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KMID : 0364820110470040328
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Korean Journal of Microbiology
2011 Volume.47 No. 4 p.328 ~ p.334
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The Development of Dimerized Chicken Recombinant Single-chain Fv (ScFv) Antibody Using Leucine Zipper Motif
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Park Dong-Woon
Kim Eon-Dong
Kim Sung-Heon
Han Jae-Yong
Kim Jin-Kyu
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Abstract
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Leucine zipper motif consists of multiple periodic leucine residues, which forms amphipathic alpha helix. The hydrophobic nature of leucine zipper motif can dimerize proteins which contain this motif. Leucine zipper motif addition at C-terminus of single-chain Fv (ScFv) antibody induces its dimerization. Since the dimeric ScFv antibody contains two antigen binding sites (bivalency) like Y-shaped complete antibody, it could increase avidity. As a result, it could show higher antigen binding activity than monomeric ScFv antibodies. Based on this concept, monomeric chicken 8C3 ScFv antibody reviously developed from chicken hybridoma was dimerized by the addition of leucine zipper motif at C-terminus of ScFv antibody. The dimeric 8C3 ScFv antibody specifically reacted with Eimerian sporozoite which causes Avian Coccidiosis. As expected, dimeric 8C3 ScFv antibody showed 3-folds higher antigen binding activity than monomer due to increased avidity. In addition, protien yields of dimer expression were 2-folds higher than monomer.
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KEYWORD
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avidity, dimer, leucine zipper motif, single-chain Fv antibody
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