This technology is a chemical approach to anchor peptides to MHC complexes while bypassing the stochastic cellular pathway normally required for antigen internalization and presentation.
Small molecules and peptides are usually not able to activate an immune response. Conventional methods to improve the immunogenicity of these compounds use large immunogenic carrier proteins, which are then internalized, processed, and presented alongside the target antigen, interfering with the subsequent immune reaction. Even after an epitope is successfully presented, it must compete with other epitopes for T-cell and B-cell recognition. There is currently no method to directly drive an immune response by regulating which epitopes are presented.
This technology covalently conjugates an azide-modified target epitope to exposed MHC complexes using a lysine-containing octopeptide with natural high binding affinity to MHC binding clefs. This improves the presentation of poorly immunogenic small molecules, and competes against existing antigens to improve the efficiency of the subsequent immune reaction and antibody production. This highly specific coupling allows targeted saturation of MHC complexes and a high yield of antibodies.
This technology is currently being validated in animal experiments with modified epitopes from SARS-CoV-2 and Wilms Tumor 1.
Ilya Trakht, Ph.D.
IR CU21177, CU21154
Licensing Contact: Jerry Kokoshka