Abstract
Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antibody-Dependent Cell Cytotoxicity
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Carbohydrate Sequence
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Crystallography, X-Ray
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Glycosylation
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Humans
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Immunoglobulin Fc Fragments / chemistry
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Immunoglobulin Fc Fragments / genetics
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Immunoglobulin Fc Fragments / metabolism
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Immunoglobulin G / chemistry*
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Immunoglobulin G / genetics
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Immunoglobulin G / metabolism
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In Vitro Techniques
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Models, Molecular
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Oligosaccharides / chemistry
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Static Electricity
Substances
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Immunoglobulin Fc Fragments
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Immunoglobulin G
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Oligosaccharides
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Recombinant Proteins
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oligomannoside