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.
| Title | 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. |
| Publication Type | Journal Article |
| Year of Publication | 2013 |
| Authors | Niarchos, A., Zouridakis M., Douris V., Georgostathi A., Kalamida D., Sotiriadis A., Poulas K., Iatrou K., & Tzartos S. J. |
| Journal | PLoS One |
| Volume | 8 |
| Issue | 12 |
| Pagination | e84791 |
| Date Published | 2013 |
| ISSN | 1932-6203 |
| Keywords | Animals, 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. |
| DOI | 10.1371/journal.pone.0084791 |
| Alternate Journal | PLoS ONE |
| PubMed ID | 24376846 |
| PubMed Central ID | PMC3869910 |
