Half-Life Extension of the IgG-Degrading Enzyme (IdeS) Using Fc-Fusion Technology.

ABSTRACT: Imlifidase (IdeS) is a bacterial protease that hydrolyzes human IgG in their hinge region, decreasing their half-life and abrogating their Fc-mediated properties. It is now successfully used in therapy to prevent graft rejection during kidney transplants and is being clinically evaluated in several IgG-mediated autoimmune diseases. IdeS short half-life however limits its clinical use, particularly in the case of chronic diseases that would request repeated administrations. Here, we developed IdeS-Fc fusion proteins as a divalent homodimer (IdeS-Fc^div) or a monovalent heterodimer (IdeS-Fc^monov), in order to extend the IgG-depleting action of IdeS over time. Both IdeS-Fc efficiently separated monoclonal and polyclonal human IgG into F(ab')₂ and Fc fragments,

SUBMITTER: Daventure V 

PROVIDER: S-EPMC11830383 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature