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Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types Jordi Pelkmans Amanda Maurits
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Antigen-IgG1-FcγRIIIa binding Antibody Dependent Cellular Cytotoxicity (ADCC) FcγRIIIa
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C1q Antigen-IgG1-C1q binding Complement Dependent Cytotoxicity (CDC)
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Human IgG1
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Three types of N-linked oligosaccharides High-mannose Hybrid Complex All types can be fucosylated
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Different types of oligosaccharides created in this article No difference in binding of the variable part of the IgG1 was observed
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Difference in binding affinity to FcγRIIIa
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Difference in ADCC activity
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Contamination of different types of oligosaccharides influences activity of Fu(-) Complex type
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Difference in CDC activity
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C1q binds best to Complex type
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Plasma clearance of different types
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The FcRn receptor Binds IgG1 and prevents its degradation
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Conclusion Oligosac charide FcγRIIIa binding affinity ADCC activity CDC activity C1q binding affinity Plasma clearance in mice FcRn binding affinity Fu(-) Complex 666663 Fu(+) Complex 226661 Fu(-) Hybrid 455555 Fu(+) Hybrid 1155-2 Fu(-) M8,9 5455-6 Fu(-) M5335544
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