Human TLR6 Antibody

Toll-like receptors (TLRs) play a critical role in early innate immunity to invading pathogens by sensing microorganisms. These evolutionary conserved receptors recognize highly conserved structural motifs only expressed by microbial pathogens, called pathogen-associated microbial patterns (PAMPs). Stimulation of TLRs by PAMPs initiates a signaling cascade leading to the secretion of proinflammatory cytokines following NF-κB activation. To date ten human and twelve murine TLRs have been characterized, TLR1 to TLR10 in humans, and TLR1 to TLR9, TLR11, TLR12 (aka TLR11) and TLR13 in mice, the homolog of TLR10 being a pseudogene.

TLR6, which is closely related to TLR1, is expressed predominantly in spleen, thymus, ovary and lung [1]. TLR6 cooperates with TLR2 to recognize diacylated lipoproteins (LPs) found in mycoplasma but is not required in the recognition of triacylated LPs found in bacteria [2]. This suggests that TLR6 is able to discriminate between the N-terminal lipoylated structures of LPs derived from mycoplasma and bacteria. TLR6 collaboration with TLR2 is essential for the recognition and signal transduction of diacylated LPs, such as MALP-2 and FSL-1 [2, 3], as well as heat-killed mycoplasma, indicating that TLR6 and TLR2 play a central role in recognizing mycoplasma [2].

1. Takeuchi O. et al., 1999. TLR6: A novel member of an expanding toll-like receptor family. Gene. 231(1-2):59-65.
2. Takeuchi O. et al., 2001. Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int Immunol, 13(7):933-40.
3. Fujita M. et al., 2003. Involvement of leucine residues at positions 107, 112, and 115 in a leucine-rich repeat motif of human Toll-like receptor 2 in the recognition of diacylated lipoproteins and lipopeptides and Staphylococcus aureus peptidoglycans. J Immunol. 171(7):3675-83.