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Toll-like receptor downstream signaling

DOI: 10.1186/ar1469

Keywords: inflammatory cytokines, innate immunity, interferons, TIR-domain containing adapter, TLR

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Abstract:

In Drosophila, Toll was initially identified as an essential protein for the determination of dorsoventral polarity during early embryogenesis. Subsequently, it was shown that flies with a mutant Toll gene are highly susceptible to fungal infection because of a defective production of specific anti-fungi peptides upon infection, demonstrating that Toll is a receptor that detects fungi invasion to trigger immune responses [1]. In 1997, a human gene similar to the Toll gene was identified through the bioinformatic approach [2]. Initial study demonstrated that this gene product can promote the expression of genes encoding inflammatory cytokines, suggesting that Toll in mammals also has a function in innate immune responses. A further five genes homologous to the Toll gene were subsequently identified, and these genes were referred to as the Toll-like receptor (TLR) family. So far, 11 members of the TLR family (TLR1-TLR11) have been identified. In both Drosophila and humans, Toll/TLRs consists of two major domains characterized by leucine-rich repeats (LRR domain) and Toll/interleukin-1 receptor (TIR domain) domain (Fig. 1). The first evidence of TLRs in the recognition of pathogens was reported from studies with mice carrying a point-mutated or disrupted Tlr4 gene [3,4]. These mice are unresponsive to bacterial lipopolysaccharide (LPS), an integral component of the outer membranes of Gram-negative bacteria that can cause endotoxin shock. Subsequently, the generation of knockout mice for each TLR gene has revealed respective pathogens that can be recognized by each TLR. TLR2 is involved in the responses to a variety of bacterial components that include peptidoglycan, lipoproteins/ lipopeptides, glycosyl-phosphatidylinositol anchors from Trypanosoma cruzi, and zymosan [5-7]. However, recognition of these TLR2 ligands requires another TLR family member. The mycoplasmal diacylated lipopeptide MALP-2 is recognized by a heterodimer of TLR2 and TLR6, whereas the bacterial tri

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