鉴定小鼠 FcγRIII 中与 Fc 结合的线性表位。

Identification of a linear epitope for Fc-binding in the mouse FcγRIII.

机构信息

School of Food Science and Technology, Henan University of Technology, Zhengzhou 450052, China.

出版信息

Peptides. 2010 Sep;31(9):1684-8. doi: 10.1016/j.peptides.2010.05.022. Epub 2010 Jun 8.

DOI:10.1016/j.peptides.2010.05.022

PMID:20566342

Abstract

Fc 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 FcgammaRIII (moFcgammaRIII) alpha-chain that bind to the Fc region, peptides derived from the proximal extracellular domain (EC2) of moFcgammaRIII alpha-chain corresponding to the homologous region of human FcgammaRIIIB 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-FcgammaR interaction and development of FcR-targeting drugs.

摘要

Fc 受体是位于免疫细胞表面的跨膜蛋白，通过与抗体的 Fc 区域结合，来帮助清除抗体包被的靶标上的外来病原体。为了鉴定与 Fc 区域结合的小鼠 FcγRIII（moFcγRIII）α 链上的结合位点，合成了源自 moFcγRIIIα 链的近胞外结构域（EC2）的肽段，该肽段与人类 FcγRIIIBα 链的同源区相对应。通过 Dot-blot 分析测试了不同肽段与小鼠 IgG 的结合。在 EC2 结构域的假定 C-C'环中发现的有效肽段（119）SFFHNEKSVRYH（130）能够特异性地结合小鼠 IgG，亲和力约为 5.58 x 10(-5) M，并抑制小鼠 IgG 与受体的结合。这种功能性肽段对于进一步了解 IgG-FcγR 相互作用以及开发针对 FcR 的药物非常有用。