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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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“Most of the NAbs target RBD [14,15], and partial antigen epitopes in other domains of the S protein may even cause the antibody-dependent effects (ADEs) [16].”
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“The RBD-pep2 is part of the RBM which in general, is very flexible and adopts a structure when binds to the ACE2 receptor (Figure 6B).”
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“4 also known as conventional virus neutralization tests (cVNTs), measure SARS-CoV-2 neutralizing antibody titer and involve the use of live pathogens and target cells (6,7).”
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“Currently, most of the discovered nAbs target the RBD [4,5] and NTD [4,6], in contrast to a small number of nAbs target the S2 subunit [6].”
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“Neutralizing antibodies typically recognize spatial epitopes located in specific regions of viral surface proteins that are involved in the initial interaction with host cells [22,23].”
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“With few exceptions, the results concur, showing that a limited number of B clones drive the humoral immune response [56–58] and that patients often share heavy (VH) and light (VL) variable gene classes [58,59].”
ResultEmerging variants develop total escape from potent monoclonal antibodies induced by BA.4/5 infection
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Next-generation treatments: Immunotherapy and advanced therapies for COVID-19
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“Similarly, we found that at the mucosal lung level, neutralizing antibodies decreased over time but over a longer period compared with blood (78, 79).”
BackgroundBhattacharya, M., Chatterjee, S., Mallik, B., Sharma, A. R., & Chakraborty, C. (2022) · Vaccines · doi:10.3390/vaccines10101612 · Cited by 16
Chaturvedi, S., Beutler, N., Vasen, G., Pablo, M., Chen, X., Calia, G., Buie, L., Rodick, R., Smith, D. M., Rogers, T. F., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2204624119 · Cited by 22
“2) in 100 μL of DMEM, as described (35).”
MethodSelf-citationScreening and Characterization of Shark-Derived VNARs against SARS-CoV-2 Spike RBD Protein
Chen, Y., Lin, J.-J., Ma, H., Zhong, N., Xie, X.-X., Yang, Y., Zheng, P., Zhang, L., Jin, T., & Cao, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810904 · Cited by 18
“20 nM, respectively, even higher than the affinity of some mAbs isolated from lymphocytes of convalescent COVID-19 patients [24,49,50].”
BackgroundWieczorek, L., Zemil, M., Merbah, M., Dussupt, V., Kavusak, E., Molnar, S., Heller, J., Beckman, B., Wollen-Roberts, S. E., Peachman, K. K., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.901217 · Cited by 16
Garrido, J. L. V., Medina, M. A., Bravo, F., McGee, S., Fuentes‐Villalobos, F., Calvo, M. A., Pinos, Y., Bowman, J. W., Bahl, C. D., Barría, M. I., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110904 · Cited by 13
“Importantly, several studies have shown that Abs targeting the RBD region mediate potent neutralization of SARS-CoV-2 in vitro and in vivo (Rogers et al., 2020; Wang et al., 2020b; Wec et al., 2020; Zost et al., 2020).”
InfluentialAnti-SARS-CoV-2 equine F (Ab′)2 immunoglobulin as a possible therapy for COVID-19
Botosso, V., Jorge, S., Astray, R., Guimarães, A. M. D. S., Mathor, M., dos Santos, D. C. P., Durigon, E., Covas, D., de Oliveira, D. B. D., Oliveira, R. D. N., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-07793-1 · Cited by 15
Clark, N. M., Janaka, S. K., Hartman, W. R., Stramer, S. L., Goodhue, E., Weiss, J., Evans, D. T., & Connor, J. P. (2022) · PLoS ONE · doi:10.1371/journal.pone.0257930 · Cited by 23
Choteau, M., Scohy, A., Messe, S., Luyckx, M., Dechamps, M., Montiel, V., Yombi, J. C., Gruson, D., Limaye, N., Michiels, T., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-06038-5 · Cited by 19
Tawinprai, K., Siripongboonsitti, T., Porntharukchareon, T., Dechates, B., Harnphadungkit, M., Sornsamdang, G., Wittayasak, K., Soonklang, K., & Mahanonda, N. (2022) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2022.2035573 · Cited by 13
“Antibodies targeting the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 can potently neutralize the virus.(2) The ChAdOx1 (AZD1222) vaccine developed by Oxford University and AstraZeneca Biopharmaceuticals consists of a replication-deficit simian adenoviral vector containing the full-length DNA seque…”
BackgroundUkey, R., Bruiners, N., Mishra, H. K., Mishra, P. K., McCloskey, D., Onyuka, A., Chen, F., Pinter, A., Weiskopf, D., Sette, A., et al. (2022) · BMC Medicine · doi:10.1186/s12916-022-02252-0 · Cited by 16
“Vero E6 were obtained from the American Type Culture Collection (ATCC), Manassas, USA; HeLa cells stably expressing ACE2 (HeLa-ACE2) were obtained from Dennis Burton at the Scripps Research Institute [8].”
