A New SARS-CoV-2 Dual-Purpose Serology Test: Highly Accurate Infection Tracing and Neutralizing Antibody Response Detection
Top Cited Papers
Open Access
- 19 March 2021
- journal article
- research article
- Published by American Society for Microbiology in Journal of Clinical Microbiology
- Vol. 59 (4)
- https://doi.org/10.1128/jcm.02438-20
Abstract
Many severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) serology tests have proven to be less accurate than expected and do not assess antibody function as neutralizing, correlating with protection from reinfection. A new assay technology measuring the interaction of the purified SARS-CoV-2 spike protein receptor binding domain (RBD) with the extracellular domain of the human angiotensin-converting enzyme 2 (hACE2) receptor detects these important antibodies.Keywords
This publication has 43 references indexed in Scilit:
- First international external quality assessment of molecular diagnostics for Mers-CoVJournal of Clinical Virology, 2015
- Atomic force microscopy analysis of IgG films at hydrophobic surfaces: A promising method to probe IgG orientations and optimize ELISA tests performanceBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015
- Variability in Dengue Titer Estimates from Plaque Reduction Neutralization Tests Poses a Challenge to Epidemiological Studies and Vaccine DevelopmentPLoS Neglected Tropical Diseases, 2014
- Non-specific binding in solid phase immunoassays for autoantibodies correlates with inflammation markersJournal of Immunological Methods, 2014
- A Virus-Binding Hot Spot on Human Angiotensin-Converting Enzyme 2 Is Critical for Binding of Two Different CoronavirusesJournal of Virology, 2011
- Potent and persistent antibody responses against the receptor-binding domain of SARS-CoV spike protein in recovered patientsVirology Journal, 2010
- Protein Adsorption on a Hydrophobic Surface: A Molecular Dynamics Study of Lysozyme on GraphiteLangmuir, 2009
- Protein Structural Perturbation and Aggregation on Homogeneous SurfacesBiophysical Journal, 2005
- In patients with rheumatoid arthritis IgG binding to denatured collagen type II is in part mediated by IgG-fibronectin complexes.The Journal of Immunology, 1997
- Changing activity of ribonuclease A during adsorption: a molecular explanation.Proceedings of the National Academy of Sciences of the United States of America, 1989