High Resolution Mapping of the Binding Site on Human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and Design of IgG1 Variants with Improved Binding to the FcγR
作者： Robert L Shields , Angela K Namenuk , Kyu Hong , Y Gloria Meng , Julie Rae
关键词: Protein engineering 、 Cell biology 、 Biology 、 Neonatal Fc receptor 、 Glycosylation 、 Effector 、 Antibody 、 Immunoglobulin G 、 Binding site 、 Receptor 、 Molecular biology
摘要: Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated immune responses with cellular effector functions. A high resolution map of the binding site on human IgG1 for FcγRI, FcγRIIA, FcγRIIB, FcγRIIIA, and FcRn has been determined. common set residues is involved to all FcγR; FcγRII FcγRIII also utilize outside this set. In addition which, when altered, abrogated one or more receptors, several were found that improved only specific simultaneously type receptor reduced another type. Select variants FcγRIIIA exhibited up 100%enhancement antibody-dependent cell cytotoxicity using cells; these included changes at not interface IgG/FcγRIIIA co-crystal structure (Sondermann, P., Huber, R., Oosthuizen, V., Jacob, U. (2000)Nature 406, 267–273). These engineered antibodies may have important implications improving antibody therapeutic efficacy.
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