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Article ; Online: H3N2 influenza hemagglutination inhibition method qualification with data driven statistical methods for human clinical trials.

Sawant, Sheetal / Gurley, Sarah Anne / Overman, R Glenn / Sharak, Angelina / Mudrak, Sarah V / Oguin, Thomas / Sempowski, Gregory D / Sarzotti-Kelsoe, Marcella / Walter, Emmanuel B / Xie, Hang / Pasetti, Marcela F / Moody, M Anthony / Tomaras, Georgia D

Frontiers in immunology

2023 Volume 14, Page(s) 1155880

Abstract: Introduction: Hemagglutination inhibition (HAI) antibody titers to seasonal influenza strains are important surrogates for vaccine-elicited protection. However, HAI assays can be variable across labs, with low sensitivity across diverse viruses due to ... ...

Abstract	Introduction: Hemagglutination inhibition (HAI) antibody titers to seasonal influenza strains are important surrogates for vaccine-elicited protection. However, HAI assays can be variable across labs, with low sensitivity across diverse viruses due to lack of standardization. Performing qualification of these assays on a strain specific level enables the precise and accurate quantification of HAI titers. Influenza A (H3N2) continues to be a predominant circulating subtype in most countries in Europe and North America since 1968 and is thus a focus of influenza vaccine research. Methods: As a part of the National Institutes of Health (NIH)-funded Collaborative Influenza Vaccine Innovation Centers (CIVICs) program, we report on the identification of a robust assay design, rigorous statistical analysis, and complete qualification of an HAI assay using A/Texas/71/2017 as a representative H3N2 strain and guinea pig red blood cells and neuraminidase (NA) inhibitor oseltamivir to prevent NA-mediated agglutination. Results: This qualified HAI assay is precise (calculated by the geometric coefficient of variation (GCV)) for intermediate precision and intra-operator variability, accurate calculated by relative error, perfectly linear (slope of -1, R-Square 1), robust (<25% GCV) and depicts high specificity and sensitivity. This HAI method was successfully qualified for another H3N2 influenza strain A/Singapore/INFIMH-16-0019/2016, meeting all pre-specified acceptance criteria. Discussion: These results demonstrate that HAI qualification and data generation for new influenza strains can be achieved efficiently with minimal extra testing and development. We report on a qualified and adaptable influenza serology method and analysis strategy to measure quantifiable HAI titers to define correlates of vaccine mediated protection in human clinical trials.
MeSH term(s)	United States ; Humans ; Animals ; Guinea Pigs ; Influenza, Human ; Influenza Vaccines ; Influenza A Virus, H3N2 Subtype ; Hemagglutination ; Antibodies, Viral
Chemical Substances	Influenza Vaccines ; Antibodies, Viral
Language	English
Publishing date	2023-04-06
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1155880
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Article ; Online: Validation of an automated system for aliquoting of HIV-1 Env-pseudotyped virus stocks.

Schultz, Anke / Germann, Anja / Fuss, Martina / Sarzotti-Kelsoe, Marcella / Ozaki, Daniel A / Montefiori, David C / Zimmermann, Heiko / von Briesen, Hagen

PloS one

2018 Volume 13, Issue 1, Page(s) e0190669

Abstract: The standardized assessments of HIV-specific immune responses are of main interest in the preclinical and clinical stage of HIV-1 vaccine development. In this regard, HIV-1 Env-pseudotyped viruses play a central role for the evaluation of neutralizing ... ...

