Measuring immunity to SARS-CoV-2 infection: comparing assays and animal models

Khoury, David S.; Wheatley, Adam K.; Ramuta, Mitchell D.; Reynaldi, Arnold; Cromer, Deborah; Subbarao, Kanta; O’Connor, David H.; Kent, Stephen J.; Davenport, Miles P.

doi:10.1038/s41577-020-00471-1

Cited by 116SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections StudiesSARS-CoV-2 detection and testing

Measuring immunity to SARS-CoV-2 infection: comparing assays and animal models

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Khoury, David S., Wheatley, Adam K., Ramuta, Mitchell D., Reynaldi, Arnold, Cromer, Deborah, Subbarao, Kanta, O’Connor, David H., Kent, Stephen J. +1 more·2020·Nature Reviews Immunology

DOI 10.1038/s41577-020-00471-1PMC PMC7605490

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Abstract

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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Animal models may not recapitulate all features of human infection but suggest the importance of looking beyond neutralizing antibodies for additional mechanisms of immune protection.
“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]
The study focused primarily on assays using live SARS-CoV-2 virus to reduce potential variability from different pseudoviral constructs, with the exception of NVX-CoV2373 for which pseudovirus data were used.
“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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Hartman, A. L., Nambulli, S., McMillen, C. M., White, A. G., Tilston‐Lunel, N. L., Albe, J. R., Cottle, E. L., Dunn, M., Frye, L. J., Gilliland, T. H., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008903 · Cited by 136 · see citing works
Acute Respiratory Distress in Aged, SARS-CoV-2–Infected African Green Monkeys but Not Rhesus Macaques
Blair, R. V., Vaccari, M., Doyle‐Meyers, L. A., Roy, C. J., Russell‐Lodrigue, K., Fahlberg, M. D., Monjure, C. J., Beddingfield, B. J., Plante, K. S., Plante, J. A., et al. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.10.016 · Cited by 132 · see citing works
Accelerating Development of SARS-CoV-2 Vaccines — The Role for Controlled Human Infection Models
Deming, M. E., Michael, N. L., Robb, M. L., Cohen, M. S., & Neuzil, K. M. (2020) · New England Journal of Medicine · doi:10.1056/nejmp2020076 · Cited by 108 · see citing works
Kinetics of Virus-Specific CD8<sup>+</sup>T Cells and the Control of Human Immunodeficiency Virus Infection
Davenport, M. P., Ribeiro, R. M., & Perelson, A. S. (2004) · Journal of Virology · doi:10.1128/jvi.78.18.10096-10103.2004 · Cited by 101 · see citing works
Self-citation
Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM
Imai, H., Uchiumi, T., & Kodera, N. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2018975117 · Cited by 88 · see citing works
Quantifying absolute neutralization titers against SARS-CoV-2 by a standardized virus neutralization assay allows for cross-cohort comparisons of COVID-19 seraPreprint
Oguntuyo, K., Stevens, C., Hung, C.-T., Ikegame, S., Acklin, J. A., Kowdle, S., Carmichael, J. C., Chiu, H.-P., Azarm, K. D., Haas, G. D., et al. (2020) · medRxiv · doi:10.1101/2020.08.13.20157222 · Cited by 72 · see citing works
Dense Array of Spikes on HIV-1 Virion Particles
Stano, A., Leaman, D. P., Kim, A. S., Zhang, L., Autin, L., Ingale, J., Gift, S. K., Truong, J., Wyatt, R. T., Olson, A. J., et al. (2017) · Journal of Virology · doi:10.1128/jvi.00415-17 · Cited by 70 · see citing works
Preclinical Assessment of HIV Vaccines and Microbicides by Repeated Low-Dose Virus Challenges
Regoes, R. R., Longini, I. M., Feinberg, M. B., & Staprans, S. I. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020249 · Cited by 69 · see citing works
Establishment of an African green monkey model for COVID-19Preprint
Woolsey, C. B., Borisevich, V., Prasad, A. N., Agans, K. N., Deer, D. J., Dobias, N. S., Heymann, J. C., Foster, S. L., Levine, C. B., Medina, L. O., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.17.100289 · Cited by 65 · see citing works
Ultra low dose aerosol challenge with Mycobacterium tuberculosis leads to divergent outcomes in rhesus and cynomolgus macaques
Sharpe, S. A., White, A., Gleeson, F. V., McIntyre, A., Smyth, D., Clark, S. O., Sarfas, C., Laddy, D. J., Rayner, E. L., Hall, G. A., et al. (2015) · Tuberculosis · doi:10.1016/j.tube.2015.10.004 · Cited by 62 · see citing works
