Abstract
In 1997, a human homologue of the Drosophila Toll protein was described, a protein later to be designated Toll-like receptor 4 (TLR4). Since that time, additional human and murine TLR proteins have been identified. Mammalian TLR proteins appear to represent a conserved family of innate immune recognition receptors. These receptors are coupled to a signaling pathway that is conserved in mammals, insects, and plants, resulting in the activation of genes that mediate innate immune defenses. Numerous studies have now identified a wide variety of chemically-diverse bacterial products that serve as putative ligands for TLR proteins. More recent studies have identified the first endogenous protein ligands for TLR proteins. TLR signaling represents a key feature of innate immune response to pathogen invasion.
MeSH terms
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Amino Acid Sequence
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Animals
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Drosophila / genetics
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Drosophila / metabolism
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Drosophila Proteins*
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Humans
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Insect Proteins / physiology
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Ligands
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Lipopolysaccharides / chemistry
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Lipopolysaccharides / metabolism*
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Mammals
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism*
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Membrane Glycoproteins / physiology
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Mice
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Mice, Knockout
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Molecular Sequence Data
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / metabolism*
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Sequence Homology, Amino Acid
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Signal Transduction*
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Toll-Like Receptor 4
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Toll-Like Receptor 5
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Toll-Like Receptor 6
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Toll-Like Receptors
Substances
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Drosophila Proteins
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Insect Proteins
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Ligands
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Lipopolysaccharides
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Membrane Glycoproteins
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Receptors, Cell Surface
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TLR4 protein, human
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TLR6 protein, human
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Tl protein, Drosophila
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Tlr6 protein, mouse
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Toll-Like Receptor 4
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Toll-Like Receptor 5
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Toll-Like Receptor 6
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Toll-Like Receptors
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tehao protein, Drosophila