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Review
. 2019 Mar 19:10:464.
doi: 10.3389/fimmu.2019.00464. eCollection 2019.

The Human FcγRII (CD32) Family of Leukocyte FcR in Health and Disease

Jessica C Anania  1   2 , Alicia M Chenoweth  1   2 , Bruce D Wines  1   2   3 , P Mark Hogarth  1   2   3
Affiliations
Review

The Human FcγRII (CD32) Family of Leukocyte FcR in Health and Disease

Jessica C Anania et al. Front Immunol. .

Abstract

FcγRs have been the focus of extensive research due to their key role linking innate and humoral immunity and their implication in both inflammatory and infectious disease. Within the human FcγR family FcγRII (activatory FcγRIIa and FcγRIIc, and inhibitory FcγRIIb) are unique in their ability to signal independent of the common γ chain. Through improved understanding of the structure of these receptors and how this affects their function we may be able to better understand how to target FcγR specific immune activation or inhibition, which will facilitate in the development of therapeutic monoclonal antibodies in patients where FcγRII activity may be desirable for efficacy. This review is focused on roles of the human FcγRII family members and their link to immunoregulation in healthy individuals and infection, autoimmunity and cancer.

Keywords: Fc receptor; FcγR; autoimmunity; cancer; infection; inflammation; mAb therapeutics.

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Figures

Figure 1
Figure 1
Composition of FCGR2A, FCGR2B, and FCGR2C and their splice variants. Leader (L), ectodomain (D), transmembrane (TM) cytoplasmic tail (c), and intervening sequence (IVS). Expressed exons are illustrated in color, while spliced exons (selectively expressed) are represented in black. The location and position number of amino acids affected by well characterized polymorphisms are shown above the exons except for the FCGR2B leader exons where the nucleotide positions are given. See text for references.
Figure 2
Figure 2
The interaction of IgG-Fc with FcγRIIA and FcγRIIB is similar. The perspectives shown are of two ectodomains of the (A) FcγRIIA [adapted from 3RY6 (61)] and (B) FcγRIIB [adapted from 3WJJ (123)] (shown in dark blue) in complex with IgG-Fc (shown in gray). The structural components of the receptor contributing to IgG binding are the two tryptophan residues that form the Trp sandwich (red), the BC loop (green), the C′E strand (yellow), and the FG loop (purple), with the “high/low resonder” polymorphic residue His131Arg highlighted (orange).
See this image and copyright information in PMC

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