Virion Envelope Content, Infectivity, and Neutralization Sensitivity of Simian Immunodeficiency Virus
Yuste, E., Johnson, W., Pavlakis, G., & Desrosiers, R. (2005) · Journal of Virology · doi:10.1128/jvi.79.19.12455-12463.2005 · Cited by 57 · see citing works
Partial efficacy of a broadly neutralizing antibody against cell-associated SHIV infection
Parsons, M. S., Lloyd, S. B., Lee, W. S., Kristensen, A. B., Amarasena, T. H., Keele, B. F., Lifson, J. D., LaBranche, C. C., Montefiori, D. C., Wines, B. D., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf1483 · Cited by 53 · see citing works
Self-citation
In Vivo Validation of the Viral Barcoding of Simian Immunodeficiency Virus SIVmac239 and the Development of New Barcoded SIV and Subtype B and C Simian-Human Immunodeficiency Viruses
Khanal, S., Fennessey, C. M., O’Brien, S. P., Thorpe, A. L., Reid, C., Immonen, T. T., Smith, R., Bess, J. W., Swanstrom, A. E., Prete, G. Q. D., et al. (2019) · Journal of Virology · doi:10.1128/jvi.01420-19 · Cited by 47 · see citing works
Self-citation
Characteristic and quantifiable COVID-19-like abnormalities in CT- and PET/CT-imaged lungs of SARS-CoV-2-infected crab-eating macaques ( Macaca fascicularis )Preprint
Finch, C. L., Crozier, I., Lee, J. H., Byrum, R., Cooper, T. K., Liang, J. Y., Sharer, K., Solomon, J. M., Sayre, P. J., Kocher, G. A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.14.096727 · Cited by 44 · see citing works
Self-citation
Defining early SIV replication and dissemination dynamics following vaginal transmission
Deléage, C., Immonen, T. T., Fennessey, C. M., Reynaldi, A., Reid, C., Newman, L. P., Lipkey, L., Schlub, T. E., Camus, C., O’Brien, S. P., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav7116 · Cited by 38 · see citing works
Self-citation
Quantitative Correlation between Infectivity and Gp120 Density on HIV-1 Virions Revealed by Optical Trapping Virometry
DeSantis, M. C., Kim, J. H., Song, H., Klasse, P. J., & Cheng, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.729210 · Cited by 36 · see citing works
An enzyme-based immunodetection assay to quantify SARS-CoV-2 infection
Conzelmann, C., Gilg, A., Groß, R. M., Schütz, D., Preising, N., Ständker, L., Jahrsdörfer, B., Schrezenmeier, H., Sparrer, K. M. J., Stamminger, T., et al. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104882 · Cited by 36 · see citing works
The Role of Exposure History on HIV Acquisition: Insights from Repeated Low-dose Challenge Studies
Regoes, R. R. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002767 · Cited by 30 · see citing works
Evaluating Use Cases for Human Challenge Trials in Accelerating SARS-CoV-2 Vaccine Development
Nguyen, L. C., Bakerlee, C. W., McKelvey, T. G., Rose, S., Norman, A. J., Joseph, N. C., Manheim, D., McLaren, M. R., Jiang, S. X., Barnes, C. F., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa935 · Cited by 29 · see citing works
SARS-CoV-2 infection leads to acute infection with dynamic cellular and inflammatory flux in the lung that varies across nonhuman primate speciesPreprint
Singh, D., Ganatra, S. R., Singh, B., Cole, J., Alfson, K. J., Clemmons, E., Gazi, M., Gonzalez, O., Escobedo, R. A., Lee, T.-H., et al. (2020) · bioRxiv · doi:10.1101/2020.06.05.136481 · Cited by 28 · see citing works
“Acute Respiratory Distress and Cytokine Storm in Aged, SARS-CoV-2 Infected African Green Monkeys, but not in Rhesus Macaques”Preprint
Blair, R. V., Vaccari, M., Doyle‐Meyers, L. A., Roy, C. J., Russell‐Lodrigue, K., Fahlberg, M. D., Monjure, C. J., Beddingfield, B. J., Plante, K. S., Plante, J. A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.18.157933 · Cited by 15 · see citing works
Quantifying Absolute Neutralization Titers against SARS-CoV-2 by a Standardized Virus Neutralization Assay Allows for Cross-Cohort Comparisons of COVID-19 Sera
Oguntuyo, K., Stevens, C., Hung, C.-T., Ikegame, S., Acklin, J. A., Kowdle, S., Carmichael, J. C., Chiu, H.-P., Azarm, K. D., Haas, G. D., et al. (2021) · mBio · doi:10.1128/mbio.02492-20 · Cited by 12 · see citing works
Viewpoint of a WHO Advisory Group Tasked to Consider Establishing a Closely-Monitored Challenge Model of COVID-19 in Healthy Volunteers.
