Neural Regeneration Research ›› 2014, Vol. 9 ›› Issue (8): 851-856.doi: 10.4103/1673-5374.131611

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Fusion protein of single-chain variable domain fragments for treatment of myasthenia gravis

Fangfang Li, Fanping Meng, Quanxin Jin, Changyuan Sun, Yingxin Li, Honghua Li, Songzhu Jin   

  1. Department of Immunology and Pathogenic Biology, College of Medicine, Yanbian University, Yanji, Jilin Province, China
  • Received:2014-03-01 Online:2014-04-25 Published:2014-04-25
  • Contact: Fanping Meng, Ph.D., Department of Immunology and Pathogenic Biology, College of Medicine, Yanbian University, 977# Gongyuan Road, Yanji 133002, Jilin Province, China, fpmeng@ybu.edu.cn.
  • Supported by:

    This work was supported by the National Natural Science Foundation of China, No. 30360100, 30760234, 30860260, 81160373, 81360458.

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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.

Key words: nerve regeneration, myasthenia gravis, acetylcholine receptor, anti-acetylcholine receptor antibody, single-chain variable domain fragment, human serum albumin, fusion protein, immunosuppressive therapy, autoimmune disease, NSFC grant, neural regeneration