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Measuring immunity to SARS-CoV-2 infection: comparing assays and animal models
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The rapid scale-up of research on coronavirus disease 2019 (COVID-19) has spawned a large number of potential vaccines and immunotherapies, accompanied by a commensurately large number of in vitro assays and in vivo models to measure their effectiveness. These assays broadly have the same end-goal - to predict the clinical efficacy of prophylactic and therapeutic interventions in humans. However, the apparent potency of different interventions can vary considerably between assays and animal models, leading to very different predictions of clinical efficacy. Complete harmonization of experimental methods may be intractable at the current pace of research. However, here we analyse a selection of existing assays for measuring antibody-mediated virus neutralization and animal models of infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and provide a framework for comparing results between studies and reconciling observed differences in the effects of interventions. Finally, we propose how we might optimize these assays for better comparison of results from in vitro and animal studies to accelerate progress.
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“although animal models may not recapitulate all of the features of human infection49, they suggest the importance of looking beyond neutralizing antibodies for additional mechanisms of immune protection.”
From Prospects for durable immune control of SARS-CoV-2 and prevention of reinfection (2021) · cites this paper as [49]
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“We focused primarily on assays using live SARS-CoV-2 virus (to reduce the potential variability that might arise from different pseudoviral constructs23), with the exception of the NVX-CoV2373 vaccine, for which only data from neutralisation assays using a spike-expressing pseudovirus were available.”
From Neutralising antibody titres as predictors of protection against SARS-CoV-2 variants and the impact of boosting: a meta-analysis (2022) · cites this paper as [23]
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ResultSelf-citationAntibody-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
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Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
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Self-citationImmunogenicity of clinically relevant SARS-CoV-2 vaccines in nonhuman primates and humans
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“of the virus preparation, the cell line used, the size of the virus inoculum, and the duration and means of quantifying virus entry into cells (60, 61).”
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Advances in Neutralization Assays for SARS‐CoV‐2
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“…moment only the direct observation and quantification of a SARS-CoV-2 variant spread [29] together with relatively “slow/controversial” in vitro binding assays [30] provide clues about the transmissibility [27] or virulence/pathogenicity [28] of new variants, when the virus is already circulating.”
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“The replication dynamics of pseudoviruses may also deviate from native SARS-CoV-2.(49) Molecular diagnostics for SARS-CoV-2 can also rely on use of antibodies specific to viral antigens.”
InfluentialA point-of-care lateral flow assay for neutralising antibodies against SARS-CoV-2
Fulford, T. S., Văn, H. T., Gherardin, N. A., Zheng, S., Ciula, M., Drummer, H. E., Redmond, S. J., Tan, H., Boo, I., Li, F., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103729 · Cited by 47
“Neutralising antibodies are emerging as a strong correlate of protection [6,7] but are only a subset of the total polyclonal response.”
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“This highlights the need for standardized neutralization assays and reference sera [22].”
BackgroundSimultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay
López, E., Haycroft, E. R., Adair, A., Mordant, F. L., O’Neill, M. T., Pymm, P., Redmond, S. J., Lee, W. S., Gherardin, N. A., Wheatley, A. K., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.150012 · Cited by 38
“108 At present, there is no standardized method for assessing the antibody109 mediated neutralization of SARS-CoV-2, which can account for variation in between 110 studies (30).”
MethodSelf-citationWang, K., Cao, Y., Zhou, Y., Wu, J., Jia, Z., Hu, Y., Yisimayi, A., Fu, W., Wang, L., Liu, P., et al. (2021) · medRxiv · doi:10.1101/2021.09.02.21261735 · Cited by 39
SARS-CoV-2 remodels the Golgi apparatus to facilitate viral assembly and secretion
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“…reading frames ORF1a and ORF1b, are self-processed into 16 individual non-structural proteins (nsps), which modulate the endoplasmic reticulum (ER) to form double-membrane vesicles (DMVs) where the viral replication and transcription complex (RTC) is anchored to produce abundant viral RNAs [4].”
