BACKGROUND: The binding of anti-acetylcholine receptor antibodies (AChRAb) to the main immunogenic region (MIR) of AChR alpha-subunit in the neuromuscular junction is the major pathogenesis of myasthenia gravis (MG). METHODS: A synthetic peptide of 10 amino acids corresponding to the MIR of human AChR was coupled with cellulose beads to make an antigen-specific immunoadsorbent (hMIR10-CB). RESULTS: The hMIR10-CB could remove AChRAb in MG sera by 40.3+/-2.3%, compared to a tryptophan nonspecific adsorbent Trp-CB by only 22.4+/-1.5% as determined in ELISA, and also showed good blood compatibility for blood cells, plasma ions and plasma proteins as checked in whole blood perfusion in rabbits. CONCLUSIONS: The antigen-specific immunoadsorbent hMIR10-CB can serve as a potential candidate in the immunoadsorption treatment of MG.
BACKGROUND: The binding of anti-acetylcholine receptor antibodies (AChRAb) to the main immunogenic region (MIR) of AChR alpha-subunit in the neuromuscular junction is the major pathogenesis of myasthenia gravis (MG). METHODS: A synthetic peptide of 10 amino acids corresponding to the MIR of human AChR was coupled with cellulose beads to make an antigen-specific immunoadsorbent (hMIR10-CB). RESULTS: The hMIR10-CB could remove AChRAb in MG sera by 40.3+/-2.3%, compared to a tryptophan nonspecific adsorbent Trp-CB by only 22.4+/-1.5% as determined in ELISA, and also showed good blood compatibility for blood cells, plasma ions and plasma proteins as checked in whole blood perfusion in rabbits. CONCLUSIONS: The antigen-specific immunoadsorbent hMIR10-CB can serve as a potential candidate in the immunoadsorption treatment of MG.