Δημοσίευση

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.

ΤίτλοςExpression 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.
Publication TypeJournal Article
Year of Publication2013
AuthorsNiarchos, A., Zouridakis M., Douris V., Georgostathi A., Kalamida D., Sotiriadis A., Poulas K., Iatrou K., & Tzartos S. J.
JournalPLoS One
Volume8
Issue12
Paginatione84791
Date Published2013
ISSN1932-6203
Λέξεις κλειδιάAnimals, Autoantibodies, Blotting, Western, Bungarotoxins, Cell Line, Circular Dichroism, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Epitopes, Humans, Immunosorbent Techniques, Iodine Radioisotopes, Moths, Muscle, Skeletal, Myasthenia Gravis, Pichia, Plasmids, Protein Structure, Tertiary, Radioimmunoassay, Receptors, Nicotinic
Abstract

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.

DOI10.1371/journal.pone.0084791
Alternate JournalPLoS ONE
PubMed ID24376846
PubMed Central IDPMC3869910

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