Dec 20, 2016 - Improved assays based on the paralog ratio test (PRT) [Armour et al., 2007]. Healthy controls, and test the association of the FCGR3B deletion with RA. The Ashaninkas and Matsiguengas live in the Amazon Yunga tropical. § Nicholas School of the Environment, Duke University, Durham, North Carolina 27708, United States ∥ Civil & Environmental Engineering, Duke University, Durham, North Carolina 27708, United States ⊥ Civil & Environmental Engineering, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.

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Fcγ receptors are a family of cell–surface receptors that are expressed by a host of different innate and adaptive immune cells, and mediate inflammatory responses by binding the Fc portion of immunoglobulin G. In humans, five low‐affinity receptors are encoded by the genes FCGR2A, FCGR2B, FCGR2C, FCGR3A, and FCGR3B, which are located in an 82.5‐kb segmental tandem duplication on chromosome 1q23.3, which shows extensive copy‐number variation (CNV). Deletions of FCGR3B have been suggested to increase the risk of inflammatory diseases such as systemic lupus erythematosus and rheumatoid arthritis (RA). In this study, we identify the deletion breakpoints of FCGR3B deletion alleles in the UK population and endogamous native American population, and show that some but not all alleles are likely to be identical‐by‐descent. We also localize a duplication breakpoint, confirming that the mechanism of CNV generation is nonallelic homologous recombination, and identify several alleles with gene conversion events using fosmid sequencing data. We use information on the structure of the deletion alleles to distinguish FCGR3B deletions from FCGR3A deletions in whole‐genome array comparative genomic hybridization (aCGH) data. Reanalysis of published aCGH data using this approach supports association of FCGR3B deletion with increased risk of RA in a large cohort of 1,982 cases and 3,271 controls (odds ratio 1.61, P = 2.9×10 −3).

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Introduction Fcγ receptors are a family of cell–surface receptors that are expressed by a host of different innate and adaptive immune cells, and mediate inflammatory responses by binding the Fc portion of immunoglobulin G (IgG) [Nimmerjahn and Ravetch, ]. They can be divided into low‐ and high‐affinity receptors, based on their affinity for IgG. Low‐affinity receptors are unable to bind monomeric IgG and instead bind to polymeric IgG in the form of antigen–antibody immune complexes. IgG binding can either activate or inhibit downstream cellular responses depending on the particular ITAM or ITIM containing Fcγ receptor that is engaged. Dysregulation of Fcγ receptors is important in a number of different inflammatory diseases, including rheumatoid arthritis (RA), systemic lupus erythematosus (SLE), and Kawasaki disease [Niederer et al.,; McKinney and Merriman,; Hargreaves et al., ]. Furthermore, not only are Fcγ receptors critical for disease etiology but also for successful immunotherapy of patients with hematological and solid cancers by mediating the effector functions of therapeutic monoclonal antibodies [Dahal et al., ]. In humans, there are five low‐affinity receptors FcγRIIa, FcγRIIb, FcγRIIc, FcγRIIIa, and FcγRIIIb encoded by the genes FCGR2A (MIM# 146790), FCGR2B (MIM# 604590), FCGR2C (MIM# 612169), FCGR3A (MIM# 146740), and FCGR3B (MIM# 610665).