Levine, M. M., Abdullah, S., Arabi, Y. M., Darko, D. M., Durbin, A. P., Estrada, V., Jamrozik, E., Kremsner, P. G., Lagos, R., Pitisuttithum, P., et al. (2020) · PubMed Central · doi:10.1093/cid/ciaa1290 · Cited by 7 · see citing works
Self-citation
Short Communication: Viremic Control Is Independent of Repeated Low-Dose SHIV SF162p3 Exposures
Henning, T., Hanson, D. L., Vishwanathan, S. A., Butler, K. A., Dobard, C., García-Lerma, G., Radzio, J., Smith, J., McNicholl, J. M., & Kersh, E. N. (2014) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2014.0238 · Cited by 5 · see citing works

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Neutralizing antibody levels are highly predictive of immune protection from symptomatic SARS-CoV-2 infection
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) · Nature Medicine · doi:10.1038/s41591-021-01377-8 · Cited by 3,742 · see citing works
Self-citation
Neutralising antibody titres as predictors of protection against SARS-CoV-2 variants and the impact of boosting: a meta-analysis
Cromer, D., Steain, M., Reynaldi, A., Schlub, T. E., Wheatley, A. K., Juno, J. A., Kent, S. J., Triccas, J. A., Khoury, D. S., & Davenport, M. P. (2022) · The Lancet Microbe · doi:10.1016/s2666-5247(21)00267-6 · Cited by 590 · see citing works
Self-citation
Respiratory mucosal delivery of next-generation COVID-19 vaccine provides robust protection against both ancestral and variant strains of SARS-CoV-2
Afkhami, S., D’Agostino, M. R., Zhang, A., Stacey, H. D., Marzok, A., Kang, A., Singh, R., Bavananthasivam, J., Ye, G., Luo, X., et al. (2022) · Cell · doi:10.1016/j.cell.2022.02.005 · Cited by 307 · see citing works
“Single-dose intranasal immunization with ChAdvectored trivalent COVID-19 vaccine protects against lethal infection by SARS-CoV-2 variants of concern We next assessed vaccine-induced protection against wild-type ancestral and VOC strains of SARS-CoV-2 in highly susceptible K18-hACE2 mouse model (Khoury et al., 2020).”
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 · see citing works
Self-citation
COVID-19 vaccination: The road ahead
Altmann, D. M., & Boyton, R. J. (2022) · Science · doi:10.1126/science.abn1755 · Cited by 195 · see citing works
Exploration of nanozymes in viral diagnosis and therapy
Lee, J., Liao, H., Wang, Q., Han, J., Han, J., Shin, H. E., Ge, M., Park, W., & Li, F. (2022) · Exploration · doi:10.1002/exp.20210086 · Cited by 167 · see citing works
Correlates of Protection, Thresholds of Protection, and Immunobridging among Persons with SARS-CoV-2 Infection
Khoury, D. S., Schlub, T. E., Cromer, D., Steain, M. C., Fong, Y., Gilbert, P. B., Subbarao, K., Triccas, J. A., Kent, S. J., & Davenport, M. P. (2023) · Emerging infectious diseases · doi:10.3201/eid2902.221422 · Cited by 148 · see citing works
“…it is clear from those discrepancies that expression of titers in international units is insufficient for normalizing between different assays and comparing the thresholds of protection reported in these studies (Appendix), which most likely results from differences in the assays themselves ( 8 ).”
ResultSelf-citation
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 145 · see citing works
“…of virus used (e.g., authentic virus, recombinant replication-competent virus, or replication-deficient pseudovirus), the type of target cell, expression levels of ACE2 and proteases, and/or the type of readout (e.g., bioluminescence, plaque reduction, or cytopathic effects) (Khoury et al., 2020).”
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
Pymm, P., Adair, A., Chan, L., Cooney, J. P., Mordant, F., Allison, C., Lopez, E., Haycroft, E., O, Neill, M., et al. (2021) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2101918118 · Cited by 134 · see citing works
Self-citation
Neutralising antibodies predict protection from severe COVID-19
Cromer, D., Steain, M., Reynaldi, A., Schlub, T. E., Sasson, S. C., Kent, S. J., Khoury, D. S., & Davenport, M. P. (2022) · doi:10.1101/2022.06.09.22275942 · Cited by 139 · see citing works
Self-citation
Immunogenicity of clinically relevant SARS-CoV-2 vaccines in nonhuman primates and humans
Klasse, P. J., Nixon, D. F., & Moore, J. P. (2021) · Science Advances · doi:10.1126/sciadv.abe8065 · Cited by 98 · see citing works
Temporal omics analysis in Syrian hamsters unravel cellular effector responses to moderate COVID-19
Nouailles, G., Wyler, E., Pennitz, P., Postmus, D., Vladimirova, D., Kazmierski, J., Pott, F., Dietert, K., Mülleder, M., Farztdinov, V. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25030-7 · Cited by 98 · see citing works
Emerging Vaccine-Breakthrough SARS-CoV-2 Variants
Wang, R., Chen, J., Hozumi, Y., Yin, C., & Wei, G. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00557 · Cited by 81 · see citing works
Susceptibility of SARS-CoV-2 Omicron Variants to Therapeutic Monoclonal Antibodies: Systematic Review and Meta-analysis
Tao, K., Tzou, P. L., Pond, S. L. K., Ioannidis, J. P. A., & Shafer, R. W. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.00926-22 · Cited by 80 · see citing works
“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).”