Abstract	The standardized assessments of HIV-specific immune responses are of main interest in the preclinical and clinical stage of HIV-1 vaccine development. In this regard, HIV-1 Env-pseudotyped viruses play a central role for the evaluation of neutralizing antibody profiles and are produced according to Good Clinical Laboratory Practice- (GCLP-) compliant manual and automated procedures. To further improve and complete the automated production cycle an automated system for aliquoting HIV-1 pseudovirus stocks has been implemented. The automation platform consists of a modified Tecan-based system including a robot platform for handling racks containing 48 cryovials, a Decapper, a tubing pump and a safety device consisting of ultrasound sensors for online liquid level detection of each individual cryovial. With the aim to aliquot the HIV-1 pseudoviruses in an automated manner under GCLP-compliant conditions a validation plan was developed where the acceptance criteria-accuracy, precision as well as the specificity and robustness-were defined and summarized. By passing the validation experiments described in this article the automated system for aliquoting has been successfully validated. This allows the standardized and operator independent distribution of small-scale and bulk amounts of HIV-1 pseudovirus stocks with a precise and reproducible outcome to support upcoming clinical vaccine trials.
MeSH term(s)	Automation ; Cell Line ; Gene Products, env/metabolism ; HIV-1/metabolism ; Humans ; Reproducibility of Results
Chemical Substances	Gene Products, env
Language	English
Publishing date	2018
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Validation Studies
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0190669
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Article ; Online: Optimization and qualification of a functional anti-drug antibody assay for HIV-1 bnAbs.

Seaman, Michael S / Bilska, Miroslawa / Ghantous, Fadi / Eaton, Amanda / LaBranche, Celia C / Greene, Kelli / Gao, Hongmei / Weiner, Joshua A / Ackerman, Margaret E / Garber, David A / Rosenberg, Yvonne J / Sarzotti-Kelsoe, Marcella / Montefiori, David C

Journal of immunological methods

2020 Volume 479, Page(s) 112736

Abstract: The recent identification of human monoclonal antibodies with broad and potent neutralizing activity against HIV-1 (bnAbs) has resulted in substantial efforts to develop these molecules for clinical use in the prevention and treatment of HIV-1 infection. ...

Abstract	The recent identification of human monoclonal antibodies with broad and potent neutralizing activity against HIV-1 (bnAbs) has resulted in substantial efforts to develop these molecules for clinical use in the prevention and treatment of HIV-1 infection. As with any protein therapeutic drug product, it is imperative to have qualified assays that can accurately detect and quantify anti-drug antibodies (ADA) that may develop in patients receiving passive administration of HIV-1 bnAbs. Here, we have optimized and qualified a functional assay to assess the potential of ADA to inhibit the neutralizing function of HIV-1 bnAbs. Using a modified version of the validated TZM-bl HIV-1 neutralization assay, murine anti-idiotype antibodies were utilized to optimize and evaluate parameters of linearity, range, limit of detection, specificity, and precision for measuring inhibitory ADA activity against multiple HIV-1 bnAbs that are in clinical development. We further demonstrate the utility of this assay for detecting naturally occurring ADA responses in non-human primates receiving passive administration of human bnAbs. This functional assay format complements binding-antibody ADA strategies being developed for HIV-1 bnAbs, and when utilized together, will support a multi-tiered approach for ADA testing that is compliant with Good Clinical Laboratory Practice (GCLP) procedures and FDA guidance.
MeSH term(s)	Animals ; Antibodies, Anti-Idiotypic/analysis ; Antibodies, Monoclonal, Murine-Derived/analysis ; Broadly Neutralizing Antibodies/immunology ; Broadly Neutralizing Antibodies/therapeutic use ; HIV Antibodies/immunology ; HIV Antibodies/therapeutic use ; HIV Infections/therapy ; HIV-1/physiology ; Humans ; Mice ; Neutralization Tests/methods
Chemical Substances	Antibodies, Anti-Idiotypic ; Antibodies, Monoclonal, Murine-Derived ; Broadly Neutralizing Antibodies ; HIV Antibodies
Language	English
Publishing date	2020-01-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2020.112736
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Article ; Online: Implementation of a three-tiered approach to identify and characterize anti-drug antibodies raised against HIV-specific broadly neutralizing antibodies.

Bharadwaj, Pranay / Riekofski, Cassidy / Lin, Shu / Seaman, Michael S / Garber, David A / Montefiori, David / Sarzotti-Kelsoe, Marcella / Ackerman, Margaret E / Weiner, Joshua A

Journal of immunological methods

2020 Volume 479, Page(s) 112764

Abstract: The ability to detect, quantify, and interrogate the properties of immune responses raised against biological therapeutics is not only important to our understanding of these molecules, but also to their success in the clinic. A tiered assay approach to ... ...

