Toll-like receptor 10 (TLR10)

Toll-like receptor 10 (TLR10) is a transmembrane pattern-recognition receptor of the innate immune system, belonging to the Toll-like receptor family. Structurally, it is a glycoprotein sharing domains common to other TLRs, including an extracellular leucine-rich repeat domain for ligand recognition and a cytoplasmic TIR domain for signal transduction[1][2][4]. TLR10 is primarily expressed in immune cell-rich tissues (spleen, lymph node, thymus, lung) and on immune cells such as B cells, dendritic cells, neutrophils, and also in non-immune tissues[2][4]. Unlike other TLRs, TLR10’s endogenous ligands and precise signaling pathways remain incompletely characterized; it can form homodimers or heterodimers (notably with TLR2 and TLR1) and appears to predominantly act as an inhibitory receptor that suppresses TLR2-driven inflammatory cytokine production, largely through increased production of IL-1Ra[2]. Some studies have reported proinflammatory activity under certain circumstances, suggesting context-dependent dual functions[1]. Genetic polymorphisms in TLR10 can modulate immune responses and are linked with disease susceptibility, including autoimmune disorders and possibly cancer[2]. No drugs are currently approved that directly target TLR10, and there are ongoing investigations into its therapeutic and biomarker potential.

Other names

TLR10CD290Toll/interleukin-1 receptor-like protein

TLR10 primarily modulates immune responses, particularly through inhibition of TLR2-mediated signaling, where antagonistic antibodies can either block or mimic its function. It induces anti-inflammatory mediators such as IL-1 receptor antagonist (IL-1Ra). TLR10 also participates in heterodimerization with TLR2 (and potentially TLR1), which affects the recognition of TLR2 ligands.