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Immunoaffinity Purification and Characterization of Specific Antibodies against Recombinant Tau Protein from Intravenous Immunoglobulin Product
Authors: Hromádková Lenka | Kolářová Michala | Jankovičová Barbora | Bartoš Aleš | Říčný Jan | Bílková Zuzana | Řípová Daniela
Year: 2014
Type of publication: ostatní - přednáška nebo poster
Name of source: Journal of Neuroimmunology
Publisher name: Elsevier Science BV
Place: Amsterdam
Page from-to: nestránkováno
Titles:
Language Name Abstract Keywords
eng Immunoaffinity Purification and Characterization of Specific Antibodies against Recombinant Tau Protein from Intravenous Immunoglobulin Product There is evidence that humoral immunity is involved in some processes associated with neurodegenerative diseases. Antibodies against many molecules occurring predominantly in brain tissue are detected also in cerebrospinal fluid as well as in plasma and serum. One of these molecules is tau protein, the integral component of paired helical filaments which were identified as the major part of neurofibrillary pathology in Alzheimer´s disease (AD). It is also known that specific antibodies against tau protein are contained in intravenous immunoglobulin (IVIG) products. IVIG was the first attempt to use multiple antibodies to treat AD, but different IVIG preparations provide various results in pilot studies. The characterization of antibodies found in these preparations can help to better understand of their benefits in AD treatment. We focused on isolation of specific antibodies against recombinant tau protein from IVIG product (Flebogamma) by immunoaffinity chromatography in a column arrangement. Two immunosorbents differing by type of antigens and solid phase were applied. In both approaches, immunocaptured specific antibodies were eluted by 0.1M glycine-HCl buffer pH 2.6. These affinity-purified antibodies were consequently characterized by blotting techniques and ELISA method in terms of their reactivity and affinity with the different tau molecules (Tau-441 and its truncated forms). In conclusion, we were able to isolate specific antibodies against Tau protein from IVIG product Flebogamma and characterize them by using techniques based on the immunocomplex formation. The isolation and characterization of antibodies against recombinant tau protein, especially their reactivity and affinity against different tau molecules, could be beneficial not only for use IVIG preparations as a potential multiple antibody therapy for AD, but also for the application of defined antibodies in immunochemical methods within neurodegenerative diseases' research. Tau protein; Alzheimer´s disease; intravenous immunoglobulin; immunoaffinity chromatography; blotting techniques; ELISA

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