publication . Other literature type . Article . 2017

Affimer proteins inhibit immune complex binding to FcγRIIIa with high specificity through competitive and allosteric modes of action

Christian Tiede; Mark P. Waterhouse; Robin Owen; Sarah Harris; Maren Thomsen; Richard Foster; Darren Tomlinson; James Robinson; Adrian Goldman; Colin Fishwick;
Open Access
  • Published: 15 Dec 2017
  • Publisher: Proceedings of the National Academy of Sciences
  • Country: United Kingdom
Abstract
<jats:p>Protein–protein interactions are essential for the control of cellular functions and are critical for regulation of the immune system. One example is the binding of Fc regions of IgG to the Fc gamma receptors (FcγRs). High sequence identity (98%) between the genes encoding FcγRIIIa (expressed on macrophages and natural killer cells) and FcγRIIIb (expressed on neutrophils) has prevented the development of monospecific agents against these therapeutic targets. We now report the identification of FcγRIIIa-specific artificial binding proteins called “Affimer” that block IgG binding and abrogate FcγRIIIa-mediated downstream effector functions in macrophages, ...
Subjects
free text keywords: PNAS Plus, Multidisciplinary
Abstract
<jats:p>Protein–protein interactions are essential for the control of cellular functions and are critical for regulation of the immune system. One example is the binding of Fc regions of IgG to the Fc gamma receptors (FcγRs). High sequence identity (98%) between the genes encoding FcγRIIIa (expressed on macrophages and natural killer cells) and FcγRIIIb (expressed on neutrophils) has prevented the development of monospecific agents against these therapeutic targets. We now report the identification of FcγRIIIa-specific artificial binding proteins called “Affimer” that block IgG binding and abrogate FcγRIIIa-mediated downstream effector functions in macrophages, ...
Subjects
free text keywords: PNAS Plus, Multidisciplinary
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