| Engineering human interferon α1c/86D with phage display technology |
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| 引用本文： | 马学军
,胡荣
,吕海
,魏开坤
,张丽兰
,薛水星
,侯云德.Engineering human interferon α1c/86D with phage display technology[J].中国科学：生命科学英文版,1999(2). |
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| 作者姓名： | 马学军 胡荣 吕海 魏开坤 张丽兰 薛水星 侯云德 |
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| 作者单位： | . State Key Laboratory for Molecular Virology and Genetic Engineering，Beijing 100052，China; . Dalian Medical University，Dalian 116027，China; The First Military Medical College，Guangzhou 510515，China |
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| 基金项目： | Project supported by the China National Expert Committee for Biotechnology Development. |
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| 摘 要： | Human interferon-α1c/86D (IFNα1c/86D) was functionally displayed on the surface of the filamentous bacteriophage using a phagemid vector system (pCANTAB5E). The key amino acid residues involved in the receptor binding were further defined with phage displayed 6-mer peptide library and two neutralizing antibodies against linear epitopes on the IFN-α1b, indicating that residues 30, 33, 34, (AB-loop) and residues 124, 126, 127 (D helix, DE-loop) were more critical than the adjacent residues for recognition of receptor. In addition, a cassette mutagenesis library was generated by fully randomizing the sequence of the four positions 29, 31, 32 and 35 in AB-loop, and used to select phage-IFN variants with WISH-hased panning method. Three phage-IFN variants were isolated to possess more antiviral activity in the range of 4—16-fold than parental phage-IFN after IPTG-induced soluble expression. The results suggest that phage displayed phage-IFN α1c/86D variants with increased specific activity might be obta
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| 关 键 词： | phage display peptide library human interferon αl. |
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