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3 results on '"VIRAL NEUTRALIZATION ASSAY"'

1. Validation of a SARS-CoV-2 Surrogate Neutralization Test Detecting Neutralizing Antibodies against the Major Variants of Concern.

Author

Santos da Silva, Eveline, Servais, Jean-Yves, Kohnen, Michel, Arendt, Vic, Staub, Therese, Krüger, Rejko, Fagherazzi, Guy, Wilmes, Paul, Hübschen, Judith M., Ollert, Markus, Perez-Bercoff, Danielle, and Seguin-Devaux, Carole

Subjects
*NEUTRALIZATION tests, *SARS-CoV-2, *COVID-19 pandemic, *SARS-CoV-2 Omicron variant, *ANTIBODY formation, *MONOCLONAL antibodies, *IMMUNOGLOBULINS
Abstract

SARS-CoV-2 infection and/or vaccination elicit a broad range of neutralizing antibody responses against the different variants of concern (VOC). We established a new variant-adapted surrogate virus neutralization test (sVNT) and assessed the neutralization activity against the ancestral B.1 (WT) and VOC Delta, Omicron BA.1, BA.2, and BA.5. Analytical performances were compared against the respective VOC to the reference virus neutralization test (VNT) and two CE-IVD labeled kits using three different cohorts collected during the COVID-19 waves. Correlation analyses showed moderate to strong correlation for Omicron sub-variants (Spearman's r = 0.7081 for BA.1, r = 0.7205 for BA.2, and r = 0.6042 for BA.5), and for WT (r = 0.8458) and Delta-sVNT (r = 0.8158), respectively. Comparison of the WT-sVNT performance with two CE-IVD kits, the "Icosagen SARS-CoV-2 Neutralizing Antibody ELISA kit" and the "Genscript cPass, kit" revealed an overall good correlation ranging from 0.8673 to −0.8773 and a midway profile between both commercial kits with 87.76% sensitivity and 90.48% clinical specificity. The BA.2-sVNT performance was similar to the BA.2 Genscript test. Finally, a correlation analysis revealed a strong association (r = 0.8583) between BA.5-sVNT and VNT sVNT using a double-vaccinated cohort (n = 100) and an Omicron-breakthrough infection cohort (n = 91). In conclusion, the sVNT allows for the efficient prediction of immune protection against the various VOCs. [ABSTRACT FROM AUTHOR]

Published
2023
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2. Quantifying Absolute Neutralization Titers against SARS-CoV-2 by a Standardized Virus Neutralization Assay Allows for Cross-Cohort Comparisons of COVID-19 Sera

Author

Oguntuyo, Kasopefoluwa, Stevens, Christian S., Hung, Chuan Tien, Ikegame, Satoshi, Acklin, Joshua A., Kowdle, Shreyas S., Carmichael, Jillian C., Chiu, Hsin Ping, Azarm, Kristopher D., Haas, Griffin D., Amanat, Fatima, Klingler, Jéromine, Baine, Ian, Arinsburg, Suzanne, Bandres, Juan C., Siddiquey, Mohammed N. A., Schilke, Robert M., Woolard, Matthew D., Zhang, Hongbo, Duty, Andrew J., Kraus, Thomas A., Moran, Thomas M., Tortorella, Domenico, Lim, Jean K., Gamarnik, Andrea Vanesa, Hioe, Catarina E., Zolla Pazner, Susan, Ivanov, Stanimir S., Kamil, Jeremy, Krammer, Florian, Lee, Benhur, Ojeda, Diego Sebastian, González López Ledesma, María Mora, Costa Navarro, Guadalupe Soledad, Pallarés, H. M., Sanchez, Lautaro Nicolas, Perez, P., Ostrowsk, M., Villordo, S. M., Alvarez, D. E., Caramelo, J. J., Carradori, J., and Yanovsky, M. J.

Subjects
viral neutralization assay, medicine.drug_class, Enzyme-Linked Immunosorbent Assay, SARS-COV-2, Monoclonal antibody, Antibodies, Viral, Microbiology, Virus, Neutralization, Article, NEUTRALIZING ANTIBODIES, purl.org/becyt/ford/1 [https], 03 medical and health sciences, 0302 clinical medicine, Viral entry, Neutralization Tests, Virology, Biosafety level, Potency, Medicine, Humans, neutralizing antibodies, 030212 general & internal medicine, purl.org/becyt/ford/1.6 [https], Neutralizing antibody, 030304 developmental biology, convalescent-phase plasma, 0303 health sciences, biology, business.industry, SARS-CoV-2, fungi, COVID-19, VIRAL NEUTRALIZATION ASSAY, Gold standard (test), biology.organism_classification, Antibodies, Neutralizing, QR1-502, body regions, Titer, Vesicular stomatitis virus, biology.protein, Antibody, business, CONVALESCENT-PHASE PLASMA, Research Article
Abstract