Method
T cell immunity to SARS-CoV-2
Niessl, J., Sekine, T., & Buggert, M. (2021) · Seminars in Immunology · doi:10.1016/j.smim.2021.101505 · Cited by 74 · see citing works
Advances in Neutralization Assays for SARS‐CoV‐2
Lu, Y., Jin, W., Li, Q., Hu, H., Lu, J., & Chen, Z. (2021) · Scandinavian Journal of Immunology · doi:10.1111/sji.13088 · Cited by 57 · see citing works
Monoclonal antibody levels and protection from COVID-19
Stadler, E., Burgess, M. T., Schlub, T. E., Khan, S. R., Chai, K. L., McQuilten, Z., Wood, E. M., Polizzotto, M. N., Kent, S. J., Cromer, D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40204-1 · Cited by 61 · see citing works
Self-citation
Performance of the Abbott SARS-CoV-2 IgG II Quantitative Antibody Assay Including the New Variants of Concern, VOC 202012/V1 (United Kingdom) and VOC 202012/V2 (South Africa), and First Steps towards Global Harmonization of COVID-19 Antibody Methods
English, E., Cook, L. E., Piec, I., Dervisevic, S., Fraser, W. D., & John, W. G. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00288-21 · Cited by 52 · see citing works
Modeling SARS-CoV-2 spike/ACE2 protein–protein interactions for predicting the binding affinity of new spike variants for ACE2, and novel ACE2 structurally related human protein targets, for COVID-19 handling in the 3PM context
Tragni, V., Preziusi, F., Laera, L., Onofrio, A., Mercurio, I., Todisco, S., Volpicella, M., Grassi, A., & Pierri, C. L. (2022) · The EPMA Journal · doi:10.1007/s13167-021-00267-w · Cited by 48 · see citing works
“…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.”
Background
SARS-CoV-2 antibody testing for estimating COVID-19 prevalence in the population
Vogl, T. J., Leviatan, S., & Segal, E. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100191 · Cited by 43 · see citing works
“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.”
Influential
A 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 46 · see citing works
“Neutralising antibodies are emerging as a strong correlate of protection [6,7] but are only a subset of the total polyclonal response.”
BackgroundMethodSelf-citation
Covid-19 in patients with chronic lymphocytic leukemia: clinical outcome and B- and T-cell immunity during 13 months in consecutive patients
Blixt, L., Bogdanović, G., Buggert, M., Gao, Y., Hober, S., Healy, K., Johansson, H., Kjellander, C., Mravinacová, S., Muschiol, S., et al. (2021) · Leukemia · doi:10.1038/s41375-021-01424-w · Cited by 41 · see citing works
Predicting Vaccine Effectiveness for Hospitalization and Symptomatic Disease for Novel SARS-CoV-2 Variants Using Neutralizing Antibody Titers
Gardner, B. J., & Kilpatrick, A. M. (2024) · Viruses · doi:10.3390/v16030479 · Cited by 43 · see citing works
“This highlights the need for standardized neutralization assays and reference sera [22].”
Background
Simultaneous 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 · see citing works
“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-citation
A third dose of inactivated vaccine augments the potency, breadth, and duration of anamnestic responses against SARS-CoV-2Preprint
Wang, 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 38 · see citing works
SARS-CoV-2 remodels the Golgi apparatus to facilitate viral assembly and secretion
Zhang, J., Kennedy, A. A., Jorge, D. M. D. M., Xing, L., Reid, W., Bui, S., Joppich, J., Rose, M., Ercan, S., Tang, Q., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013295 · Cited by 38 · see citing works
“…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
Zhang, J., Du, Y., Zhou, P., Ding, J., Xia, S., Wang, Q., Chen, F., Zhou, M., Zhang, X., Wang, W.-F., et al. (2022) · Nature Machine Intelligence · doi:10.1038/s42256-022-00553-w · Cited by 37 · see citing works
“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 .”