Predicting unseen antibodies’ neutralizability via adaptive graph neural networks
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“The conventional experiments include phage display 5 , enzyme-linked immunosorbent assay (ELISA) 6 , pseudovirus assay 7 and so on, which are resource intensive and time consuming 8 .”
MethodWhat level of neutralising antibody protects from COVID-19?
Khoury, D. S., Cromer, D., Reynaldi, A., Schlub, T. E., Wheatley, A. K., Juno, J. A., Subbarao, K., Kent, S. J., Triccas, J. A., & Davenport, M. P. (2021) · doi:10.1101/2021.03.09.21252641 · Cited by 3,742
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“Inherent differences between the pseudotyped viruses and authentic, replicationcompetent SARS-CoV-2 viruses, such as spike density and geometry on the virion surface, may also result in differences in sensitivity.(29,30) However, neutralization titers from pseudovirus and replication-competent SARS-CoV-2 assays genera…”
Protection Duration of COVID-19 Vaccines: Waning Effectiveness and Future Perspective
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COVID-19 Research: Lessons from Non-Human Primate Models
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“In this regard, a better rationalization and harmonization of preclinical assays in terms of inoculum size, viral isolate, routes of administration, standardization of assays to evaluate antiviral effect and correlates of protection, for instance, could certainly accelerate research and limit the number of inconclusiv…”
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“of a humoral response against specific viral variants (47).”
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“pseudovirus neutralizing assays often involve longer periods of coincubation between the virus and patient sera, which may provide ample time for lower-affinity/avidity antibodies to engage their target (16).”
BackgroundThe role of pseudotype neutralization assays in understanding SARS CoV-2
Cantoni, D. M., Neto, M. M., & Temperton, N. J. (2021) · Oxford Open Immunology · doi:10.1093/oxfimm/iqab005 · Cited by 27
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“Cross-immunity can be detected using in vitro studies (Adams et al., 2006; Khoury et al., 2020) by determiningwhether antibodies are able to prevent the virus from binding to human protein, but these results are difficult to verify in vivo.”
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“The key assumptions underlying NAb kinetics are the following: NAbs grow linearly until they reach their peak after three weeks and then follow a two-part exponential decay, with a 100-day half-life in the first 250 days and an exponentially decaying decay rate until a 10-year half-life is achieved [31,53].”
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“Several reviews succinctly compare the advantages and disadvantages of different animal models [19,20].”
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“Low dose challenge models for SARS-CoV-2 have not yet been systematically developed [26].”
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Multiple sclerosis in the era of COVID-19: disease course, DMTs and SARS-CoV2 vaccinations
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“In line with results from the RSV mRNA-1345 phase 1 study, vaccination signi fi cantly boosted RSV-A and RSV-B nAbs, with a higher GMT observed against RSV-A, which may be due to assay differences (26, 27, 30, 31).”
Fc engineered ACE2-Fc is a potent multifunctional agent targeting SARS-CoV2
Wines, B. D., Kurtovic, L., Trist, H. M., Esparon, S. E., López, E., Chappin, K., Chan, L., Mordant, F. L., Lee, W. S., Gherardin, N. A., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.889372 · Cited by 15
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“The development and implementation of immunoassays is a route of significant interest for increasing the accuracy and reliability of quantitative tests that measure neutralizing antibodies [31].”
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“A viable alternative is the use of pseudo-typed, non-replicative viral particles [8].”
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“However, the lack of a standardised in vitro neutralisation assayremains a signi fi cant impediment to the ongoing comparisons of immunity following vaccination and infection 48,49 .”
Self-citationQuantitation of SARS-CoV-2 neutralizing antibodies with a virus-free, authentic test
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Using in vivo animal models for studying SARS-CoV-2
da Costa, C. B. P., Cruz, A. C. D. M., Penha, J. C. Q., Castro, H. C., da Cunha, L. E. R., Ratcliffe, N. A., Cisne, R., & Martins, F. J. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.1995352 · Cited by 11
“Ferrets were able to transmit the virus through direct contact with other animals or by indirect contact [8,16,42,62].”
