The Toll-like receptor (TLR) family in mammal comprises a family of transmembrane proteins characterized by multiple copies of leucine rich repeats in the extracellular domain and IL-1 receptor motif in the cytoplasmic domain. Like its counterparts in Drosophila, TLRs signal through adaptor molecules (1). The TRL family is a phylogenetically conserved mediator of innate immunity that is essential for microbial recognition (2). TLRs characterized so far activate the MyD88:interleukin-1 receptor-associated kinase (IRAK) signaling pathway. Ten human homologs of TLRs (TLR1-10) have been described. The aa sequence of human TLR6 is most similar to hTLR1 with 69% identity at the aa level. Human TLR6 consists of a predicted 807aa with a molecular weight of approximately 92kD (3). Human and mouse TLR6 share an aa identity of 73%. TLR6 activates both NF-kB and c-Jun N-terminal Kinase (JNK). The amino acids in the cytoplasmic domain of IL-1 receptor, which are critical for NF-kB activation, are conserved in TLR6. It has also been shown that TLR2-mediated response to a phenol-soluble factor from staphylococcus epidermidis is enhanced by TLR6 (4). TLR6 is predominantly expressed in spleen, thymus, ovary, and lung (3).