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Fusion protein of single-chain variable domain fragments for treatment of myasthenia gravis
Authors:Fangfang Li  Fanping Meng  Quanxin Jin  Changyuan Sun  Yingxin Li  Honghua Li  Songzhu Jin
Institution:Department of Immunology and Pathogenic Biology, College of Medicine, Yanbian University, Yanji, Jilin Province, China
Abstract:Single-chain variable domain fragment (scFv) 637 is an antigen-specific scFv of myasthenia gravis. In this study, scFv and human serum albumin genes were conjugated and the fusion protein was expressed in Pichia pastoris. The affinity of scFv-human serum albumin fusion protein to bind to acetylcholine receptor at the neuromuscular junction of human intercostal muscles was detected by immunofluorescence staining. The ability of the fusion protein to block myasthenia gravis patient sera binding to acetylcholine receptors and its stability in healthy serum were measured by competitive ELISA. The results showed that the inhibition rate was 2.0-77.4%, and the stability of fusion protein in static healthy sera was about 3 days. This approach suggests the scFv-human serum albumin is a potential candidate for specific immunosuppressive therapy of myasthenia gravis.
Keywords:nerve regeneration  myasthenia gravis  acetylcholine receptor  anti-acetylcholine re-ceptor antibody  single-chain variable domain fragment  human serum albumin  fusion protein  immunosuppressive therapy  autoimmune disease  NSFC grant  neural regeneration
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