The sialylation of antibodies within the Fc domain (at ASN297) regulates the balance between inflammation and tolerance. Non-sialylated antibodies promote inflammation via activation of the Type I Fc receptors, whereas sialylated antibodies reduce inflammation and restore immune self-tolerance via activation of the Type II immunomodulatory Fc receptors DC-SIGN and CD23.
Patients with chronic autoimmune disease commonly present with the low circulating titers of sialylated antibodies, and therefore do not appropriately engage the Type II tolerizing Fc receptors. In this webinar, the expert speakers will discuss a novel therapeutic strategy for the treatment of autoimmune diseases and the administration of a recombinant human IgG1 Fc engineered to agonize the Type II Fc receptors to re-establish normal immune homeostasis.
In this webinar, the experts will also provide some background on how glycosylation is linked to modulating the immune system and how the glycosylation pathways can be engineered for a range of drug development effects, including increasing half-life and bioavailability, enhancing antibody-drug conjugate (ADC) effects and modulating the anti-inflammatory response.
Register for this webinar today to gain insights into the effects of glycosylation on drug efficacy and safety and how engineering glycan profiles can enhance clinical outcomes.
Join Bjørn Voldborg, Head of the National Biologics Facility, Technical University of Denmark (DTU); Greg Coffey, PhD, Co-Founder & Vice President, Immunology & Clinical Translational Research, Nuvig Therapeutics; and Divya Teja Vavilala, PhD, Head of Protein Analytics, ATUM, for the live webinar on Monday, September 9, 2024, at 10am EDT (2pm BST/UK).
For more information, or to register for this event, visit Enabling Clinical Programs Through Antibody Glycosylation.
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