%0 Journal Article
%T Engineering human interferon αlc/86D with phage display technology<br>
%A MA XuejunHU Rong LU Hai WEI KaikunZHANG LilanXUE Shuixing HOU Yunde
%A <br>
%J 中国科学C辑(英文版)
%D 1999
%I Springer
%X 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 epitopeson 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-based 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 obtained after purification procedures. Project supported by the China National Expert Committee for Biotechnology Development.
%K phage display
%K peptide library
%K human interferon α
%K 1<br>
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=180CF3A72E750F3261A8A60EDC957784&aid=9452243F0D52734946647E38EE12EB41&yid=B914830F5B1D1078&vid=ECE8E54D6034F642&iid=0B39A22176CE99FB&sid=AC1578C6BB9EBDEF&eid=BC084ACE66B62CC8&journal_id=1674-7305&journal_name=ScienceChina.Lifesciences&referenced_num=0&reference_num=15