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. Activation of TLR2 leads to the initiation of apoptosis and the activation of the NK-kappaB pathway by the adaptor molecule MyD88. TLR2 recognizes and is activated by components from a broad variety of microorganisms including lipoproteins from Gram-negative bacteria, Mycoplasma, spirochetes, peptidoglycan and LTAs from Gram-positive bacteria, lipoarabinomannan from mycobacteria, glycoinositolphospholipids, phenolsoluble modulin, zymosan from yeast and neisserial porins. TLR2 has been reported to functionally associate with TLR1 and TLR6 in order to recognize various lipopeptides.1-16
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