Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6020348 | Journal of Neuroimmunology | 2015 | 7 Pages |
Abstract
Myasthenia gravis (MG) is usually caused by antibodies against the muscle acetylcholine receptor (AChR). Plasmapheresis and immunoadsorption are often used to treat non-responsive patients. Antigen-specific immunoadsorption would remove only the pathogenic autoantibodies reducing side-effects. We expressed AChR extracellular domain mutants for use as specific adsorbents, and characterized them. Antigenicity and capacity for autoantibody binding were improved compared to the wild-type proteins. Adsorption appeared to be fast, as high plasma flow-rates could be applied. The bound autoantibodies were eluted repeatedly, allowing column reuse, without compromise in efficiency. Overall, the adsorbents were specific, efficient and suitable for use in therapy.
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Authors
K. Lazaridis, P. Evaggelakou, E. Bentenidi, A. Sideri, E. Grapsa, S.J. Tzartos,