

|
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基本情報 |
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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
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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
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