Affiliations: [a] Department of Neurology, Philipps-University, Marburg, Germany | [b] Department of Neuroanatomy, University of Bonn, Bonn, Germany | [c] Department of Microbiology, Philipps-University, Marburg, Germany | [d] Department of Chemistry and Biotechnology, Aachen University of Applied Sciences, Jülich, Germany
Correspondence:
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Correspondence to: Richard Dodel, MD, Department of Neurology, Philipps-University Marburg, Rudolf-Bultmann str. 8, 35039 Marburg, Germany. Tel.: +49 6421 586 6251; Fax: +39 6421 586 5474; E-mail: [email protected].
Abstract: Intravenous immunoglobulins (IVIG) are currently used for therapeutic purposes in autoimmune disorders. Recently, we demonstrated the presence of naturally occurring antibodies against amyloid-β (nAbs-Aβ) within the pool of IVIG. In this study, we compared different brands of IVIG for nAbs-Aβ and have found differences in the specificity of the nAbs-Aβ towards Aβ1–40 and Aβ1–42. We analyzed the influence of a pH-shift over the course of antibody storage using ELISA and investigated antibody dimerization at acidic and neutral pH as well as differences in the IgG subclass distributions among the IVIG using both HPLC and a nephelometric assay. Furthermore, we investigated the epitope region of purified nAbs-Aβ. The differences found in Aβ specificity are not directly proportionate to the binding nature of these antibodies when administered in vivo. This information, however, may serve as a guide when choosing the commercial source of IVIG for therapeutic applications in Alzheimer's disease.
Keywords: Alzheimer's disease, amyloid-β specific nAbs, immunotherapy for AD, IVIG
