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Selected Publication:

Kopecky, EM; Greinstetter, S; Pabinger, I; Buchacher, A; Römisch, J; Jungbauer, A.
(2006): Mapping of FVIII inhibitor epitopes using cellulose-bound synthetic peptide arrays.
J Immunol Methods. 2006; 308(1-2):90-100 FullText FullText_BOKU

Epitope mapping using antibodies against factor VIII (FVIII) has been performed using blotting techniques with truncated and/or digested FVIII molecules. Here, we focused on the precise mapping of affinity purified IgG from patients with an immune response against blood clotting FVIII using synthetic peptide arrays on cellulose membranes comprising the entire sequence of FVIII. The aim was to elucidate the epitope profile from different inhibitors and possibly detect new epitopes, which have not been described before. The epitope patterns from five patients showed reactivity with all domains in the FVIII molecule, but were different between various patients. These results included epitopes usually buried within the folded protein. However, in competition assays using FVIII as competitive agent in a mixture with inhibitor IgG, the most immunogenic regions were located in the FVIII light chain. Our results show that the C1 domain was the region with highest immunogenicity in all patients. Here, we demonstrate that the SPOT method is very well suited for the precise location of epitopes in the core of the protein, which usually cannot be detected by other methods. (c) 2005 Elsevier B.V. All rights reserved.
Authors BOKU Wien:
Jungbauer Alois
Kopecky Eva Maria
Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Antibody Affinity -
Cellulose -
Epitope Mapping - methods
Factor VIII - antagonists & inhibitors
Hemophilia A - blood
Humans - blood
Immunoglobulin G - blood
Male - blood
Peptide Fragments - genetics
Peptide Library - genetics
Recombinant Proteins - genetics

Find related publications in this database (Keywords)
epitope mapping
hemophilia A
inhibitory antibodies
solid phase peptide synthesis

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