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  1. Article: A Pseudovirus-Based Neutralization Assay for SARS-CoV-2 Variants: A Rapid, Cost-Effective, BSL-2-Based High-Throughput Assay Useful for Vaccine Immunogenicity Evaluation.

    Cai, Zhaohui / Kalkeri, Raj / Zhu, Mingzhu / Cloney-Clark, Shane / Haner, Benjamin / Wang, Mi / Osman, Bahar / Dent, Dominic / Feng, Sheau-Line / Longacre, Zach / Glenn, Greg / Plested, Joyce S

    Microorganisms

    2024  Volume 12, Issue 3

    Abstract: Neutralizing antibody responses from COVID-19 vaccines are pivotal in conferring protection against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Effective COVID-19 vaccines and assays measuring neutralizing antibodies against emerging ... ...

    Abstract Neutralizing antibody responses from COVID-19 vaccines are pivotal in conferring protection against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Effective COVID-19 vaccines and assays measuring neutralizing antibodies against emerging variants (i.e., XBB.1.5, XBB.1.16, and XBB.2.3) are needed. The use of biosafety level (BSL)-3 laboratories for live virus assays results in higher costs and a longer turnaround time; therefore, a BSL-2-based pseudovirus neutralization assay (PNT) was developed. The pseudoviruses were produced by cotransfecting cells with plasmids encoding a lentiviral backbone-expressing luciferase reporter; non-surface proteins for lentiviral production; and ancestral or Omicron (BA.1 and BA.5) SARS-CoV-2 spike (S) proteins. The PNT was developed and optimized in dose and kinetics experiments. The representative serum samples (COVID-19-convalescent or NVX-CoV2373-vaccinated participants enrolled in the 2019nCoV-101 trial) demonstrated a wide dynamic range. The neutralization data showed robust correlation with validated anti-recombinant spike IgG levels and angiotensin-converting enzyme 2 inhibition titers (ancestral). This assay is suitable for measurement of the neutralization ability in clinical samples from individuals infected with SARS-CoV-2 or immunized with a COVID-19 vaccine. The results suggest that this PNT provides a lower cost, high-throughput, rapid turnaround alternative to BSL-3-based microneutralization assays and enables the discovery and development of effective vaccines against emerging variants.
    Language English
    Publishing date 2024-02-29
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms12030501
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: A Severe Acute Respiratory Syndrome Coronavirus 2 Anti-Spike Immunoglobulin G Assay: A Robust Method for Evaluation of Vaccine Immunogenicity Using an Established Correlate of Protection.

    Zhu, Mingzhu / Cloney-Clark, Shane / Feng, Sheau-Line / Parekh, Anand / Gorinson, Drew / Silva, David / Skonieczny, Paul / Wilson, Adjele / Kalkeri, Raj / Woo, Wayne / Cai, Miranda R / Fries, Louis / Glenn, Greg / Plested, Joyce S

    Microorganisms

    2023  Volume 11, Issue 7

    Abstract: As the COVID-19 pandemic continues, variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continue to emerge. Immunogenicity evaluation of vaccines and identification of correlates of protection for vaccine effectiveness is critical to ...

    Abstract As the COVID-19 pandemic continues, variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continue to emerge. Immunogenicity evaluation of vaccines and identification of correlates of protection for vaccine effectiveness is critical to aid the development of vaccines against emerging variants. Anti-recombinant spike (rS) protein immunoglobulin G (IgG) quantitation in the systemic circulation (serum/plasma) is shown to correlate with vaccine efficacy. Thus, an enzyme-linked immunosorbent assay (ELISA)-based binding assay to detect SARS-CoV-2 (ancestral and variant strains) anti-rS IgG in human serum samples was developed and validated. This assay successfully met acceptance criteria for inter/intra-assay precision, specificity, selectivity, linearity, lower/upper limits of quantitation, matrix effects, and assay robustness. The analyte in serum was stable for up to 8 freeze/thaw cycles and 2 years in -80 °C storage. Similar results were observed for the Beta, Delta, and Omicron BA.1/BA.5/XBB.1.5 variant-adapted assays. Anti-rS IgG assay results correlated significantly with neutralization and receptor binding inhibition assays. In addition, usage of international reference standards allows data extrapolation to WHO international units (BAU/mL), facilitating comparison of results with other IgG assays. This anti-rS IgG assay is a robust, high-throughput method to evaluate binding IgG responses to S protein in serum, enabling rapid development of effective vaccines against emerging COVID-19 variants.
    Language English
    Publishing date 2023-07-11
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720891-6
    ISSN 2076-2607
    ISSN 2076-2607
    DOI 10.3390/microorganisms11071789
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: The Fn14 cytoplasmic tail binds tumour-necrosis-factor-receptor-associated factors 1, 2, 3 and 5 and mediates nuclear factor-kappaB activation.