Method
What 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 · see citing works
Self-citation
Ad26.COV2.S breakthrough infections induce high titers of neutralizing antibodies against Omicron and other SARS-CoV-2 variants of concern
Kitchin, D., Richardson, S. I., van der Mescht, M. A., Motlou, T. P., Mzindle, N. B., Moyo-Gwete, T., Makhado, Z., Ayres, F., Manamela, N. P., Spencer, H., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100535 · Cited by 35 · see citing works
“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
Zhuang, C., Liu, X., Chen, Q., Yuxin, S., Su, Y., Huang, S., Wu, T., & Xia, N. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.828806 · Cited by 36 · see citing works
Comparison of the immunogenicity & protective efficacy of various SARS-CoV-2 vaccine candidates in non-human primates
Mukhopadhyay, L., Yadav, P. D., Gupta, N., Mohandas, S., Patil, D. Y., Shete-Aich, A., Panda, S., & Bhargava, B. (2021) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_4431_20 · Cited by 33 · see citing works
Proteases and variants: context matters for SARS-CoV-2 entry assays
Stevens, C. S., Oguntuyo, K. Y., & Lee, B. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.07.004 · Cited by 26 · see citing works
COVID-19 Research: Lessons from Non-Human Primate Models
Albrecht, L., Bishop, E., Jay, B., Lafoux, B., Minoves, M., & Passaes, C. (2021) · Vaccines · doi:10.3390/vaccines9080886 · Cited by 28 · see citing works
“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…”
Background
Anti-SARS-CoV-2 Immunoglobulin Isotypes, and Neutralization Activity Against Viral Variants, According to BNT162b2-Vaccination and Infection History
Tarkowski, M., de Jager, W., Schiuma, M., Covizzi, A., Lai, A., Gabrieli, A., Corbellino, M., Bergna, A., Ventura, C. D., Galli, M., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.793191 · Cited by 27 · see citing works
“of a humoral response against specific viral variants (47).”
Background
SARS-CoV-2 Serologic Assays Dependent on Dual-Antigen Binding Demonstrate Diverging Kinetics Relative to Other Antibody Detection Methods
Theel, E. S., Johnson, P. W., Kunze, K. L., Wu, L. L., Gorsh, A. P., Granger, D., Roforth, M. M., Jerde, C. R., Lasho, M. A., Andersen, K. J., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.01231-21 · Cited by 25 · see citing works
“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).”
Background
The role of pseudotype neutralization assays in understanding SARS CoV-2
Cantoni, D., Mayora-Neto, M., & Temperton, N. (2021) · Oxford Open Immunology · doi:10.1093/oxfimm/iqab005 · Cited by 15 · see citing works
Converting non-neutralizing SARS-CoV-2 antibodies into broad-spectrum inhibitors
Weidenbacher, P. A. B., Waltari, E., Kobara, I. D. L. R., Bell, B. N., Morris, M. K., Cheng, Y.-C., Hanson, C. V., Pak, J. E., & Kim, P. S. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01140-1 · Cited by 23 · see citing works
The Hard Lessons and Shifting Modeling Trends of COVID-19 Dynamics: Multiresolution Modeling Approach
Akman, O., Chauhan, S., Ghosh, A., Liesman, S., Michael, E., Mubayi, A., Perlin, R., Seshaiyer, P., & Tripathi, J. P. (2021) · Bulletin of Mathematical Biology · doi:10.1007/s11538-021-00959-4 · Cited by 22 · see citing works
“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.”
Background
Cell and Animal Models for SARS-CoV-2 Research
Bestion, E., Halfon, P., Mezouar, S., & Mege, J. (2022) · Viruses · doi:10.3390/v14071507 · Cited by 19 · see citing works
Modelling herd immunity requirements in Queensland: impact of vaccination effectiveness, hesitancy and variants of SARS-CoV-2
Sanz‐Leon, P., Hamilton, L. H. W., Raison, S. J., Pan, A. J. X., Stevenson, N. J., Stuart, R. M., Abeysuriya, R., Kerr, C. C., Lambert, S. B., & Roberts, J. A. (2022) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2021.0311 · Cited by 18 · see citing works
“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].”
Background
Distinct spatial arrangements of ACE2 and TMPRSS2 expression in Syrian hamster lung lobes dictates SARS-CoV-2 infection patterns
Tomris, I., Bouwman, K. M., Adolfs, Y., Noack, D., van der Woude, R., Kerster, G., Herfst, S., Sanders, R. W., van Gils, M. J., Boons, G., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010340 · Cited by 21 · see citing works
“Several reviews succinctly compare the advantages and disadvantages of different animal models [19,20].”
Background
Evaluation of Two Rapid Lateral Flow Tests and Two Surrogate ELISAs for the Detection of SARS-CoV-2 Specific Neutralizing Antibodies
Girl, P., Zwirglmaier, K., von Buttlar, H., Wölfel, R., & Müller, K. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.820151 · Cited by 19 · see citing works
Repeated Exposure to Subinfectious Doses of SARS-CoV-2 May Promote T Cell Immunity and Protection against Severe COVID-19
Angelis, M. L. D., Francescangeli, F., Rossi, R., Giuliani, A., Maria, R. D., & Zeuner, A. (2021) · Viruses · doi:10.3390/v13060961 · Cited by 17 · see citing works
“Low dose challenge models for SARS-CoV-2 have not yet been systematically developed [26].”
