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Title: Characterization of FcR Ig-binding sites and epitope mapping.
Austin Authors: Hogarth, P Mark;Ierino, F L;Hulett, M D
Affiliation: Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australia
Issue Date: 1-Feb-1994
Publication information: Immunomethods; 4(1): 17-24
Abstract: The low-affinity receptor for IgG, Fc gamma RII, and the high-affinity receptor for IgE, Fc epsilon RI, are functionally distinct but structurally homologous receptors. These characteristics have been exploited using a chimeric receptor strategy to examine segments of human Fc gamma RII for IgG-binding function. A series of chimeric receptors was generated by exchanging coding regions of the extracellular ligand-binding regions between Fc gamma RII and the Fc epsilon RI alpha chain using splice overlap extension by the polymerase chain reaction. The expression of these chimeric receptors in COS-7 cells and analysis of their IgG/IgE binding capacities have enabled the Ig-binding region of Fc gamma RII to be localized to a subregion of the second extracellular domain. The localization of the Ig-binding region of Fc gamma RII has provided the opportunity of performing site-directed mutagenesis to determine the key amino acids involved in the interaction of the receptor with IgG. These findings demonstrate that the chimeric receptor approach is a powerful technique for the dissection of structure/function relationships of structurally related yet functionally different molecules.
Gov't Doc #: 7520815
Journal: ImmunoMethods
Type: Journal Article
Subjects: Amino Acid Sequence
Antibodies, Monoclonal
Base Sequence
Binding Sites
Cell Line
Fluorescent Antibody Technique
Immunoglobulin G.metabolism
Molecular Sequence Data
Receptors, IgE.genetics.metabolism
Receptors, IgG.genetics.metabolism
Recombinant Fusion Proteins.genetics.metabolism
Rosette Formation
Appears in Collections:Journal articles

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