    Brown, Sharron A N / Richards, Christine M / Hanscom, Heather N / Feng, Sheau-Line Y / Winkles, Jeffrey A

    The Biochemical journal

    2003  Volume 371, Issue Pt 2, Page(s) 395–403

    Abstract: Fn14 is a growth-factor-inducible immediate-early-response gene encoding a 102-amino-acid type I transmembrane protein. The human Fn14 protein was recently identified as a cell-surface receptor for the tumour necrosis factor (TNF) superfamily member ... ...

    Abstract Fn14 is a growth-factor-inducible immediate-early-response gene encoding a 102-amino-acid type I transmembrane protein. The human Fn14 protein was recently identified as a cell-surface receptor for the tumour necrosis factor (TNF) superfamily member named TWEAK (TNF-like weak inducer of apoptosis). In the present paper, we report that the human TWEAK extracellular domain can also bind the murine Fn14 protein. Furthermore, site-specific mutagenesis and directed yeast two-hybrid interaction assays revealed that the TNFR-associated factor (TRAF) 1, 2, 3 and 5 adaptor molecules bind the murine Fn14 cytoplasmic tail at an overlapping, but non-identical, amino acid sequence motif. We also found that TWEAK treatment of quiescent NIH 3T3 cells stimulates inhibitory kappaBalpha phosphorylation and transcriptional activation of a nuclear factor-kappaB (NF-kappaB) enhancer/luciferase reporter construct. Fn14 overexpression in transiently transfected NIH 3T3 cells also promotes NF-kappaB activation, and this cellular response requires an intact TRAF binding site. These results indicate that Fn14 is a functional TWEAK receptor that can associate with four distinct TRAF family members and stimulate the NF-kappaB transcription factor signalling pathway.
    MeSH term(s) 3T3 Cells ; Animals ; Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/metabolism ; Cell Line ; Cloning, Molecular ; Cytokine TWEAK ; Cytoplasm/metabolism ; Genes, Reporter ; Genetic Vectors ; Humans ; Luciferases/genetics ; MAP Kinase Signaling System/physiology ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mice ; NF-kappa B/metabolism ; Plasmids ; Protein Binding ; Proteins/chemistry ; Proteins/metabolism ; Receptors, Tumor Necrosis Factor ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Spodoptera ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; TNF Receptor-Associated Factor 3 ; TNF Receptor-Associated Factor 5 ; TWEAK Receptor ; Transfection ; Tumor Necrosis Factors
    Chemical Substances Apoptosis Regulatory Proteins ; Carrier Proteins ; Cytokine TWEAK ; Membrane Proteins ; NF-kappa B ; Proteins ; Receptors, Tumor Necrosis Factor ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; TNF Receptor-Associated Factor 3 ; TNF Receptor-Associated Factor 5 ; TNFRSF12A protein, human ; TNFSF12 protein, human ; TWEAK Receptor ; Tnfrsf12a protein, mouse ; Tnfsf12 protein, mouse ; Tumor Necrosis Factors ; Luciferases (EC 1.13.12.-)
    Language English
    Publishing date 2003-04-15
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
    ISSN (online) 1470-8728
    ISSN 0264-6021 ; 0006-2936 ; 0306-3275
    DOI 10.1042/BJ20021730
    Database MEDical Literature Analysis and Retrieval System OnLINE

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