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Identification of a linear epitope for Fc-binding in the mouse Fc gamma RIII

文献类型： 外文期刊

作者： Xi, Jun 1 ; Zhang, Li N. 1 ; Hu, Guang P. 3 ; Wang, Li 1 ; Qiao, Song L. 1 ; Guo, Jun Q. 1 ; Lu, Qi Y. 2 ; Zhang, Gai P.; 1 ;

作者机构： 1.Henan Acad Agr Sci, Key Lab Anim Immunol, Minist Agr, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

2.Henan Univ Technol, Sch Food Sci & Technol, Zhengzhou 450052, Peoples R China

3.Henan Inst E

关键词： moFc gamma RIII alpha-chain;EC2 domain;Peptides

期刊名称：PEPTIDES （ 影响因子：3.75； 五年影响因子：3.389 ）

ISSN： 0196-9781

年卷期： 2010 年 31 卷 9 期

页码：

收录情况： SCI

摘要： Fe receptors are transmembrane proteins, found on the surfaces of immune cells, that aid in the removal of foreign pathogens by binding to antibody-coated targets via the Fc regions of the antibodies. To identify sites on mouse Fc gamma RIII (moFc gamma RIII) alpha-chain that bind to the Fc region, peptides derived from the proximal extracellular domain (EC2) of moFc gamma RIII alpha-chain corresponding to the homologous region of human Fc gamma RIIIB alpha-chain were synthesized. Binding of mouse IgG to the different peptides was tested by Dot-blot assay. The effective peptide (119)SFFHNEKSVRYH(130) located in the putative C-C' loop of the EC2 domain was found to bind mouse IgG specifically with an affinity of approximately 5.58 x 10(-5) M and inhibit the binding of mouse IgG to the receptor. Such a functional peptide should be very useful for further understanding the IgG-Fc gamma R interaction and development of FcR-targeting drugs. (C) 2010 Elsevier Inc. All rights reserved.

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