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Expression of a Highly Antigenic and Native-Like Folded Extracellular Domain of the Human α1 Subunit of Muscle Nicotinic Acetylcholine Receptor, Suitable for Use in Antigen Specific Therapies for Myasthenia Gravis
Author(s) -
Athanasios Niarchos,
Marios Zouridakis,
Vassilis Douris,
Assimina Georgostathi,
Dimitra Kalamida,
Alexandros Sotiriadis,
Konstantinos Poulas,
Kostas Iatrou,
Socrates J. Tzartos
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0084791
Subject(s) - nicotinic acetylcholine receptor , acetylcholine receptor , myasthenia gravis , antigen , autoantibody , acetylcholine , epitope , extracellular , monoclonal antibody , microbiology and biotechnology , receptor , chemistry , antibody , biology , immunology , biochemistry , pharmacology
We describe the expression of the extracellular domain of the human α1 nicotinic acetylcholine receptor (nAChR) in lepidopteran insect cells (i-α1-ECD) and its suitability for use in antigen-specific therapies for Myasthenia Gravis (MG). Compared to the previously expressed protein in P. pastoris (y-α1-ECD), i - α1 - ECD had a 2-fold increased expression yield, bound anti-nAChR monoclonal antibodies and autoantibodies from MG patients two to several-fold more efficiently and resulted in a secondary structure closer to that of the crystal structure of mouse α1-ECD. Our results indicate that i - α1 - ECD is an improved protein for use in antigen-specific MG therapeutic strategies.

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