TEACHER
Date:24 July
Time:14:15– 14:40 (GMT+8)
CEO
AB Biosciences
Human IVIG, a plasma-derived immunoglobulin preparation from thousands of donors, is widely used for immune replacement therapy in immunodeficient patients. Beyond its established role in passive protection against infections, IVIG has long demonstrated potent anti-inflammatory effects in autoimmune diseases—though its mechanism remained elusive. Recent studies have attributed this activity not to the antibody variable regions but to oligomerized Fc fragments that mimic immune complexes.
Despite its clinical success, recombinant IVIG has remained an unmet challenge, particularly in replicating the anti-inflammatory effects. This difficulty lies in engineering an oligomeric Fc with the necessary stability, manufacturability, and receptor-binding characteristics.
AB Biosciences has addressed this challenge by creating a novel trimeric Fc fusion protein. By fusing a fully human IgG1 Fc domain to a trimerization scaffold derived from the NC1 domain of human collagen XXI, the resulting construct—termed PRIM (Pan Receptor Interacting Molecule)—forms a covalently linked trimer with strong avidity binding to all classical Fcγ receptors as well as the neonatal Fc receptor (FcRn). PRIM has demonstrated robust anti-inflammatory activity in preclinical studies, including excellent efficacy in the collagen-induced arthritis (CIA) mouse model.
This innovation marks a key advancement toward a recombinant alternative to plasma-derived IVIG for autoimmune therapy. Building on the success of PRIM, AB Biosciences is now expanding its platform to develop multivalent protein biologics with enhanced therapeutic potency over traditional bivalent antibodies. The integration of cutting-edge AI tools such as AlphaFold3 and Rosetta enables high-throughput structural modeling and in silico triage of therapeutic candidates, accelerating the path from design to clinic.