BackgroundDevelopment of a Rapid Live SARS-CoV-2 Neutralization Assay Based on a qPCR Readout
Lichtenegger, S., Saiger, S., Hardt, M., Kulnik, S., Wagner, G. E., Kleinhappl, B., Assig, K., Zauner, A., Ober, M., Kimpel, J., et al. (2022) · Journal of Clinical Microbiology · doi:10.1128/jcm.00376-22 · Cited by 11
“protein epitopes and cannot detect antibodies targeting other viral proteins (27).”
BackgroundYounes, N., Al‐Sadeq, D. W., Shurrab, F. M., Zedan, H. T., Abou-Saleh, H., Halawa, B. Y. A., AlHamaydeh, F. M., Elsharafi, A. E., Daas, H. I., Thomas, S., et al. (2022) · Vaccines · doi:10.3390/vaccines10081318 · Cited by 9
“Therefore, neutralization assays remain the gold standard for measuring the nAbs titer against SARS-CoV-2 [9].”
BackgroundOrganotypic human ex vivo models for coronavirus disease 2019 research and drug development
Youhanna, S. C., Wright, S. C., & Lauschke, V. M. (2021) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2021.04.006 · Cited by 10
Tao, K., Tzou, P. L., Pond, S. L. K., Ioannidis, J. P. A., & Shafer, R. W. (2022) · Preprints.org · doi:10.20944/preprints202203.0155.v1 · Cited by 9
Standardized Two-Step Testing of Antibody Activity in COVID-19 Convalescent Plasma
Gilchuk, P., Thomsen, I. P., Yoder, S. M., Brady, E. J., Chappell, J. D., Stevens, L. J., Denison, M. R., Sutton, R. E., Chen, R. E., VanBlargan, L. A., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103602 · Cited by 7
“Infection is measured by quantifying either the number of infected cells, signal from the reporter gene, the production of viral RNA or infectious virus, or virus-induced CPE (Khoury et al., 2020).”
BackgroundMethodInfluentialEvaluation of Simple Lateral Flow Immunoassays for Detection of SARS-CoV-2 Neutralizing Antibodies
Nickel, O., Rockstroh, A., Borte, S., & Wolf, J. (2022) · Vaccines · doi:10.3390/vaccines10030347 · Cited by 8
“However, detection of nAb is time-consuming and harbors a number of technical pitfalls [2].”
BackgroundRisk of sustained SARS-CoV-2 transmission in Queensland, Australia
Sanz‐Leon, P., Stevenson, N. J., Stuart, R. M., Abeysuriya, R., Pang, J. C. S., Lambert, S. B., Kerr, C. C., & Roberts, J. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-10349-y · Cited by 8
Hirabidian, M., Bocket, L., Demaret, J., Vuotto, F., Rabat, A., Faure, K., Labalette, M., Hober, D., Lefèvre, G., & Alidjinou, E. K. (2022) · Journal of Clinical Virology · doi:10.1016/j.jcv.2022.105268 · Cited by 8
Plans-Rubió, P. (2023) · Vaccines · doi:10.3390/vaccines11121836 · Cited by 7
What Can We Still Learn from Brain Autopsies in COVID-19?
Solomon, I. H., Singh, A., Folkerth, R. D., & Mukerji, S. S. (2023) · Seminars in Neurology · doi:10.1055/s-0043-1767716 · Cited by 7
Thinking Outside the Box: Utilizing Nontraditional Animal Models for COVID-19 Research
Gunasekara, S., Selvan, M. T., Miller, C., & Rudd, J. M. (2022) · International Journal of Translational Medicine · doi:10.3390/ijtm2010010 · Cited by 7
Dimeglio, C., Hérin, F., Da-Silva, I., Gernigon, C., Porcheron, M., Chapuy‐Regaud, S., & Izopet, J. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02706-21 · Cited by 7
Sun, H., Xia, L., Li, J., Zhang, Y., Zhang, G., Huang, P. J., Wang, X., Cui, Y., Fang, T., Fan, P., et al. (2024) · Emerging Microbes & Infections · doi:10.1080/22221751.2024.2373307 · Cited by 6
“The IC 50 of each tested sample against different variants was calculated by the Reed-Muench method [36,37]. logIC 50 = log (concentration of antibody with > 50% inhibition) + (A-50%)/(A-B) × ( − log (dilution factor)).”