Margolin, E., Verbeek, M., de Moor, W. R. J., Chapman, R., Meyers, A., Schäfer, G., Williamson, A., & Rybicki, E. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2021.798822 · Cited by 15
“The gene sequence was cloned into pEAQ-HT, using AgeI and XhoI, for expression in plants (Sainsbury et al., 2009).”
MethodMuir, L., Jaffer, A., Rees-Spear, C., Gopalan, V., Chang, F. Y., Fernando, R., Vaitkute, G., Roustan, C., Rosa, A., Earl, C. P., et al. (2021) · Kidney International Reports · doi:10.1016/j.ekir.2021.03.902 · Cited by 15
VanBlargan, L. A., Adams, L., Liu, Z.-M., Chen, R. E., Gilchuk, P., Raju, S., Smith, B. K., Zhao, H.-Y., Case, J., Winkler, E. S., et al. (2021) · bioRxiv · doi:10.1101/2021.04.26.441501 · Cited by 15
Rubio-Acero, R., Castelletti, N., Fingerle, V., Olbich, L., Bakuli, A., Woelfel, R., Girl, P., Mueller, K., Jochum, S., Strobl, M., et al. (2021) · medRxiv · doi:10.1101/2021.02.19.21252080 · Cited by 15
The development of neutralizing antibodies against SARS-CoV-2 and their common features
Liu, L. D., Lian, C., Yeap, L.-S., & Meng, F. (2020) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjaa070 · Cited by 14
Immunopathology, host-virus genome interactions, and effective vaccine development in SARS-CoV-2
Singh, D. D., Han, I., Choi, E. H., & Yadav, D. K. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.11.011 · Cited by 14
de Mattos Barbosa, M. G., Liu, H., Huynh, D., Shelley, G., Keller, E. T., Emmer, B. T., Sherman, E., Ginsburg, D., Kennedy, A. A., Tai, A. W., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.147386 · Cited by 14
Kirk, N. M., Liang, Y., & Ly, H. (2024) · Virulence · doi:10.1080/21505594.2024.2316438 · Cited by 13
Kim, I., Lee, Y.-H., Khalid, M., Chen, I. P., Zhang, Y.-N., Ott, M., & Verdin, E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104955 · Cited by 14
“In accordance with the previous literature (34), Spike forms with the deletion of the cytoplasmic tail were used for comparative studies between SARS-CoV – and SARS-CoV-2 – derived Spikes and for studies using SARS-CoV-2 pseudo-typed viruses.”
Chernyshev, M., Sakharkar, M., Connor, R. I., Dugan, H. L., Sheward, D. J., Rappazzo, C. G., Stålmarck, A., Forsell, M. N. E., Wright, P. F., Corcoran, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37972-1 · Cited by 17
Hurtado, J., Rogers, T., Jaffe, D., Adams, B. A., Bangaru, S., Garcia, E., Capozzola, T., Messmer, T., Sharma, P., Song, G., et al. (2023) · bioRxiv · doi:10.1101/2023.03.28.534602 · Cited by 14
“Neutralizing Abs (nAbs) have been reported against each of these regions [13,14], with the broadest nAbs targeting epitopes in S2 [15–19] or the RBD [20,21].”
