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Engineering therapeutic antibodies for improved function
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DOI：10.1042/bst0300487.png)
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摘要
En 中文
The binding sites on human IgG1 for human Fcgamma receptor (FcgammaR) 1, FcgammaRIIa, FcgammaRIIb, FcgammaRIIIa and neonatal FcR have been mapped. A common set of IgG1 residues is involved in binding to all FcgammaRs, while FcgammaRII and FcgammaRIII utilize distinct sites outside this common set. In addition to residues which abrogated binding to the FcgammaR, several positions were found which improved binding only to specific FcgammaRs or simultaneously improved binding to one type of FcgammaR and reduced binding to another type. Selected IgG1 variants with improved binding to FcgammaRIIIa were then tested in an in vitro antibody-dependent cellular cytotoxicity (ADCC) assay and showed an enhancement in ADCC when either peripheral blood mononuclear cells or natural killer cells were used.
Keyword:
antibody
antibody-dependent cellular cytotoxicity (ADCC)
Fc receptor
neonatal Fc receptor (FcRn)
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