Conserved FcγR- glycan discriminates between fucosylated and afucosylated IgG in humans and mice.

@article{Dekkers2018ConservedFG,
  title={Conserved FcγR- glycan discriminates between fucosylated and afucosylated IgG in humans and mice.},
  author={Gillian Dekkers and Arthur E. H. Bentlage and Rosina Plomp and Remco Visser and Carolien A. M. Koeleman and Anna Beentjes and Juk Yee Mok and Wim J E van Esch and Manfred Wuhrer and Theo Rispens and Gestur Vidarsson},
  journal={Molecular immunology},
  year={2018},
  volume={94},
  pages={
          54-60
        }
}
The binding strength between IgG and FcγR is influenced by the composition of the N-linked glycan at position N297 in the Fc-domain of IgG. Particularly, afucosylation increases the binding affinity of human IgG1 to human FcγRIIIa up to ∼20 fold, and additional galactosylation of the afucosylated IgG increases the affinity up to ∼40 fold. The increase in affinity for afucosylated IgG has previously been shown to depend on direct carbohydrate-carbohydrate interactions between the IgG-Fc glycan… CONTINUE READING

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