Identification of the linear epitope for Fc-binding on the bovine IgG2 Fc receptor (boFc gamma 2R) using synthetic peptides
文献类型： 外文期刊
作者： Zhang, GP 1 ; Guo, JQ 2 ; Zhou, JY 2 ; Wang, XN 2 ; Li, QM 2 ; Yang, YY 2 ; Shen, HG 3 ; Zhao, D; Zhang, H; Xi, J; Wang, 1 ;
作者机构： 1.Zhejiang Univ, Coll Anim Sci, Lab Virol & Immunol, Hangzhou 310029, Peoples R China
2.Zhejiang Univ, Coll Anim Sci, Lab Virol & Immunol, Hangzhou 310029, Peoples R China; Henan Acad Agr Sci, Henan Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China
3.Zhejiang Univ, Coll Anim Sci, Lab Virol & Immunol, Hangzhou 310029, Peoples R China; Henan Acad Agr
关键词： Fc-binding epitope;bovine IgG2 receptor;bovine IgG2;synthetic peptides
期刊名称：FEBS LETTERS （ 2020影响因子：4.124； 五年影响因子：3.814 ）
ISSN： 0014-5793
年卷期： 2006 年 580 卷 5 期
收录情况： SCI
摘要： To identify the linear epitope for Fe-binding on the bovine IgG2 Fe receptor (boFc gamma 2R), peptides derived from the membrane-distal extracellular domain (EC1) of boFc gamma 2R corresponding to the homologous region of human Fc alpha RI were synthesized. Binding of bovine IgG2 to the different peptides was tested by Dot-blot assay, and the peptide showing maximal binding was further modified by truncation and mutation. The minimum effective peptide (82)FIGV(85) located in the putative F-G loop of the EC1 domain was found to bind bovine IgG2 specifically and inhibit the binding of bovine IgG2 to the receptor. The Phe(82), Ile(83) and Val(85) residues within the linear epitope were shown to be critical for IgG2-binding. Such functional epitope peptide should be very useful for understanding the IgG-Fc gamma interaction and development of FcR-targeting drugs. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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