The Toll-like receptor (TLR) family is comprised of Type I transmembrane proteins characterized by an extracellular leucine-rich domain and a cytoplasmic tail that contains a conserved region call the Toll/IL-1 (TIR) domain. First discovered in Drosophila, TLRs recognize specific molecular patterns that are present in microbial components and respond to these components in order eliminate or limit invading microbes. To date, ten mammalian homologs of TLRs have been described. TLRs signal through adaptor molecules such as MyD88 leading to NF-kappaB activation, c-Jun N-terminal kinase activation (JNK), cytokine secretion and the inflammatory response. The amino acid sequence of human TLR6 is most similar to hTLR1 with 69% identity. TLR6 recognizes mycoplasmal macrophage-activating lipopeptide- 2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B. burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2.1-6
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