Interleukin-12 receptor subunit beta-1 (IL12RB1) (IL12RB1)

The Interleukin-12 receptor subunit beta-1 (IL12RB1), also known as CD212, is a type I transmembrane protein that serves as a critical component of both the IL-12 and IL-23 receptor complexes [2.1.1, 2.2.4]. It binds to the p40 subunit shared by these two cytokines, facilitating the formation of high-affinity signaling complexes with IL-12Rβ2 (for IL-12) or IL-23R (for IL-23) [2.3.3, 3.1.3]. Biologically, IL12RB1 is essential for the differentiation of T helper 1 (Th1) and Th17 cells, the production of interferon-gamma (IFN-γ), and the activation of natural killer (NK) cells [2.2.4, 3.3.4]. Mutations in the IL12RB1 gene lead to Mendelian susceptibility to mycobacterial diseases (MSMD), a condition characterized by severe infections from poorly pathogenic mycobacteria and salmonella [2.1.2, 2.2.2]. In therapeutic contexts, IL12RB1 is a key target for treating autoimmune and inflammatory conditions such as psoriasis and Crohn's disease [2.2.1, 3.2.5]. While most approved therapies like ustekinumab target the p40 ligand to prevent its binding to IL12RB1, direct receptor-blocking antibodies are also under investigation to overcome resistance mechanisms associated with ligand-targeting drugs [3.2.3, 3.2.5].

Other names

IL-12R-beta1IL12RBCD212Interleukin-12 receptor beta-1 subunitIMD30

Ligand neutralization (blocking the p40 subunit of IL-12 and IL-23 from binding to the IL12RB1 receptor subunit)