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The story of Toll-like receptors started almost 35 years ago with the discovery that the Toll protein plays a crucial role in embryonic development, including the dorsoventral body patterning in the Drosophila melanogaster (the common fruit fly). In 1991, Gay and Keith showed that the cytoplasmic domain of the Drosophila Toll protein is homologous to the human interleukin-1 receptor (IL1R). Later studies established that, both Toll and IL-1R share common aminoacids (AAs) that are crucial for nuclear factor-kappa B (NF-κB) signaling that plays a significant role in embryonic development, immunity, and in the inflammatory immune response. For example, Toll protein in the D. melanogaster plays a crucial role in antifungal and antibacterial immunity through regulating the production of drosomycin, an antifungal peptide and Dif (a member of NF-κB) that induces the production of antimicrobial peptide cecropin. In 1997, the first report of the expression of human homolog of Toll protein called hToll (human Toll) came from the laboratory of Charles A. Janeway Jr. that is now called Tolllike receptor 4 (TLR4).
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