Method
MVA vector expression of SARS-CoV-2 spike protein and protection of adult Syrian hamsters against SARS-CoV-2 challenge
Meseda, C. A., Stauft, C. B., Selvaraj, P., Lien, C. Z., Pedro, C. L., Nuñez, I. A., Woerner, A. M., Wang, T. T., & Weir, J. P. (2021) · npj Vaccines · doi:10.1038/s41541-021-00410-8 · Cited by 19 · see citing works
Multiple sclerosis in the era of COVID-19: disease course, DMTs and SARS-CoV2 vaccinations
Pugliatti, M., Berger, T., Hartung, H., Oreja‐Guevara, C., & Bar‐Or, A. (2022) · Current Opinion in Neurology · doi:10.1097/wco.0000000000001066 · Cited by 19 · see citing works
Development of receptor binding domain-based double-antigen sandwich lateral flow immunoassay for the detection and evaluation of SARS-CoV-2 neutralizing antibody in clinical sera samples compared with the conventional virus neutralization test
Zhang, Y., Chen, Y., He, Y., Li, Y., Zhang, X., Liang, J., He, J., Lü, S., Gao, Z., Xu, J., et al. (2022) · Talanta · doi:10.1016/j.talanta.2022.124200 · Cited by 18 · see citing works
Shared clinical and immunologic features of mRNA vaccines: preliminary results from a comparative clinical study
Fierro, C. A., Sánchez-Crespo, N., Makrinos, D. L., Zhang, W., Sun, Y., Rohilla, P., Girard, B., Adeniji, A., DiPiazza, A. T., & Paris, R. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1501275 · Cited by 17 · see citing works
“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 · see citing works
Self-citation
Plaque Reduction Neutralization Test (PRNT) Accuracy in Evaluating Humoral Immune Response to SARS-CoV-2
Horbach, I. S., Azevedo, A. D. S., Schwarcz, W. D., Alves, N. D. S., Dias, B. D. M., Setatino, B. P., Moura, L. D. C., de Souza, A. F., Denani, C. B., da Silva, S. A., et al. (2024) · Diseases · doi:10.3390/diseases12010029 · Cited by 17 · see citing works
“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].”
Background
CXCL13 in laboratory diagnosis of Lyme neuroborreliosis—the performance of the recomBead and ReaScan CXCL13 assays in human cerebrospinal fluid samples
Haglund, S., Lager, M., Gyllemark, P., Andersson, G., Ekelund, O., Sundqvist, M., & Henningsson, A. J. (2021) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-021-04350-y · Cited by 15 · see citing works
Rapid electrochemical immunodetection of SARS-CoV-2 using a pseudo-typed vesicular stomatitis virus model
Ashur, I., Alter, J., Werbner, M., Ogungbile, A., Dessau, M. A., Gal-Tanamy, M., & Vernick, S. (2021) · Talanta · doi:10.1016/j.talanta.2021.123147 · Cited by 16 · see citing works
“A viable alternative is the use of pseudo-typed, non-replicative viral particles [8].”
Background
Comparative analysis of SARS-CoV-2 neutralization titers reveals consistency between human and animal model serum and across assays
Mühlemann, B., Wilks, S. H., Baracco, L., Bekliz, M., Carreño, J. M., Corman, V. M., Davis-Gardner, M. E., Dejnirattisai, W., Diamond, M., Douek, D. C., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adl1722 · Cited by 18 · see citing works
Predicting COVID-19 booster immunogenicity against future SARS-CoV-2 variants and the benefits of vaccine updates
Cromer, D., Reynaldi, A., Mitchell, A., Schlub, T. E., Juno, J. A., Wheatley, A. K., Kent, S. J., Khoury, D. S., & Davenport, M. P. (2024) · Nature Communications · doi:10.1038/s41467-024-52194-9 · Cited by 15 · see citing works
“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-citation
Quantitation of SARS-CoV-2 neutralizing antibodies with a virus-free, authentic test
Roessler, J., Pich, D., Albanese, M., Wratil, P. R., Krähling, V., Hellmuth, J. C., Scherer, C., von Bergwelt‐Baildon, M., Becker, S., Keppler, O. T., et al. (2022) · PNAS Nexus · doi:10.1093/pnasnexus/pgac045 · Cited by 11 · see citing works
SARS-CoV-2 Spike Protein-Activated Dendritic Cell-Derived Extracellular Vesicles Induce Antiviral Immunity in Mice
Barnwal, A., Basu, B., Tripathi, A., Soni, N., Mishra, D., Banerjee, A. K., Kumar, R., Vrati, S., & Bhattacharyya, J. (2022) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.2c01094 · Cited by 11 · see citing works
Review on In Silico Methods, High-throughput Screening Techniques, and Cell Culture Based In Vitro Assays for SARS-CoV-2
Çetin, Y., Aydınlık, Ş., Güngör, A., Kan, T., Avşar, T., & Durdağı, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220627121416 · Cited by 10 · see citing works
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 10 · see citing works
“Ferrets were able to transmit the virus through direct contact with other animals or by indirect contact [8,16,42,62].”