MethodLiang, T., Qiu, J., Niu, X., Ma, Q., Zhou, C., Chen, P., Zhang, Q., Chen, M., Yang, Z., Liu, S., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.603830 · Cited by 7
Passive Immunity Should and Will Work for COVID-19 for Some Patients
Cimolai, N. (2021) · Clinical Hematology International · doi:10.2991/chi.k.210328.001 · Cited by 7
A cell-free high throughput assay for assessment of SARS-CoV-2 neutralizing antibodies
Mravinacová, S., Jönsson, M., Christ, W., Klingström, J., Yousef, J., Hellström, C., Hedhammar, M., Havervall, S., Thålin, C., Pin, E., et al. (2021) · New Biotechnology · doi:10.1016/j.nbt.2021.10.002 · Cited by 7
“Spike-f [11,12] and ACE2 [16] (Supplementary Fig.”
Antiviral activity of an ACE2-Fc fusion protein against SARS-CoV-2 and its variants
Bermúdez-Abreut, E., Fundora-Barrios, T., Fernández, D. R. H., Romero, E. N., Quintero, A. F., Casadesús, A. V., Fernández-Marrero, B., Plasencia, C. A., Pérez, M. C., Sosa, K., et al. (2025) · PLoS ONE · doi:10.1371/journal.pone.0312402 · Cited by 5
“In contrast with Tsai’s works that used pseudovirus assay, we accomplished the neutralization experiments by using authentic virus, which enables a more accurate assessment of the actual neutralizing capacity of the fusion protein [51].”
Prospects of animal models and their application in studies on adaptive immunity to SARS-CoV-2
Wei, X., Rong, N., & Liu, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.993754 · Cited by 6
AbdelWareth, L., Alhousani, F., Abuyadek, R., Donnelly, J., Leinberger-Jabari, A., Atef, S., & Al-Rifai, R. H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1230974 · Cited by 5
Emerging Landscape of Preclinical Models for Studying COVID-19 Neurologic Diseases
Li, J., Wang, J., & Wang, H. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00127 · Cited by 5
Genetically engineered pair of cells for serological testing and its application for SARS‐CoV ‐2
Ssemadaali, M. A., Arredondo, J., Buser, E., Newmyer, S. L., Radhakrishnan, H., Javitz, H. S., Dandekar, S., & Bhatnagar, P. (2023) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10508 · Cited by 5
“22,23 This work complements existing serological testing technologies 18,20,24,25 enabling informed public health decisions required to reopen economies.”
Bian, S., Shang, M., Tao, Y., Wang, P., Xu, Y., Wang, Y., Shen, Z., & Sawan, M. (2024) · Vaccines · doi:10.3390/vaccines12040352 · Cited by 5
O'Mahoney, C., Watt, I. N., Fiedler, S., Devenish, S. R. A., Srikanth, S., Justice, E., Dover, T., Dean, D. M. D., & Peng, C. A. (2024) · Annals of Biomedical Engineering · doi:10.1007/s10439-024-03478-0 · Cited by 4
“Head-to-head comparisons of these methods have been done by Khoury and colleagues and Perkmann and colleagues [24, 35].”
