255
Treatment of influenza and SARS-CoV-2 infections via mRNA-encoded Cas13a in rodents
Blanchard, E. L., Vanover, D. A., Bawage, S. S., Tiwari, P. M., Rotolo, L., Beyersdorf, J. P., Peck, H. E., Bruno, N. C., Hincapie, R., Michel, F. J., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00822-w · Cited by 244
Monoclonal antibodies for COVID-19 therapy and SARS-CoV-2 detection
Hwang, Y., Lu, R., Su, S.-C., Chiang, P.-Y., Ko, S.-H., Ke, F.-Y., Liang, K.-H., Hsieh, T.-Y., & Wu, H. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-021-00784-w · Cited by 247
“The major strategy used for rapid isolation of high-efficacy nAbs is reverse transcriptase-polymerase chain reaction (RT-PCR) from single human B cells [38, 39].”
MethodExtremely potent human monoclonal antibodies from COVID-19 convalescent patients
Andreano, E., Nicastri, E., Paciello, I., Pileri, P., Manganaro, N., Piccini, G., Manenti, A., Pantano, E., Kabanova, A., Troisi, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.035 · Cited by 199
“This model has shown to manifest severe forms of SARS-CoV-2 infection mimicking more closely the clinical disease observed in humans (Baum et al., 2020; Imai et al., 2020; Rogers et al., 2020; Sia et al., 2020).”
InfluentialStructural basis for broad coronavirus neutralization
Sauer, M. M., Tortorici, M. A., Park, Y., Walls, A. C., Homad, L. J., Acton, O. J., Bowen, J. E., Wang, C., Xiong, X., de van der Schueren, W., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00596-4 · Cited by 175
High genetic barrier to SARS-CoV-2 polyclonal neutralizing antibody escape
Schmidt, F., Weisblum, Y., Rutkowska, M., Poston, D., DaSilva, J., Zhang, F., Bednarski, E., Cho, A., Schaefer-Babajew, D. J., Gaebler, C., et al. (2021) · Nature · doi:10.1038/s41586-021-04005-0 · Cited by 216
de Alwis, R., Gan, E. S., Chen, S., Leong, Y. S., Tan, H. C., Zhang, S. L., Yau, C., Low, J. G. H., Kalimuddin, S., Matsuda, D., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.04.001 · Cited by 191
“Notably, IgG that bind the RBD of S 219 protein, which is an immunodominant site of neutralizing antibodies [26, 27], were also 220 higher in LUNAR-COV19 compared to conventional mRNA vaccinated animals.”
ResultThe effect of spike mutations on SARS-CoV-2 neutralization
Rees-Spear, C., Muir, L., Griffith, S. A., Heaney, J., Aldon, Y., Snitselaar, J. L., Thomas, P., Graham, C., Seow, J., Lee, N., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108890 · Cited by 221
“…HEK293T/17 cells American Type Culture Collection ATCC CRL-11268 Human: HeLa-ACE-2 cells James Voss Laboratory, The Scripps Research Institute; Rogers et al., 2020 N/A Oligonucleotides 50-agcaatttcagagtgcagcctaccgGg GAcatcgtgagattccctaatatcacc-30 ES324-6GD Forward…”
Kuzmina, A., Khalaila, Y., Voloshin, O., Keren‐Naus, A., Cohen, L. B., Raviv, Y., Shemer‐Avni, Y., Rosenberg, E., & Taube, R. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.008 · Cited by 177
“These are elicited by prior infection or vaccination, and inhibit SARS-CoV-2-ACE2 engagement and viral entry, and are thus likely to be key for future protection against SARS-CoV-2 (Alsoussi et al., 2020; Brouwer et al., 2020; Gaebler et al., 2021; ACTIV-3/TICO LY-CoV555 Study Group, 2021; Klasse and Sattentau, 2002;…”
BackgroundSARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103154118 · Cited by 429
Wang, C., van Haperen, R., Gutierrez-Alvarez, F. J., Li, W., Okba, N. M. A., Albulescu, I. C., Widjaja, I., van Dieren, B., Fernández‐Delgado, R., Sola, I., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21968-w · Cited by 178
Walls, A. C., Miranda, M. C., Schäfer, A., Pham, M. N., Greaney, A., Arunachalam, P. S., Navarro, M.-J., Tortorici, M. A., Rogers, K., O’Connor, M. A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.015 · Cited by 185
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
BackgroundGerminal center responses to SARS-CoV-2 mRNA vaccines in healthy and immunocompromised individuals
Lederer, K., Parvathaneni, K., Painter, M. M., Bettini, E., Agarwal, D., Lundgreen, K. A., Weirick, M., Goel, R. R., Xu, X., Drapeau, E. M., et al. (2021) · doi:10.1101/2021.09.16.21263686 · Cited by 179
“SARS-CoV-2-specific Abs, including nAbs, play a key role in the protection against COVID-19, in animal models (McMahan et al., 2021; Rogers et al., 2020; Zost et al., 2020) and humans (Bergwerk et al., 2021; Earle et al., 2021; Khoury et al., 2021; Lumley et al., 2021).”
Anand, S. P., Prévost, J., Nayrac, M., Beaudoin-Bussières, G., Benlarbi, M., Gasser, R., Brassard, N., Laumaea, A., Gong, S. Y., Bourassa, C., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100290 · Cited by 174
“preventing infection in animal models (10, 23, 24).”
