| 
 
 |  | 
						
							
								
									| 基本情報 |   |  
							
								| 氏名 | 二見 翠 |  
								| 氏名(カナ) | フタミ ミドリ |  
								| 氏名(英語) | Futami Midori |  
								| 所属 | 生命科学部 生物科学科 |  
								| 職名 | 准教授 |  
								| researchmap研究者コード | B000345493 |  
								| researchmap機関 | 岡山理科大学 |  
						
							Sterilizable autoantigen immobilized column platform for broad-spectrum removal of pathogenic autoantibodies in autoimmune diseases
 
						
							Midori Futami,  Eri Kurozumi,  Masaya Kamo,  Soudai Taguchi,  Tomoaki Nakai,  Junichiro Futami 
						
							
								
									|  |  |  Blood purification using immunoadsorbent columns is a therapeutic strategy for removing pathogenic autoantibodies in autoimmune diseases. Currently available columns have limitations: Trp/Phe columns offer cost-effectiveness and sterilizability, but lack antigen specificity and have limited capacity to remove diverse pathogenic autoantibodies; whereas Protein A/peptide/anti-human IgG columns target all antibodies, regardless of pathogenicity, limiting specificity, and often require sterile production due to low stability under sterilization conditions, except for peptide ligands. Full-length autoantigen-immobilized immunoadsorbent columns have great potential to specifically adsorb targeted autoantibodies, because autoantibodies recognize diverse epitopes that vary among individuals. However, it is challenging to prepare biologically active autoantigens on a large scale and maintain the quality of antigen-immobilized columns after sterilization. This study introduced a novel approach for preparing sterilizable antigen-immobilized columns that target autoantibodies, excluding those with conformational epitope specificity. Two type I transmembrane protein-coding extracellular domains associated with autoimmunity and their rabbit antisera were used as models. Recombinant human contactin-associated protein-like 2 (Caspr2) and muscle-specific tyrosine-protein kinase receptor (MuSK) were expressed as bacterial inclusion bodies. These compounds were solubilized and purified using Cys-specific chemical cationization. Columns immobilized with water-soluble S-cationized Caspr2 or MuSK effectively captured specific antibodies from rabbit antisera against each antigen, retaining their capacity after standard sterilization. This approach offers a promising solution for developing immunoadsorbent columns with enhanced specificity and sterilizability and is applicable to various autoantibody-related disorders. 
						
							Journal of Bioscience and Bioengineering
 
						
							10.1016/j.jbiosc.2025.08.007 |