Abstract

Clinically relevant differences amongst therapeutic antibodies against the same target may relate to their unique molecular attributes. Differences in therapeutic profile across the domains of psoriatic disease between guselkumab (GUS) and risankizumab (RIS) have been observed. To explore potential mechanisms underpinning this, we studied GUS, a fully human IgG1 specific for interleukin (IL)-23 with a native Fc region, and RIS, a humanized anti-IL-23 IgG1 with a mutated Fc region. We compared binding and functional characteristics of the antigen-binding and Fc regions of these antibodies.

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