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Updated: Jun 12, 2026
Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Identification of a linear epitope for Fc-binding in the mouse FcγRIII
Jun Xi1, Li N Zhang, Guang P Hu
1School of Food Science and Technology, Henan University of Technology, Zhengzhou 450052, China.
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.
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.
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