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RI and FcRIIa Bind to a Region in the Fc Distinct from That Recognized by Neonatal FcR and Protein A1
*
The Helen M. Schutt Laboratory for Immunology, Austin Research Institute, Austin Repatriation Medical Centre, Heidelberg, Victoria, Australia; and
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037
The CH2-CH3 interface of the IgG Fc domain contains the binding
sites for a number of Fc receptors including
Staphylococcal protein A and the neonatal Fc receptor
(FcRn). It has recently been proposed that the CH2-CH3 interface also
contains the principal binding site for an isoform of the low affinity
IgG Fc receptor II (Fc
RIIb). The FcRI and FcRII binding sites
have previously been mapped to the lower hinge and the adjacent surface
of the CH2 domain although contributions of the CH2-CH3 interface to
binding have been suggested. This study addresses the question whether
the CH2-CH3 interface plays a role in the interaction of IgG with
FcRI and FcRIIa. We demonstrate that recombinant soluble murine
FcRI and human FcRIIa did not compete with protein A and FcRn for
binding to IgG, and that the CH2-CH3 interface therefore appears not to
be involved in FcRI and FcRIIa binding. The importance of the
lower hinge was confirmed by introducing mutations in the proposed
binding site (LL234,235AA) which abrogated binding of recombinant
soluble FcRIIa to human IgG1. We conclude that the lower hinge and
the adjacent region of the CH2 domain of IgG Fc is critical for the
interaction between FcRIIa and human IgG, whereas contributions of
the CH2-CH3 interface appear to be
insignificant.
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