Research ArticleAutoimmunity

Elucidating the interplay between IgG-Fc valency and FcγR activation for the design of immune complex inhibitors

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Science Translational Medicine  16 Nov 2016:
Vol. 8, Issue 365, pp. 365ra158
DOI: 10.1126/scitranslmed.aaf9418

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Third Fc’s the charm

The activation of Fcγ receptors by autoantibody immune complexes plays a pathogenic role in multiple autoimmune diseases. In an attempt to systematically evaluate potential therapeutic approaches, Ortiz et al. tested different shapes and sizes of Fc-containing molecules. One particular design, a trimer with a Y-shaped configuration, was particularly effective at binding to Fcγ receptors and blocking them without causing inappropriate activation. To demonstrate therapeutic potential, the authors tested this Fc trimer construct in mouse models of three different autoimmune diseases: immune thrombocytopenic purpura, collagen-induced arthritis, and epidermolysis bullosa acquisita, all with promising results.

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