Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFc gamma RI) by synthetic peptide

文献类型： 外文期刊

第一作者： Wang, F. Y.

作者： Wang, F. Y.;Guo, J. Q.;Zhang, G. P.

作者机构：

关键词： Fc-binding linear epitope;IgG;Fc gamma RI;Synthetic peptide

期刊名称：GENETICS AND MOLECULAR RESEARCH （ 影响因子：0.764； 五年影响因子：0.912 ）

ISSN： 1676-5680

年卷期： 2014 年 13 卷 2 期

页码：

收录情况： SCI

摘要： To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor (moFc gamma RI), peptides derived from the membrane-distal extracellular domain (EC2) of moFc gamma RI, corresponding to the homologous region of human Fc gamma RI (huFc gamma RI) and huFc gamma RII, were synthesized. Using a dot-blot assay, six peptides were tested. The results showed that the moRI3 peptide (CVFYRNGKSFQFS) could combine with mouse IgG efficiently. A competitive enzyme-linked immunosorbent assay (ELISA) showed that the IC50 value of the moRI3 peptide was 38.03 mu M. The moRI3 peptide could inhibit the combination of mouse IgG to the transfected COS 7 cells significantly with an IC50 value of 72.68 mu M. The IgG-binding region of moFc gamma RI was also localized in the C'-E loop of the EC2 domain as predicted according to huFc gamma RI and huFc gamma RII. We predicted that the minimum effective IgG-binding region of moFc gamma RI may be the peptide (153)SFQFSS(158). The linear epitope for immunoglobulin-binding to mouse Fc gamma R is also described. Thus, we generated a peptide that targets a fundamental aspect of ligand recognition by this receptor class.

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