Background
Development 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 10 · see citing works
“protein epitopes and cannot detect antibodies targeting other viral proteins (27).”
Background
Validation of a Novel Fluorescent Lateral Flow Assay for Rapid Qualitative and Quantitative Assessment of Total Anti-SARS-CoV-2 S-RBD Binding Antibody Units (BAU) from Plasma or Fingerstick Whole-Blood of COVID-19 Vaccinees
Younes, 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 · see citing works
“Therefore, neutralization assays remain the gold standard for measuring the nAbs titer against SARS-CoV-2 [9].”
Background
Organotypic 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 9 · see citing works
Susceptibility of SARS-CoV-2 Omicron Variants to Therapeutic Monoclonal Antibodies: Systematic Review and Meta-AnalysisPreprint
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 · see citing works
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 · see citing works
“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).”
BackgroundMethodInfluential
Evaluation 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 · see citing works
“However, detection of nAb is time-consuming and harbors a number of technical pitfalls [2].”
Background
Risk 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 · see citing works
Evaluation of a Rapid Semiquantitative Lateral Flow Assay for the Prediction of Serum Neutralizing Activity Against SARS-CoV-2 Variants
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 · see citing works
Effectiveness of Adapted COVID-19 Vaccines and Ability to Establish Herd Immunity against Omicron BA.1 and BA4-5 Variants of SARS-CoV-2
Plans-Rubió, P. (2023) · Vaccines · doi:10.3390/vaccines11121836 · Cited by 7 · see citing works
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 · see citing works
Thinking Outside the Box: Utilizing Nontraditional Animal Models for COVID-19 Research
Gunasekara, S., Selvan, M. T., Miller, C. A., & Rudd, J. M. (2022) · International Journal of Translational Medicine · doi:10.3390/ijtm2010010 · Cited by 5 · see citing works
Decreased Efficiency of Neutralizing Antibodies from Previously Infected or Vaccinated Individuals against the B.1.617.2 (Delta) SARS-CoV-2 Variant
Diméglio, 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 8 · see citing works
A novel bispecific antibody targeting two overlapping epitopes in RBD improves neutralizing potency and breadth against SARS-CoV-2
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 · see citing works
“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)).”
Method
3-Hydroxyphthalic Anhydride-Modified Chicken Ovalbumin as a Potential Candidate Inhibits SARS-CoV-2 Infection by Disrupting the Interaction of Spike Protein With Host ACE2 Receptor
Liang, 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 6 · see citing works
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 6 · see citing works
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 · see citing works
“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 · see citing works
“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 · see citing works
Natural infection versus hybrid (natural and vaccination) humoral immune response to SARS-CoV-2: a comparative paired analysis
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 · see citing works
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 · see citing works
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 · see citing works
“22,23 This work complements existing serological testing technologies 18,20,24,25 enabling informed public health decisions required to reopen economies.”
Dynamic Profiling and Prediction of Antibody Response to SARS-CoV-2 Booster-Inactivated Vaccines by Microsample-Driven Biosensor and Machine Learning
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 · see citing works
Microfluidic Diffusional Sizing (MDS) Measurements of Secretory Neutralizing Antibody Affinity Against SARS-CoV-2
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 · see citing works
“Head-to-head comparisons of these methods have been done by Khoury and colleagues and Perkmann and colleagues [24, 35].”
Method
RLEAAI: improving antibody–antigen interaction prediction using protein language model and sequence order information
Hu, J. S., Zhou, Y., Zhang, W., & Zhou, X. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf238 · Cited by 4 · see citing works
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 4 · see citing works
“There are numerous limitations regarding animal experimentation such as problems with the translation and extrapolation of results to humans [19,20].”
Background
SARS-CoV-2 and Epstein–Barr Virus-like Particles Associate and Fuse with Extracellular Vesicles in Virus Neutralization Tests
Roessler, J., Pich, D., Krähling, V., Becker, S., Keppler, O. T., Zeidler, R., & Hammerschmidt, W. (2023) · Biomedicines · doi:10.3390/biomedicines11112892 · Cited by 4 · see citing works
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 · see citing works
“…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 ).”