The global coronavirus disease 2019 (COVID-19) pandemic has mobilized efforts to develop vaccines and antibody-based therapeutics, including convalescent-phase plasma therapy, that inhibit viral entry by inducing or transferring neutralizing antibodies (nAbs) against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein (CoV2-S). However, rigorous efficacy testing requires extensive screening with live virus under onerous biosafety level 3 (BSL3) conditions, which limits high-throughput screening of patient and vaccine sera. Myriad BSL2-compatible surrogate virus neutralization assays (VNAs) have been developed to overcome this barrier. Yet, there is marked variability between VNAs and how their results are presented, making intergroup comparisons difficult. To address these limitations, we developed a standardized VNA using CoV2-S pseudotyped particles (CoV2pp) based on vesicular stomatitis virus bearing the Renilla luciferase gene in place of its G glyco-protein (VSVDG); this assay can be robustly produced at scale and generate accurate neutralizing titers within 18 h postinfection. Our standardized CoV2pp VNA showed a strong positive correlation with CoV2-S enzyme-linked immunosorbent assay (ELISA) results and live-virus neutralizations in confirmed convalescent-patient sera. Three independent groups subsequently validated our standardized CoV2pp VNA (n . 120). Our data (i) show that absolute 50% inhibitory concentration (absIC50), absIC80, and absIC90 values can be legitimately compared across diverse cohorts, (ii) highlight the substantial but consistent variability in neutralization potency across these cohorts, and (iii) support the use of the absIC80 as a more meaningful metric for assessing the neutralization potency of a vaccine or convalescent-phase sera. Lastly, we used our CoV2pp in a screen to identify ultrapermissive 293T clones that stably express ACE2 or ACE2 plus TMPRSS2. When these are used in combination with our CoV2pp, we can produce CoV2pp sufficient for 150,000 standardized VNAs/week. IMPORTANCE Vaccines and antibody-based therapeutics like convalescent-phase plasma therapy are premised upon inducing or transferring neutralizing antibodies that inhibit SARS-CoV-2 entry into cells. Virus neutralization assays (VNAs) for measuring neutralizing antibody titers (NATs) are an essential part of determining vaccine or therapeutic efficacy. However, such efficacy testing is limited by the inherent dangers of working with the live virus, which requires specialized high-level biocontainment facilities. We there-fore developed a standardized replication-defective pseudotyped particle system that mimics the entry of live SARS-CoV-2. This tool allows for the safe and efficient measurement of NATs, determination of other forms of entry inhibition, and thorough investigation of virus entry mechanisms. Four independent labs across the globe validated our standardized VNA using diverse cohorts. We argue that a standardized and scalable assay is necessary for meaningful comparisons of the myriad of vaccines and antibody-based therapeutics becoming available. Our data provide generalizable metrics for assessing their efficacy. Fil: Oguntuyo, Kasopefoluwa. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Stevens, Christian S.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Hung, Chuan Tien. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Ikegame, Satoshi. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Acklin, Joshua A.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Kowdle, Shreyas S.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Carmichael, Jillian C.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Chiu, Hsin Ping. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Azarm, Kristopher D.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Haas, Griffin D.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Amanat, Fatima. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Klingler, Jéromine. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Baine, Ian. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Arinsburg, Suzanne. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Bandres, Juan C.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Siddiquey, Mohammed N. A.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Schilke, Robert M.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Woolard, Matthew D.. State University of Louisiana; Estados Unidos Fil: Zhang, Hongbo. State University of Louisiana; Estados Unidos Fil: Duty, Andrew J.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Kraus, Thomas A.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Moran, Thomas M.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Tortorella, Domenico. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Lim, Jean K.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Gamarnik, Andrea Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Hioe, Catarina E.. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Zolla Pazner, Susan. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Ivanov, Stanimir S.. State University of Louisiana; Estados Unidos Fil: Kamil, Jeremy. State University of Louisiana; Estados Unidos Fil: Krammer, Florian. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Lee, Benhur. Icahn School of Medicine at Mount Sinai; Estados Unidos Fil: Ojeda, Diego Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas en Retrovirus y Sida. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas en Retrovirus y Sida; Argentina Fil: González López Ledesma, María Mora. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: Costa Navarro, Guadalupe Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: Pallarés, H. M.. No especifíca; Fil: Sanchez, Lautaro Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: Perez, P.. No especifíca; Fil: Ostrowsk, M.. No especifíca; Fil: Villordo, S. M.. No especifíca; Fil: Alvarez, D. E.. No especifíca; Fil: Caramelo, J. J.. No especifíca; Fil: Carradori, J.. No especifíca; Fil: Yanovsky, M. J.. No especifíca

Published
2021
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3. Identification of envelope protein ORF10 of channel catfish herpesvirus.

Author

Liu, Yulin, Yuan, Junfa, Wang, Weimin, Chen, Xiaoxuan, Tang, Rong, Wang, Min, and Li, Lijuan

Subjects
*CHANNEL catfish, *CHANNEL catfish virus disease, *FISH mortality, *CELL culture, *GLYCOSAMINOGLYCANS, *WESTERN immunoblotting
Abstract

Channel catfish virus (CCV) is a viral pathogen of fry and fingerling channel catfish and can cause significant commercial loss. Previous studies have shown that the CCV virion contains at least 25 predicted structural proteins, including viral protein 10, which is encoded by the orf10 gene of the CCV. In this paper, the orf10 gene was expressed in and used to produce a specific antibody. Western blot analysis confirmed that open reading frame 10 is an envelope protein. A viral neutralization assay demonstrated that open reading frame 10 antiserum was able to inhibit CCV infection of channel catfish ovary cells, suggesting that viral protein 10 is likely to play an important role in the CCV infection of channel catfish ovary cells. [ABSTRACT FROM AUTHOR]

Published
2012
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