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Identification and characterization of natural antibodies against tau protein in an intravenous immunoglobulin product

L. Hromadkova, M. Kolarova, B. Jankovicova, A. Bartos, J. Ricny, Z. Bilkova, D. Ripova,

. 2015 ; 289 (-) : 121-9. [pub] 20151028

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc16009902

The latest therapeutic approaches to Alzheimer disease are using intravenous immunoglobulin (IVIG) products. Therefore, the detailed characterization of target-specific antibodies naturally occurring in IVIG products is beneficial. We have focused on characterization of antibodies isolated against tau protein, a biomarker of Alzheimer's disease, from Flebogamma IVIG product. The analysis of IgG subclass distribution indicated skewing toward IgG3 in anti-tau-enriched IgG fraction. The evaluation of their reactivity and avidity with several recombinant tau forms was performed by ELISA and blotting techniques. Truncated non-phosphorylated tau protein (amino acids 155-421) demonstrated the highest reactivity and avidity index. We provide the first detailed insight into the reactivity of isolated natural antibodies against tau protein.

Citace poskytuje Crossref.org

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$a Hromadkova, Lenka $u Department of Neurobiology, AD Center, National Institute of Mental Health, Klecany, Czech Republic; Faculty of Science, Charles University in Prague, Prague, Czech Republic; Department of Biological and Biochemical Sciences, University of Pardubice, Pardubice, Czech Republic.
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$a The latest therapeutic approaches to Alzheimer disease are using intravenous immunoglobulin (IVIG) products. Therefore, the detailed characterization of target-specific antibodies naturally occurring in IVIG products is beneficial. We have focused on characterization of antibodies isolated against tau protein, a biomarker of Alzheimer's disease, from Flebogamma IVIG product. The analysis of IgG subclass distribution indicated skewing toward IgG3 in anti-tau-enriched IgG fraction. The evaluation of their reactivity and avidity with several recombinant tau forms was performed by ELISA and blotting techniques. Truncated non-phosphorylated tau protein (amino acids 155-421) demonstrated the highest reactivity and avidity index. We provide the first detailed insight into the reactivity of isolated natural antibodies against tau protein.
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$a Kolarova, Michala $u Department of Neurobiology, AD Center, National Institute of Mental Health, Klecany, Czech Republic; Third Faculty of Medicine, Charles University in Prague, Prague, Czech Republic. Electronic address: michala.kolarova@nudz.cz.
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$a Jankovicova, Barbora $u Department of Biological and Biochemical Sciences, University of Pardubice, Pardubice, Czech Republic.
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$a Bartos, Ales $u Department of Neurobiology, AD Center, National Institute of Mental Health, Klecany, Czech Republic; Third Faculty of Medicine, Charles University in Prague, Prague, Czech Republic.
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$a Ricny, Jan $u Department of Neurobiology, AD Center, National Institute of Mental Health, Klecany, Czech Republic.
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$a Bilkova, Zuzana $u Department of Biological and Biochemical Sciences, University of Pardubice, Pardubice, Czech Republic.
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$a Ripova, Daniela $u Department of Neurobiology, AD Center, National Institute of Mental Health, Klecany, Czech Republic.
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