Antibody receptors steal the sweet spotlight

Immunoglobulin G (IgG) antibodies function, in part, through ligation of cell-surface Fc receptors such as FcγRIIIA (also known as CD16A). IgG glycosylation is known to impact antibody function, but the role of FcγRIIIA glycans, if any, is unclear. Patel et al. now reveal that these glycans do impac...

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Bibliographic Details
Published in:The Journal of biological chemistry 2018-03, Vol.293 (10), p.3490-3491
Main Authors: Oliva, Kelsey D., Cavanaugh, Jill M., Cobb, Brian A.
Format: Article
Language:English
Subjects:
Animals
Editors' Picks Highlights
Glycosylation
Humans
Immunoglobulin Fc Fragments - metabolism
Immunoglobulin G - metabolism
Killer Cells, Natural - cytology
Killer Cells, Natural - immunology
Killer Cells, Natural - metabolism
Kinetics
Ligands
Models, Molecular
Protein Conformation
Protein Processing, Post-Translational
Receptors, IgG - agonists
Receptors, IgG - chemistry
Receptors, IgG - metabolism
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Description
Summary:Immunoglobulin G (IgG) antibodies function, in part, through ligation of cell-surface Fc receptors such as FcγRIIIA (also known as CD16A). IgG glycosylation is known to impact antibody function, but the role of FcγRIIIA glycans, if any, is unclear. Patel et al. now reveal that these glycans do impact protein conformation and IgG affinity and display cell-specific glycosylation patterns, leading to a potential model in which the affinity and possibly function of Fc receptors is dictated by the cell type and its surface glycome.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.H118.001955