Self-citationSARS-CoV-2 Establishes a Productive Infection in Hepatoma and Glioblastoma Multiforme Cell Lines
Smirnova, O., Ivanova, O., Fedyakina, I., Yusubalieva, G., Baklaushev, V., Yanvarev, D., Kechko, O., Mitkevich, V., Vorobyev, P., Fedorov, V., et al. (2023) · Cancers · doi:10.3390/cancers15030632 · Cited by 14
Dormeshkin, D., Shapira, M., Dubovik, S., Kavaleuski, A., Katsin, M., Migas, A., Meleshko, A., & Semyonov, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.965446 · Cited by 14
Lee, H.-J., Jung, J. H., Lee, J. H., Lee, D., Kim, Y. B., & Oh, E. (2022) · Viruses · doi:10.3390/v14050946 · Cited by 15
SARS-CoV-2 spike variants differ in their allosteric responses to linoleic acid
Oliveira, A. S. F., Shoemark, D. K., Davidson, A. D., Berger, I., Schaffitzel, C., & Mulholland, A. J. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad021 · Cited by 18
“The RBM contains the residues that directly interact with the host ACE2 receptor ( Lan et al., 2020 ; Wrapp et al., 2020 ) and is a known target for neutralizing antibodies ( Robbiani et al., 2020 ; Rogers et al., 2020 ; Wec et al., 2020 ) .”
BackgroundLi, R., Mor, M., Ma, B., Clark, A. E., Alter, J., Werbner, M., Lee, J. C., Leibel, S. L., Carlin, A. F., Dessau, M., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03739-5 · Cited by 25
van der Straten, K., van Gils, M. J., de Taeye, S. W., & de Bree, G. J. (2022) · Frontiers in Medical Technology · doi:10.3389/fmedt.2022.867982 · Cited by 17
“SARS-CoV-2 challenge studies in animals revealed that the neutralization potency of antibodies correlates with protection against COVID-19 (15, 16).”
BackgroundSARS-CoV-2 and Coronavirus Disease Mitigation: Treatment Options, Vaccinations and Variants
Khamees, A., Bani-Issa, J., Zoubi, M. S. A., Qasem, T., Alarjah, M. I. A., Alawadin, S. A., Al‐Shami, K., Hussein, F. H., Hussein, E. I., Bashayreh, I. H., et al. (2022) · Pathogens · doi:10.3390/pathogens11020275 · Cited by 19
Cheng, Z. J., Li, B., Zhan, Z., Zhao, Z., Xue, M., Zheng, P., Lyu, J., Hu, C., He, J., Chen, R., et al. (2022) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-021-08912-y · Cited by 15
“[39] found that although viral infection induces a strong immune response against the non-RBD regions of the S protein, only a small part of this response is neutralizing.”
BackgroundZhao, F., Keating, C., Ozorowski, G., Shaabani, N., Francino-Urdaniz, I. M., Barman, S., Limbo, O., Burns, A., Zhou, P.-P., Ricciardi, M. J., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104914 · Cited by 14
Self-citationColwill, K., Galipeau, Y., Stuible, M., Gervais, C., Arnold, C., Rathod, B., Abe, K., Wang, J. H., Pasculescu, A., Maltseva, M., et al. (2021) · medRxiv · doi:10.1101/2021.10.25.21265476 · Cited by 14
“Adding the spike RBD as a third antigen increases specificity [of the three antigens, it is the least conserved in coronaviruses (32-34)] and provides insight into possible protection, as it is also the antigen most correlated with neutralization potential (13, 35, 36).”