Abstract	The ability to detect, quantify, and interrogate the properties of immune responses raised against biological therapeutics is not only important to our understanding of these molecules, but also to their success in the clinic. A tiered assay approach to identify the presence, specificity, and titer of anti-drug antibody (ADA) responses has been adopted as a gold standard by industry leaders, the FDA, and the EMA. In order to support pre-clinical and clinical trials, these assays must be standardized, and their performance sufficiently characterized to ensure the accuracy and reproducibility of results under relevant testing conditions. Here we present implementation of electrochemiluminiscence assays that fit into the tiered paradigm of ADA testing for five HIV broadly neutralizing antibodies (3BNC117, 3BNC117-LS, 10-1074, PGT121, and PGDM1400) in compliance with Good Clinical Laboratory practices. Assay sensitivities and matrix effects were evaluated and used to inform the development of positivity cut points. Once cut points were established, assay precision, specificity, free-drug tolerance, and robustness were defined. In all cases, assay characteristics met or surpassed recommendations set forth by the FDA. To further evaluate the performance of these assays and the tiered approach, samples from non-human primates that had received a subset of the five therapeutics were evaluated. In sum, this study reports qualification of a set of ADA assays available to the scientific community as pre-clinical and clinical trials of broadly HIV-neutralizing antibodies proceed, and a framework that is easily adapted as new drug products are advanced in the clinic.
MeSH term(s)	Animals ; Antibodies, Anti-Idiotypic/blood ; Broadly Neutralizing Antibodies/immunology ; Broadly Neutralizing Antibodies/therapeutic use ; Electrochemical Techniques ; HIV Antibodies/immunology ; HIV Antibodies/therapeutic use ; HIV Infections/immunology ; HIV Infections/therapy ; HIV-1/immunology ; Humans ; Immunotherapy/methods ; Luminescent Measurements/methods ; Reference Standards ; Sensitivity and Specificity
Chemical Substances	Antibodies, Anti-Idiotypic ; Broadly Neutralizing Antibodies ; HIV Antibodies
Language	English
Publishing date	2020-02-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2020.112764
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Article ; Online: Validation of a Triplex Pharmacokinetic Assay for Simultaneous Quantitation of HIV-1 Broadly Neutralizing Antibodies PGT121, PGDM1400, and VRC07-523-LS.

Wesley, Martina S / Chiong, Kelvin T / Seaton, Kelly E / Arocena, Christine A / Sawant, Sheetal / Hare, Jonathan / Hernandez, Kasey / Rojas, Michelle / Heptinstall, Jack / Beaumont, David / Crisafi, Katherine / Nkolola, Joseph / Barouch, Dan H / Sarzotti-Kelsoe, Marcella / Tomaras, Georgia D / Yates, Nicole L

Frontiers in immunology

2021 Volume 12, Page(s) 709994

Abstract: The outcome of the recent Antibody Mediated Prevention (AMP) trials that tested infusion of the broadly neutralizing antibody (bnAb) VRC01 provides proof of concept for blocking infection from sensitive HIV-1 strains. These results also open up the ... ...

Abstract	The outcome of the recent Antibody Mediated Prevention (AMP) trials that tested infusion of the broadly neutralizing antibody (bnAb) VRC01 provides proof of concept for blocking infection from sensitive HIV-1 strains. These results also open up the possibility that triple combinations of bnAbs such as PGT121, PGDM1400, as well as long-lasting LS variants such as VRC07-523 LS, have immunoprophylactic potential. PGT121 and PGDM1400 target the HIV-1 V3 and V2 glycan regions of the gp120 envelope protein, respectively, while VRC07-523LS targets the HIV-1 CD4 binding site. These bnAbs demonstrate neutralization potency and complementary breadth of HIV-1 strain coverage. An important clinical trial outcome is the accurate measurement of
MeSH term(s)	Broadly Neutralizing Antibodies/blood ; HIV Antibodies/blood ; HIV-1/immunology ; Humans ; Limit of Detection ; Microspheres ; Reproducibility of Results
Chemical Substances	Broadly Neutralizing Antibodies ; HIV Antibodies
Language	English
Publishing date	2021-08-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Validation Study
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2021.709994
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Article ; Online: Implementation of a responsible conduct of research education program at Duke University School of Medicine.

Simon, Christian / Beerman, Rebecca W / Ariansen, Jennifer L / Kessler, Donna / Sanchez, Ana M / King, Kindra / Sarzotti-Kelsoe, Marcella / Samsa, Gregory / Bradley, Ann / Torres, Laurianne / Califf, Robert / Swamy, Geeta K

Accountability in research

2019 Volume 26, Issue 5, Page(s) 288–310

Abstract: Academic medical centers rarely ... ...

Abstract	Academic medical centers rarely require
MeSH term(s)	Curriculum ; North Carolina ; Program Development ; Schools, Medical ; Scientific Misconduct
Language	English
Publishing date	2019-06-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2069334-5
ISSN	1545-5815 ; 0898-9621
ISSN (online)	1545-5815
ISSN	0898-9621
DOI	10.1080/08989621.2019.1621755
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Article: Implementation of a three-tiered approach to identify and characterize anti-drug antibodies raised against HIV-specific broadly neutralizing antibodies

Bharadwaj, Pranay / Riekofski, Cassidy / Lin, Shu / Seaman, Michael S / Garber, David A / Montefiori, David / Sarzotti-Kelsoe, Marcella / Ackerman, Margaret E / Weiner, Joshua A

Journal of immunological methods. 2020 Apr., v. 479

2020

Abstract	The ability to detect, quantify, and interrogate the properties of immune responses raised against biological therapeutics is not only important to our understanding of these molecules, but also to their success in the clinic. A tiered assay approach to identify the presence, specificity, and titer of anti-drug antibody (ADA) responses has been adopted as a gold standard by industry leaders, the FDA, and the EMA. In order to support pre-clinical and clinical trials, these assays must be standardized, and their performance sufficiently characterized to ensure the accuracy and reproducibility of results under relevant testing conditions. Here we present implementation of electrochemiluminiscence assays that fit into the tiered paradigm of ADA testing for five HIV broadly neutralizing antibodies (3BNC117, 3BNC117-LS, 10–1074, PGT121, and PGDM1400) in compliance with Good Clinical Laboratory practices. Assay sensitivities and matrix effects were evaluated and used to inform the development of positivity cut points. Once cut points were established, assay precision, specificity, free-drug tolerance, and robustness were defined. In all cases, assay characteristics met or surpassed recommendations set forth by the FDA. To further evaluate the performance of these assays and the tiered approach, samples from non-human primates that had received a subset of the five therapeutics were evaluated. In sum, this study reports qualification of a set of ADA assays available to the scientific community as pre-clinical and clinical trials of broadly HIV-neutralizing antibodies proceed, and a framework that is easily adapted as new drug products are advanced in the clinic.
Keywords	Human immunodeficiency virus ; Primates ; clinical trials ; compliance ; drugs ; immune response ; industry ; neutralizing antibodies ; therapeutics
Language	English
Dates of publication	2020-04
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	120142-6
ISSN	1872-7905 ; 0022-1759
ISSN (online)	1872-7905
ISSN	0022-1759
DOI	10.1016/j.jim.2020.112764
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Calibration of two validated SARS-CoV-2 pseudovirus neutralization assays for COVID-19 vaccine evaluation.

Huang, Yunda / Borisov, Oleg / Kee, Jia Jin / Carpp, Lindsay N / Wrin, Terri / Cai, Suqin / Sarzotti-Kelsoe, Marcella / McDanal, Charlene / Eaton, Amanda / Pajon, Rolando / Hural, John / Posavad, Christine M / Gill, Katherine / Karuna, Shelly / Corey, Lawrence / McElrath, M Juliana / Gilbert, Peter B / Petropoulos, Christos J / Montefiori, David C

Scientific reports

2021 Volume 11, Issue 1, Page(s) 23921

Abstract: Vaccine-induced neutralizing antibodies (nAbs) are key biomarkers considered to be associated with vaccine efficacy. In United States government-sponsored phase 3 efficacy trials of COVID-19 vaccines, nAbs are measured by two different validated ... ...