MethodHu, J. S., Zhou, Y., Zhang, W., & Zhou, X. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf238 · Cited by 6
Animal Research in Spain: A Study of Public Perception and Attitudes
Miguel-Batuecas, A., Fuertes‐Recuero, M., Díaz‐Regañón, D., Ortiz‐Díez, G., Revuelta, L., & Pablo-Moreno, J. A. D. (2023) · Animals · doi:10.3390/ani13122039 · Cited by 5
“There are numerous limitations regarding animal experimentation such as problems with the translation and extrapolation of results to humans [19,20].”
BackgroundRoessler, J., Pich, D., Krähling, V., Becker, S., Keppler, O. T., Zeidler, R., & Hammerschmidt, W. (2023) · Biomedicines · doi:10.3390/biomedicines11112892 · Cited by 4
Comparative Analysis of SARS-CoV-2 Antigenicity across Assays and in Human and Animal Model SeraPreprint
Mühlemann, B., Wilks, S., Baracco, L., Bekliz, M., Carreño, J. M., Corman, V. M., Davis-Gardner, M. E., Dejnirattisai, W., Diamond, M., Douek, D. C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.27.559689 · Cited by 4
“…multiple replication cycles, and titers in these assays correspond to a different endpoint, requiring ~99% of the initial inoculum to be inhibited by antibodies, compared to a ~50% or ~90% inhibition measured in corresponding PRNT, FRNT, and single-cycle pseudovirus neutralization assays ( 32 ).”
Hansur, L., Louisa, M., & Wuyung, P. E. (2022) · AIP conference proceedings · doi:10.1063/5.0098285 · Cited by 3
Ravindran, R. K., Kang, H., McReynolds, C. B., Sanghar, G. K., Chang, W. L. W., Ramasamy, S., Kolloli, A., Kumar, R., Subbian, S., Hammock, B. D., et al. (2023) · PLoS ONE · doi:10.1371/journal.pone.0287377 · Cited by 3
Dunn, D. T., Gilson, R. J. C., McCormack, S., & McCoy, L. E. (2023) · Vaccine · doi:10.1016/j.vaccine.2023.06.037 · Cited by 5
Couderé, K., Benschop, K., Koen, G., van Eijk, H. W. M., Harvala, H., Bailly, J., Bessaud, M., Kamau, E., Simon, I., Joffret, M., et al. (2024) · Journal of General Virology · doi:10.1099/jgv.0.001986 · Cited by 3
Lv, N., Chen, P., Dai, X., Xu, H., Li, Z., Shan, Z., Li, J., Guo, F., Chen, Y., Li, J., et al. (2025) · Advanced Science · doi:10.1002/advs.202517192 · Cited by 2
Pagni, R. L., Cunha-Neto, E., Santos, Y. D. S., Postól, E., de Alencar, R. E., Moretti, A. I. S., dos Santos, J. J., Silva, T. L., Daher, I. P., Knirsch, M. C., et al. (2026) · npj Vaccines · doi:10.1038/s41541-026-01407-x · Cited by 2
“…vaccine against COVID-19 elicited robust local and systemic immune responses, we subsequently assessed whether immunization with the SiNP-MaP vaccine provided protection against infectious challenge with the ancestral Wuhan strain of SARS-CoV-2 in a highly susceptible K18-hACE2 mouse model 58 (Fig.”
