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Protective effect of scFv‐DAF fusion protein on the complement attack to acetylcholine receptor: A possible option for treatment of myasthenia gravis
Author(s) -
Song Chen,
Xu Zhikai,
Miao Jianting,
Xu Jiang,
Wu Xingan,
Zhang Fanglin,
Lin Hong,
Li Zhuyi,
Kaminski Henry J.
Publication year - 2012
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.23247
Subject(s) - complement system , decay accelerating factor , acetylcholine receptor , in vitro , recombinant dna , antibody , chemistry , in vivo , myasthenia gravis , complement factor b , receptor , fusion protein , complement factor i , microbiology and biotechnology , autoantibody , biology , biochemistry , immunology , gene
Abstract Introduction: Autoantibody‐induced complement activation, which causes disruption of the postsynaptic membrane, is recognized as a key pathogenic factor in myasthenia gravis (MG). Therefore, specific targeting of complement inhibitors to the site of complement activation is a potential therapeutic strategy for treatment of MG. Methods: We assessed expression of single‐chain antibody fragment–decay accelerating factor (scFv‐DAF), comprising a single‐chain fragment scFv1956 based on the rat complement inhibitor DAF in prokaryotic systems, and studied its inhibitory effect on complement deposition in vitro . Results: The recombinant conjugate scFv‐DAF completely retained the wild‐type binding activity of scFv1956 to AChR and inhibited complement activation of DAF in vitro . Conclusions: We found that scFv‐DAF could bind specifically to TE671 cells, and it is significantly more potent at inhibiting complement deposition than the untargeted parent molecule DAF. scFv‐DAF may be a candidate for in vivo protection of the AChR in MG. Muscle Nerve, 2012

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