Toll-like receptor 1

Toll-like receptor 1 (TLR1) is a member of Toll-like receptors (TLRs), which is a family of pattern recognition receptors (PRRs) that form the cornerstone of the innate immune system. TLR1 recognizes bacterial lipoproteins and glycolipids in complex with TLR2. TLR1 is a cell surface receptor. TLR1 is in humans encoded by the TLR1 gene, which is located on chromosome 4. The binding of ligands to TLR1 activates intracellular signaling cascades leading to an inflammatory response and initiation of immune processes. TLR1 cooperates with TLR2 in the recognition of bacterial triacyl lipoproteins. TLR1 has been shown to recognize the outer surface lipoprotein of Borrelia burgdorferi. The important role of TLR1 in recognizing triacyl lipopeptides has been shown in TLR1-deficient mice. Toll-like receptors, including TLR-1, found on the epithelial cell layer that lines the small and large intestine are important players in the management of the gut microbiota and detection of pathogens. TLR1 is synthesized in the endoplasmic reticulum. The trafficking of TLR1 from endoplasmic reticulum is controlled by protein associated with TLR4 (PRAT4A), which is endoplasmic reticulum resident chaperone. TLR1 is then transported to Golgi complex and to cell membrane. TLR1 mRNA was expressed at high levels in the kidney, lung, and spleen in adult humans, but in low levels in fetal brain and liver as well as in HeLa cell line. TLR1 is expressed in the highest levels on NK cells compared to other TLRs. TLR1 has been found to be expressed on human peripheral blood γδT cells, myeloid-derived suppressor cells, platelets, CD4+ T cells, microglia, astrocytes, immature dendritic cells, LTi-like innate lymphoid cells and eosinophils. It is also found on the surface of macrophages and neutrophils. TLR1 is a type I transmembrane glycoprotein composed of extracellular, transmembrane and intracellular domains. The extracellular domain of TLR1 contains leucine-rich repeat (LRR) domains, which play a crucial role in binding PAMPs.