Effect of IVIG Formulation on IgG Binding to Self- and Exo- Antigens In Vitro and In Vivo
| Autor: | Sylvia Miescher, Reinhard Bolli, Marc W. Nolte, Alain Kropf, Susann Cattepoel, Annette Gaida |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Bacterial Diseases Herpesvirus 3 Human Physiology Antibody Affinity lcsh:Medicine Toxicology Pathology and Laboratory Medicine Biochemistry Autoantigens Immunoglobulin G Binding Analysis 0302 clinical medicine Immune Physiology Medicine and Health Sciences Tetanus Toxoid Toxins Enzyme-Linked Immunoassays Amino Acids lcsh:Science Multidisciplinary Immune System Proteins biology Chemistry Organic Compounds Toxoid Immunoglobulins Intravenous Hematology Toxoids Body Fluids Infectious Diseases Blood IgG binding Physical Sciences Female Antibody Anatomy Research Article Protein Binding Proline Immunology Toxic Agents Bacterial Toxins Glycine Enzyme-Linked Immunosorbent Assay Research and Analysis Methods Antibodies Blood Plasma 03 medical and health sciences Antigen In vivo Alzheimer Disease Potency Animals Humans Antigens Immunoassays Chemical Characterization Tetanus Amyloid beta-Peptides lcsh:R Organic Chemistry Chemical Compounds Biology and Life Sciences Proteins Cyclic Amino Acids Molecular biology In vitro Actins Peptide Fragments Rats 030104 developmental biology Aliphatic Amino Acids biology.protein Immunologic Techniques lcsh:Q 030217 neurology & neurosurgery |
| Zdroj: | PLoS ONE PLoS ONE, Vol 11, Iss 8, p e0161826 (2016) |
| ISSN: | 1932-6203 |
| Popis: | In relation to the recent trials of Intravenous Immunoglobulin (IVIG) in Alzheimer's Disease (AD) it was demonstrated that different IgG preparations contain varying amounts of natural anti-amyloid β (Aβ) antibodies as measured by ELISA. We therefore investigated the relevance of ELISA data for measuring low-affinity antibodies, such as anti-Aβ. We analysed the binding of different commercial Immunoglobulin G (IgG) preparations to Aβ, actin and tetanus toxoid in different binding assays to further investigate the possible cause for observed differences in binding to Aβ and actin between different IgG preparations. We show that the differences of commercial IgG preparations in binding to Aβ and actin in ELISA assays are artefactual and only evident in in vitro binding assays. In functional assays and in vivo animal studies the different IVIG preparations exhibited very similar potency. ELISA data alone are not appropriate to analyse and rank the binding capacity of low-affinity antibodies to Aβ or other endogenous self-antigens contained in IgG preparations. Additional analytical methods should be adopted to complement ELISA data. |
| Databáze: | OpenAIRE |
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