AI Article Synopsis
- The study investigates how immune receptors, specifically Fcγ receptors (FcγRs), activate through clustering when binding to antibodies attached to multivalent antigens, complicating the understanding of their functions.
- Researchers developed a model to analyze how varying affinities of IgG antibodies and differences in antigen binding affect FcγR clustering and immune response.
- This model allows for precise predictions regarding the impact of specific immune complex compositions, aiding in the design of immune complexes for targeted IgG functions.
Article Abstract
Many immune receptors transduce activation across the plasma membrane through their clustering. With Fcγ receptors (FcγRs), 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 immunoglobulin (Ig)G 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6062446 | PMC |
| http://dx.doi.org/10.1016/j.cels.2018.05.018 | DOI Listing |
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