ArticleClinical biochemistry2022
Analytical characterization of the SARS-CoV-2 EURM-017 reference material.
Article in Clinical biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Post-Hoc Analysis of Potential Correlates of Protection of a Recombinant SARS-CoV-2 Spike Protein Extracellular Domain Vaccine Formulated with Advax-CpG55.2-Adjuvant.International journal of molecular sciences · 2024Trial
- Application of a Biomimetic Nanoparticle-Based Mock Virus to Determine SARS-CoV-2 Neutralizing Antibody Levels in Blood Samples Using a Lateral Flow Assay.Analytical chemistry · 2024Article
- A bead-based multiplex assay covering all coronaviruses pathogenic for humans for sensitive and specific surveillance of SARS-CoV-2 humoral immunity.Scientific reports · 2023Article
- Vaccine-induced SARS-CoV-2 antibody response: the comparability of S1-specific binding assays depends on epitope and isotype discrimination.Frontiers in immunology · 2023Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCurrent serological methods for SARS-CoV-2 lack adequate standardization to a universal standard reference material. Standardization will allow comparison of results across various lab-developed and commercial assays and publications. SARS-CoV-2 EURM-017 is human sera reference material containing antibodies directed against SARS-CoV-2 proteins, S1/S2 (full-length spike [S]), S1 receptor-binding domain (S1 RBD), S1, S2, and nucleocapsid (N) protein. The goal of this study was to characterize five antigen-specific serum fractions in EURM-017 for standardization of serology assays.
methodsFive antigen-specific serum fractions were affinity purified, quantified, and PRNT
resultsAnti-sera protein content was as follows: S1 (17.7 µg/mL), S1 RBD (17.4 µg/mL), S1/S2 (full-length S) (34.1 µg/mL), S2 (29.7 µg/mL), and N protein (72.5 µg/mL). S1 anti-serum had the highest neutralization activity. A standardization method for S1 RBD anti-serum and an anti-S1 RBD IgG assay yielded the linear equation (y = 0.75x-0.10; y = index, x=µg/mL anti-serum). Patient sample index values for the S1-RBD IgG assay correlated well with PRNT
conclusionsStandardization of different lab-developed and commercial assays to EURM-017 antigen-specific anti-sera will allow comparison of results across studies globally due to traceability to a single standard reference material.
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Registered trials
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