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The N-glycan composition of Fc gamma receptor IIIa (FcγRIIIa) significantly impacts its binding affinity for IgG1 antibodies. Oligomannose N-glycans on FcγRIIIa dramatically increase binding affinity, highlighting its unique role among low-affinity FcγRs.

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Area of Science:

  • Immunology
  • Glycobiology
  • Structural Biology

Background:

  • Fc gamma receptors (FcγRs) on leukocytes mediate immune responses by binding IgG antibodies.
  • Previous studies suggest FcγRIIIa/CD16a N-glycan composition influences IgG1 binding affinity.

Purpose of the Study:

  • To investigate how N-glycan composition affects the binding affinity of low-affinity FcγRs for various IgG1 Fc N-glycoforms.
  • To determine the unique role of FcγRIIIa/CD16a in FcγR-IgG1 interactions.

Main Methods:

  • Assessed binding affinities of FcγRIIIa and other low-affinity FcγRs for six homogeneous IgG1 Fc N-glycoforms.
  • Utilized site-directed mutagenesis to investigate the role of specific glycosylation sites (Asn162).

Main Results:

  • FcγRIIIa with oligomannose N-glycans exhibited a KD of 1.0 ± 0.1 nm for IgG1 Fc (A2G2), a 51-fold increase compared to complex-type N-glycans.
  • FcγRIIIa N-glycan composition increased binding affinity for other IgG1 Fc glycoforms by 10-50 fold.
  • Mutation at Asn162 abolished this sensitivity, while other mutations preserved tighter binding.
  • Other low-affinity FcγRs showed minimal affinity changes (≤3.1-fold) with modified N-glycans.

Conclusions:

  • FcγRIIIa/CD16a is unique among low-affinity FcγRs due to its N-glycan-dependent binding affinity for IgG1.
  • Modulating N-glycan composition of both FcγRIIIa and IgG1 Fc can create a 400-fold range in binding affinities.
  • This glycan-mediated affinity modulation has significant implications for immune response regulation.