Vladimirov, I. S., Zhdanova, A. S., Евгеньевич, М. В., Makarov, V. V., Yudin, V. S., & Александрович, К. С. (2023) · Medical Immunology (Russia) · doi:10.15789/1563-0625-iaf-2921 · Cited by 2
Алексеевич, С. А., Витальевич, Г. Д., Меркулов, В. А., & Бондарев, В. П. (2022) · Biological Products Prevention Diagnosis Treatment · doi:10.30895/2221-996x-2022-22-4-361-381 · Cited by 2
Dunn, D. T., Gilson, R. J. C., McCormack, S., & McCoy, L. E. (2022) · medRxiv · doi:10.1101/2022.09.20.22276701 · Cited by 2
“11 animal models, but extrapolation to humans is problematic.(21) Thus, it is prudent to study a wide range of doses, although this means that resources are spread thinly, with a small”
BackgroundMoore, J. P., & Gounder, C. R. (2021) · Nature Immunology · doi:10.1038/s41590-021-01033-w · Cited by 1
Experimental Models of SARS-COV-2 Infection in the Central Nervous System
Paoletti, A. M., Melilli, M. G., & Vecchio, I. (2022) · Journal of Central Nervous System Disease · doi:10.1177/11795735221102231 · Cited by 1
Virus Quantification Methods with Focus on Marek's Disease Viruses
Piryaei, M. R., Razmyar, J., Dolatyabi, S., & Bozorgmehrifard, M. H. (2023) · Journal of Poultry Sciences and Avian Diseases · doi:10.61838/kman.jpsad.1.1.5 · Cited by 1
Müller-Kräuter, H., Mezzacapo, J., Klüver, M., Baumgart, S., Becker, D., Fathi, A., Pfeiffer, S., & Krähling, V. (2024) · Medical Microbiology and Immunology · doi:10.1007/s00430-024-00789-w · Cited by 1
Maghsood, F., Dashti, N., Bahadori, T., Golsaz‐Shirazi, F., Moog, C., Amiri, M. M., & Shokri, F. (2025) · Analytical Biochemistry · doi:10.1016/j.ab.2025.115860 · Cited by 1
Methods to Measure Antibody Neutralization of Live Human Coronavirus OC43
Boonyaratanakornkit, J. B., Sholukh, A. M., Gray, M. D., Bossard, E. L., Ford, E. S., Corbett, K. S., Corey, L., & Taylor, J. J. (2021) · Viruses · doi:10.3390/v13102075 · Cited by 1
“While others have isolated mAbs from a SARS-CoV-2 convalescent individual or from mice immunized with MERS-CoV that cross-neutralize OC43 in a pseudotyped virus assay, OC2 is the first human mAb, to our knowledge, that specifically binds and neutralizes OC43 [17,18].”
BackgroundInfluentialImmunologie in der dermatologischen Praxis – wieviel, warum, wann?
Diamanti, E., Föhr, J., Papageorgiou, A., Herbst, M., & Jahn, S. (2022) · Aktuelle Dermatologie · doi:10.1055/a-1699-5440 · Cited by 1
Metadata
- Authors
- Khoury, D. S., Wheatley, A. K., Ramuta, M. D., Reynaldi, A., Cromer, D., Subbarao, K., O’Connor, D. H., Kent, S. J., & Davenport, M. P.
- Affiliations
- UNSW Sydney (AU)
- The University of Melbourne (AU)
- University of Wisconsin–Madison (US)
- Corresponding author
- Davenport, Miles P.
- ORCID
- Venue
- Nature Reviews Immunology
- Published
- 2020-11-02
- Volume
- 20
- Issue
- 12
- Pages
- 727-738
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- PMC
- PMC7605490
- OpenAlex
- W3096510866
- Cited by
- 115
- References
- 83
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 13 · 2023: 18 · 2022: 38 · 2021: 35
- FWCI
- 1.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature reviews. Immunology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion)
- UNSWorks (University of New South Wales, Sydney, Australia) (submittedVersion)
- Funders
- Wisconsin Alumni Research Foundation
- World Health Organization (SARS-CoV-2, COVID-19)
- Australian Government
- National Institutes of Health (COVID-19, R24OD017850, P51OD011106)
- Medical Research Council (COVID-19)
- National Health and Medical Research Council (1136322, 1173027, 1173433, 1173528, 1177174, 1141921)
- 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
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 detection and testing
- Keywords
- SARS-CoV-2, COVID-19 pandemic, neutralizing antibody assay, assay harmonization, immunotherapy efficacy
- MeSH terms
- COVID-19, COVID-19 Serological Testing, COVID-19 Drug Treatment, Animals, Disease Models, Animal, Humans, Immunoassay, Neutralization Tests, Pre-Exposure Prophylaxis
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