Immunogenicity of Pfizer-BioNTech COVID-19 vaccine in patients with inborn errors of immunity
Hagin, D., Freund, T., Navon, M., Halperin, T., Adir, D., Marom, R., Levi, I., Benor, S., Alcalay, Y., & Freund, N. T. (2021) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2021.05.029 · Cited by 174
SARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms
Clark, S. A., Clark, L. E., Pan, J., Coscia, A., McKay, L. G. A., Shankar, S., Johnson, R. I., Brusic, V., Choudhary, M. C., Regan, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.027 · Cited by 193
Prolonged 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
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
Circulating ACE2-expressing extracellular vesicles block broad strains of SARS-CoV-2
El-Shennawy, L., Hoffmann, A. D., Dashzeveg, N. K., McAndrews, K. M., Mehl, P. J., Cornish, D., Yu, Z., Tokars, V. L., Nicolaescu, V. I., Τοματσίδου, Α., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27893-2 · Cited by 197
Song, G., He, W., Callaghan, S., Anzanello, F., Huang, D., Ricketts, J., Torres, J. L., Beutler, N., Peng, L., Vargas, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23074-3 · Cited by 277
Self-citationAntibody neutralization of SARS-CoV-2 through ACE2 receptor mimicry
Ge, J., Wang, R., Ju, B., Zhang, Q., Sun, J., Chen, P., Zhang, S., Tian, Y., Shan, S., Cheng, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20501-9 · Cited by 149
Antibody titers against SARS-CoV-2 decline, but do not disappear for several months
Yamayoshi, S., Yasuhara, A., Ito, M., Akasaka, O., Nakamura, M., Nakachi, I., Koga, M., Mitamura, K., Yagi, K., Maeda, K., et al. (2021) · EClinicalMedicine · doi:10.1016/j.eclinm.2021.100734 · Cited by 151
“Numerous studies involving COVID-19 patients and animal models have been conducted all over the world, and the induction of neutralizing antibodies by infection and vaccination and the ef fi cacy of monoclonal antibody, serum, or plasma therapies have been reported [12,29,45].”
Kinetics and correlates of the neutralizing antibody response to SARS-CoV-2 infection in humans
Vanshylla, K., Di Cristanziano, V., Kleipass, F., Dewald, F., Schommers, P., Gieselmann, L., Gruell, H., Schlotz, M., Ercanoglu, M. S., Stumpf, R., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.015 · Cited by 153
Ullah, 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
“In agreement with the previous smFRET data for S006 plasma, CV3-1 stabilized S in the RBD-up ( 0.1 FRET) conformation (Figures 3F–3H), as seen with hACE2 and most RBD-directed NAbs (Lu et al., 2020).”
BackgroundInfluential
Metadata
- Authors
- Rogers, T. F., Zhao, F., Huang, D., Beutler, N., Burns, A., He, W.-T., Limbo, O., Smith, C., Song, G., Woehl, J., Yang, L., Abbott, R. K., Callaghan, S., Garcia, E., Hurtado, J., Parren, M., Peng, L., Ramirez, S., Ricketts, J., Ricciardi, M. J., Rawlings, S. A., Wu, N. C., Yuan, M., Smith, D. M., Nemazee, D., Teijaro, J. R., Voss, J. E., Wilson, I. A., Andrabi, R., Briney, B., Landais, E., Sok, D., Jardine, J. G., & Burton, D. R.
- Affiliations
- Scripps Research Institute (US)
- Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
- La Jolla Institute for Immunology (US)
- George Washington University (US)
- University of California San Diego (US)
- Corresponding author
- Rogers, Thomas F.
- Zhao, Fangzhu
- Huang, Deli
- Beutler, Nathan
- Sok, Devin
- Jardine, Joseph G.
- Burton, Dennis R.
- ORCID
- Rogers, Thomas F.
- Zhao, Fangzhu
- Huang, Deli
- Beutler, Nathan
- Burns, Alison
- He, Wan-ting
- Limbo, Oliver
- Smith, Chloe
- Song, Ge
- Woehl, Jordan
- Yang, Linlin
- Abbott, Robert K.
- Callaghan, Sean
- Garcia, Elijah
- Hurtado, Jonathan
- Parren, Mara
- Peng, Linghang
- Ramirez, Sydney
- Ricketts, James
- Ricciardi, Michael J.
- Rawlings, Stephen A.
- Wu, Nicholas C.
- Yuan, Meng
- Smith, Davey M.
- Nemazee, David
- Teijaro, John R.
- Voss, James E.
- Wilson, Ian A.
- Andrabi, Raiees
- Briney, Bryan
- Landais, Elise
- Sok, Devin
- Jardine, Joseph G.
- Burton, Dennis R.
- Venue
- Science
- Published
- 2020-08-21
- Volume
- 369
- Issue
- 6506
- Pages
- 956-963
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC7299280
- OpenAlex
- W3035459690
- Cited by
- 1,230
- References
- 33
- Citations by year
- 2026: 23 · 2025: 47 · 2024: 68 · 2023: 126 · 2022: 242 · 2021: 504 · 2020: 217
- FWCI
- 35.77
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (UM1 AI144462)
- Bill and Melinda Gates Foundation (OPP 1170236, OPP 1206647, OPP1196345)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2, neutralizing antibodies, COVID-19 pandemic, receptor binding domain, spike protein epitopes, passive antibody transfer, Syrian hamster model, antibody isolation, high-throughput antibody screening, prophylaxis, vaccine design, lung viral titers
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