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Dissecting FcγR Regulation Through a Multivalent Binding Model

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Many immune receptors transduce activation across the plasma membrane through their clustering. With Fcγ receptors, this clustering is driven by binding to antibodies of differing affinities that are in turn bound to multivalent antigen. As a consequence of this activation mechanism, accounting for and rationally manipulating IgG effector function is complicated by, among other factors, differing affinities between FcγR species and changes in the valency of antigen binding. In this study, we show that a model of multivalent receptor-ligand binding can effectively account for the contribution of IgG-FcγR affinity and immune complex valency. This model in turn enables us to make specific predictions about the effect of immune complexes of defined composition. In total, these results enable both rational immune complex design for a desired IgG effector function and the deconvolution of effector function by immune complexes.

Summary points

Avidity most prominently modulates low-affinity FcγR-immune complex binding A multivalent binding model can quantitatively predict FcγR-immune complex binding Immune complex avidity has an outsized contribution to FcγR multimerizationas compared to binding A binding model deconvoles and predicts the influence of interventions modulating in vivo FcγR-driven effector function

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