Abstract	Vaccine-induced neutralizing antibodies (nAbs) are key biomarkers considered to be associated with vaccine efficacy. In United States government-sponsored phase 3 efficacy trials of COVID-19 vaccines, nAbs are measured by two different validated pseudovirus-based SARS-CoV-2 neutralization assays, with each trial using one of the two assays. Here we describe and compare the nAb titers obtained in the two assays. We observe that one assay consistently yielded higher nAb titers than the other when both assays were performed on the World Health Organization's anti-SARS-CoV-2 immunoglobulin International Standard, COVID-19 convalescent sera, and mRNA-1273 vaccinee sera. To overcome the challenge this difference in readout poses in comparing/combining data from the two assays, we evaluate three calibration approaches and show that readouts from the two assays can be calibrated to a common scale. These results may aid decision-making based on data from these assays for the evaluation and licensure of new or adapted COVID-19 vaccines.
MeSH term(s)	2019-nCoV Vaccine mRNA-1273/immunology ; Antibodies, Neutralizing/blood ; Antibodies, Viral/blood ; COVID-19/blood ; COVID-19/immunology ; Clinical Decision-Making ; Clinical Trials as Topic ; Diagnostic Tests, Routine ; Humans ; Neutralization Tests/methods ; Neutralization Tests/standards ; SARS-CoV-2/immunology ; World Health Organization
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; 2019-nCoV Vaccine mRNA-1273 (EPK39PL4R4)
Language	English
Publishing date	2021-12-14
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-03154-6
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Article: Calibration of Two Validated SARS-CoV-2 Pseudovirus Neutralization Assays for COVID-19 Vaccine Evaluation.

medRxiv : the preprint server for health sciences

2021

Abstract: Vaccine-induced neutralizing antibodies (nAbs) are key biomarkers considered to be associated with vaccine efficacy. In United States Government-sponsored phase 3 efficacy trials of COVID-19 vaccines, nAbs are measured by two different validated ... ...

Abstract	Vaccine-induced neutralizing antibodies (nAbs) are key biomarkers considered to be associated with vaccine efficacy. In United States Government-sponsored phase 3 efficacy trials of COVID-19 vaccines, nAbs are measured by two different validated pseudovirus-based SARS-CoV-2 neutralization assays, with each trial using one of the two assays. Here we describe and compare the nAb titers obtained in the two assays. We observe that one assay consistently yielded higher nAb titers than the other when both assays were performed on the World Health Organizationâ€™s anti-SARS-CoV-2 immunoglobulin International Standard, COVID-19 convalescent sera, and mRNA-1273 vaccinee sera. To overcome the challenge this difference in readout poses in comparing/combining data from the two assays, we evaluate three calibration approaches and show that readouts from the two assays can be calibrated to a common scale. These results may aid decision-making based on data from these assays for the evaluation and licensure of new or adapted COVID-19 vaccines.
Language	English
Publishing date	2021-09-14
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.09.09.21263049
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Article: Calibration of Two Validated SARS-CoV-2 Pseudovirus Neutralization Assays for COVID-19 Vaccine Evaluation.

Research square

2021

Abstract	Vaccine-induced neutralizing antibodies (nAbs) are key biomarkers considered to be associated with vaccine efficacy. In United States Government-sponsored phase 3 efficacy trials of COVID-19 vaccines, nAbs are measured by two different validated pseudovirus-based SARS-CoV-2 neutralization assays, with each trial using one of the two assays. Here we describe and compare the nAb titers obtained in the two assays. We observe that one assay consistently yielded higher nAb titers than the other when both assays were performed on the World Health Organizationâ€™s anti-SARS-CoV-2 immunoglobulin International Standard, COVID-19 convalescent sera, and mRNA-1273 vaccinee sera. To overcome the challenge this difference in readout poses in comparing/combining data from the two assays, we evaluate three calibration approaches and show that readouts from the two assays can be calibrated to a common scale. These results may aid decision-making based on data from these assays for the evaluation and licensure of new or adapted COVID-19 vaccines.
Language	English
Publishing date	2021-09-02
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-862572/v1
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