BackgroundBubonja‐Šonje, M., Batičić, L., Abram, M., & Grbeša, Đ. C. (2021) · Journal of Virological Methods · doi:10.1016/j.jviromet.2021.114173 · Cited by 14
Kanji, J. N., Bailey, A., Fenton, J., Ling, S. H., Rivera, R., Plitt, S. S., Sligl, W., Taylor, S. C., Turnbull, L., Tipples, G. A., et al. (2021) · Vaccine · doi:10.1016/j.vaccine.2021.08.022 · Cited by 13
Zhang, Y.-N., Paynter, J., Sou, C., Fourfouris, T., Wang, Y., Abraham, C., Ngo, T. A., Zhang, Y., He, L.-L., & Zhu, J. (2021) · bioRxiv · doi:10.1101/2021.03.26.437274 · Cited by 14
Wang, D., Ge, Y., Zhong, B., & Liu, D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.03.021 · Cited by 15
Immune responses in COVID-19 patients: Insights into cytokine storms and adaptive immunity kinetics
Zhang, J. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34577 · Cited by 13
“The neutralizing antibodies, developed by B cells with a diversity of heavy and light chain variable (V) genes [86,87], tend to be readily produced against SARS-CoV-2 as they require minimal to no affinity maturation [88].”
BackgroundChi, X., Xia, L., Zhang, G., Chi, X., Huang, B., Zhang, Y., Chen, Z., Han, J., Wu, L., Li, Z., et al. (2023) · Cell Discovery · doi:10.1038/s41421-023-00535-1 · Cited by 16
Humoral immunity for durable control of SARS-CoV-2 and its variants
Kotaki, R., Moriyama, S., & Takahashi, Y. (2023) · Inflammation and Regeneration · doi:10.1186/s41232-023-00255-9 · Cited by 15
Jugler, C., Sun, H., Grill, F. J., Kibler, K. V., Esqueda, A., Lai, H., Li, Y., Lake, D. F., & Chen, Q. (2022) · Vaccines · doi:10.3390/vaccines10050772 · Cited by 16
Potent Anti‐SARS‐CoV‐2 Efficacy of COVID‐19 Hyperimmune Globulin from Vaccine‐Immunized Plasma
Yu, D., Li, Y., Hong, L., Wu, J., Hu, Y., Peng, Y., Li, T., Hou, J., Huang, W., Guan, L., et al. (2022) · Advanced Science · doi:10.1002/advs.202104333 · Cited by 11
Hancock, T. J., Hickman, P. G., Kazerooni, N., Kennedy, M. A., Kania, S. A., Dennis, M. M., Szafranski, N., Gerhold, R. W., Su, C., Masi, T. J., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00250-22 · Cited by 20
Zhou, P.-P., Song, G., He, W.-T., Beutler, N., Tse, L.-P. V., Martinez, D. R., Schäfer, A., Anzanello, F., Yong, P., Peng, L., et al. (2022) · bioRxiv · doi:10.1101/2022.03.04.479488 · Cited by 13
Self-citationHingankar, N. K., Deshpande, S., Das, P., Rizvi, Z. A., Wibmer, C. K., Mashilo, P., Ansari, M. Y., Burns, A., Barman, S., Zhao, F., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010465 · Cited by 14
“We therefore utilized RBD as antigen bait to rapidly isolate antiSARS-CoV-2 mAbs using single B cell FACS sorting method as described previously [20].”
BackgroundMethodResultInfluentialSelf-citationExperimental Models for SARS-CoV-2 Infection
Kim, T., Lee, J. S., & Ju, Y. S. (2021) · Molecules and Cells · doi:10.14348/molcells.2021.0094 · Cited by 13
“Due to their small size and cost-effectiveness, antiviral agents and other potential therapeutic agents were tested in hamsters (Driouich et al., 2021; Kaptein et al., 2020; Rogers et al., 2020).”
BackgroundZhao, F.-Z., Yuan, M., Keating, C., Shaabani, N., Limbo, O., Joyce, C., Woehl, J., Barman, S., Burns, A., Zhu, X.-Y., et al. (2021) · bioRxiv · doi:10.1101/2021.05.29.443900 · Cited by 13
Self-citationWatashi, K. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.094 · Cited by 17
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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