Approach for the study of COVID-19 infection and vaccine development using mice model: A narrative review
Hansur, L., Louisa, M., & Wuyung, P. E. (2022) · AIP conference proceedings · doi:10.1063/5.0098285 · Cited by 3 · see citing works
Dynamics of temporal immune responses in nonhuman primates and humans immunized with COVID-19 vaccines
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 · see citing works
Licenced doses of approved COVID-19 vaccines may not be optimal: A review of the early-phase, dose-finding trials
Dunn, D. T., Gilson, R. J. C., McCormack, S., & McCoy, L. E. (2023) · Vaccine · doi:10.1016/j.vaccine.2023.06.037 · Cited by 3 · see citing works
Assessment of twelve echovirus virus-neutralisation assays in Europe: recommendations for harmonisation of non-polio enterovirus sero-surveillance studies
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 · see citing works
IgG‐Bridging–Seeded Synergistic Aggregation of SARS‐CoV‐2 Spikes Underlies Potent Neutralization by a Low‐Affinity Antibody
Lv, N.-N., Chen, P., Dai, X., Xu, H., Li, Z.-H., Shan, Z., Li, J.-Q., Guo, F.-L., Chen, Y.-F., Li, J.-Y., et al. (2025) · bioRxiv · doi:10.1002/advs.202517192 · Cited by 3 · see citing works
An innovative nasal nanovaccine against SARS-CoV-2 induces systemic and upper airway immunity controlling viral replication
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 · see citing works
“…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.”
Identification and functional characteristic of SARS-CoV-2-specific T lymphocytes in COVID-19 patients up to 16 months after disease onset
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 · see citing works
Aspects and issues of marketing authorisation and use of medicinal products for COVID-19 prevention during the pandemic
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 · see citing works
Dose of approved COVID-19 vaccines is based on weak evidence: a review of early-phase, dose-finding trialsPreprint
Dunn, D. T., Gilson, R. J. C., McCormack, S., & McCoy, L. E. (2022) · medRxiv · doi:10.1101/2022.09.20.22276701 · Cited by 2 · see citing works
“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”
Background
Beta testing the monkey model
Moore, J. P., & Gounder, C. R. (2021) · Nature Immunology · doi:10.1038/s41590-021-01033-w · Cited by 1 · see citing works
Experimental Models of SARS-COV-2 Infection in the Central Nervous System
Paoletti, A., Melilli, M., & Vecchio, I. (2022) · Journal of Central Nervous System Disease · doi:10.1177/11795735221102231 · Cited by 1 · see citing works
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 · see citing works
Quantitative assay to analyze neutralization and inhibition of authentic Middle East respiratory syndrome coronavirus
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 · see citing works
Comparative assessment of four virus neutralization assays for detection of SARS-CoV-2 neutralizing antibodies
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 · see citing works
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 · see citing works
“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].”
BackgroundInfluential
Immunologie 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 · see citing works

Advances in Neutralization Assays for SARS‐CoV‐2
Lu, Y., Jin, W., Li, Q., Hu, H., Lu, J., & Chen, Z. (2021) · Scandinavian Journal of Immunology · doi:10.1111/sji.13088 · Cited by 57 · see citing works
Evaluating Humoral Immunity against SARS-CoV-2: Validation of a Plaque-Reduction Neutralization Test and a Multilaboratory Comparison of Conventional and Surrogate Neutralization Assays
Valcourt, E. J., Manguiat, K., Robinson, A., Lin, Y.-C., Abe, K., Mubareka, S., Shigayeva, A., Zhong, Z., Girardin, R. C., Dupuis, A. P., et al. (2021) · Microbiology spectrum · doi:10.1128/spectrum.00886-21 · Cited by 25 · see citing works
Detection of SARS-CoV-2 Neutralizing Antibodies and Vaccine Development
(2026) · MDPI eBooks · doi:10.3390/books978-3-7258-6535-2
Importance, Applications and Features of Assays Measuring SARS-CoV-2 Neutralizing Antibodies
Gattinger, P., Ohradanova‐Repic, A., & Valenta, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065352 · Cited by 22 · see citing works
Assay Harmonization Study To Measure Immune Response to SARS-CoV-2 Infection and Vaccines: a Serology Methods Study
Kemp, T. J., Hempel, H., Pan, Y., Roy, D., Cherry, J. D., Lowy, D. R., & Pinto, L. A. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.05353-22 · Cited by 12 · see citing works

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: Khoury, David S.
Wheatley, Adam K.
Ramuta, Mitchell D.
Reynaldi, Arnold
Cromer, Deborah
Subbarao, Kanta
O’Connor, David H.
Kent, Stephen J.
Davenport, Miles P.
Venue: Nature Reviews Immunology
Publisher: Springer Science and Business Media LLC
Published: 2020-11-02
Volume: 20
Issue: 12
Pages: 727-738
ISSN: 1474-1733 (ISSN-L)
1474-1741
DOI: 10.1038/s41577-020-00471-1
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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