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Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc

M Raghavan1, Y Wang, P J Bjorkman

  • 1Division of Biology, California Institute of Technology, Pasadena 91125, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 21, 1995
PubMed

Insights

Neonatal Fc receptor (FcRn) dimerization is crucial for binding immunoglobulin G (IgG). This finding supports a model where FcRn dimerization signals cells to internalize IgG-FcRn complexes, impacting nutrient transfer in newborns.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The neonatal Fc receptor (FcRn) is essential for transferring maternal immunoglobulin G (IgG) to newborns via milk.
  • Previous studies observed FcRn dimers in crystal structures, but their functional significance remained unclear.

Purpose of the Study:

  • To investigate the biological relevance of FcRn dimerization in the context of IgG binding.
  • To determine if FcRn dimerization plays a role in the initiation of endocytosis.

Main Methods:

  • Utilized surface plasmon resonance (SPR)-based biosensor assays to analyze FcRn-IgG interactions.
  • Immobilized FcRn on biosensor chips in orientations that either promote or disrupt dimerization.

Main Results:

  • High-affinity binding of IgG to FcRn was observed only when FcRn was oriented to facilitate dimerization.
  • Disrupting FcRn dimerization prevented high-affinity IgG binding.

Conclusions:

  • FcRn dimerization is a critical factor for high-affinity IgG binding.
  • The results support a model where IgG binding induces FcRn dimerization, triggering cellular endocytosis of the IgG-FcRn complex.

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