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The J-Immune Cell Binding Ligand (J-ICBL) receptor is a cell surface molecule expressed on dendritic cell (DC) precursors, including monocytes and bone marrow-derived cells, that mediates their maturation into type 1 dendritic cells (DC1). It is specifically engaged by the J-ICBL, a 13-amino-acid peptide (DLLKNGERIEKVE) derived from the beta-2-microglobulin component of the MHC class I molecule. This interaction is the foundational mechanism of the Ligand Epitope Antigen Presentation System (LEAPS) technology, which utilizes heteroconjugate peptides to direct immune responses toward a Th1/Tc1 profile characterized by IL-12 and IFN-gamma production. While its exact molecular identity is still under investigation, it is hypothesized to be a member of the leukocyte immunoglobulin-like receptor (LIR) family, such as CD85 (LILRB1 or LILRB2). Therapeutic vaccines targeting this receptor, such as CEL-2000, are being developed for the treatment of autoimmune diseases like rheumatoid arthritis and infectious diseases including herpes simplex virus and COVID-19.
Agonism (Binding of J-ICBL triggers receptor signaling that promotes the maturation of dendritic cell precursors into IL-12-producing DC1 cells).
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