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acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 14978119, 11673543, 12935358 TLR2 acts as a heterodimer in concert with either TLR1 or TLR6, to mediate responses to moieties including lipoproteins and lipoteichoic acids (LTA) from Gram-positive bacteria [18] and rare lipopolysaccharide (LPS) species [19], and lipoarabinomannan from mycobacteria [20]. PMID: 17223959, 15728506 TLR10 was the orphan member of the family, but recent work has demonstrated its ability to form homodimers and also heterodimers with TLR1 and TLR2, although specific ligands for these combinations have yet to be identified. PMID: 17223959, 15728506 TLR10 was the orphan member of the family, but recent work has demonstrated its ability to form homodimers and also heterodimers with TLR1 and TLR2, although specific ligands for these combinations have yet to be identified. PMID: 17223959, 11932926, 12794153 TLR4 acts essentially as a homodimer (although there is some evidence for heterodimerization with TLR1 [22] and TLR5 [23]), and it also recognizes an extensive range of agonists. PMID: 17223959, 11932926, 12794153 TLR4 acts essentially as a homodimer (although there is some evidence for heterodimerization with TLR1 [22] and TLR5 [23]), and it also recognizes an extensive range of agonists. PMID: 17223959, 11932926, 12794153 TLR4 acts essentially as a homodimer (although there is some evidence for heterodimerization with TLR1 [22] and TLR5 [23]), and it also recognizes an extensive range of agonists. PMID: 17223959, 9851930, 9989976, 10201887 TLR4 is crucial for effective responses to the Gram-negative bacterial component LPS [5–7], but also recognizes viral proteins [25,26]. PMID: 17223959, 11607032, 14579267, 14976261 TLR3 recognizes double-stranded RNA [29], while TLR7 and/or 8 mediate responses to single-stranded RNA, also derived from viruses [30,31]. PMID: 17223959, 11323673, 14625549 In contrast, only a single agonist group has been identified so far for TLR5 comprising the flagellins, an essential protein component of bacterial flagella found in both Gram-positive and Gram-negative bacteria [27,28]. PMID: 17223959, 11607032, 14579267, 14976261 TLR3 recognizes double-stranded RNA [29], while TLR7 and/or 8 mediate responses to single-stranded RNA, also derived from viruses [30,31]. PMID: 17223959, 11607032, 14579267, 14976261 TLR3 recognizes double-stranded RNA [29], while TLR7 and/or 8 mediate responses to single-stranded RNA, also derived from viruses [30,31]. PMID: 17223959, 14563635, 12900525 TLR9 recognizes unmethylated CG dinucleotides (CpG motifs), mediating responses to bacterial DNA and some viruses [34,35]. PMID: 17223959, 14729660, 12411706, 11083876 There is increasing evidence that ‘endogenous’ ligands may also activate TLRs; these include products derived from host cells, for example mRNA [43] (recognized by TLR3), and anti-microbial molecules such as defensins [44] and reactive oxygen species (TLR2) [45]. PMID: 17223959, 14579267, 12464152 TLR7 and 8 also respond to potent immunomodulatory nucleoside or nucleoside-like drugs, such as loxoribine and the imidazoquinolines [30,32], and appear to be responsible for the potent actions of the imidazoquinolines in the treatment of skin tumours [33]. PMID: 17223959, 14579267, 12464152 TLR7 and 8 also respond to potent immunomodulatory nucleoside or nucleoside-like drugs, such as loxoribine and the imidazoquinolines [30,32], and appear to be responsible for the potent actions of the imidazoquinolines in the treatment of skin tumours [33]. PMID: 17223959, 14579267, 12464152 TLR7 and 8 also respond to potent immunomodulatory nucleoside or nucleoside-like drugs, such as loxoribine and the imidazoquinolines [30,32], and appear to be responsible for the potent actions of the imidazoquinolines in the treatment of skin tumours [33]. PMID: 17223959, 14579267, 12464152 TLR7 and 8 also respond to potent immunomodulatory nucleoside or nucleoside-like drugs, such as loxoribine and the imidazoquinolines [30,32], and appear to be responsible for the potent actions of the imidazoquinolines in the treatment of skin tumours [33]. PMID: 17223959, 14729660, 12411706, 11083876 There is increasing evidence that ‘endogenous’ ligands may also activate TLRs; these include products derived from host cells, for example mRNA [43] (recognized by TLR3), and anti-microbial molecules such as defensins [44] and reactive oxygen species (TLR2) [45]. PMID: 17223959, 14729660, 12411706, 11083876 There is increasing evidence that ‘endogenous’ ligands may also activate TLRs; these include products derived from host cells, for example mRNA [43] (recognized by TLR3), and anti-microbial molecules such as defensins [44] and reactive oxygen species (TLR2) [45]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959, 16709864,11509636, 12055204 In addition, products derived from damaged or dying cells can act as agonists, and proposed members of this category of TLR4-activators include heat shock protein B8 [46], fibrinogen [47], surfactant protein A [48] and the tissue matrix breakdown products fibronectin extra domain A [49] and hyaluronic acid oligosaccharides [50]. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. PMID: 17223959 Upon activation MyD88 recruits IRAK-4, allowing association and phosphorylation of IRAK-1, which in turn recruits TRAF6. PMID: 17223959 Upon activation MyD88 recruits IRAK-4, allowing association and phosphorylation of IRAK-1, which in turn recruits TRAF6. PMID: 17223959 Upon activation MyD88 recruits IRAK-4, allowing association and phosphorylation of IRAK-1, which in turn recruits TRAF6. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. PMID: 17223959 MyD88 is utilized by all the TLRs, except TLR3, and requires the bridging adapter Mal/TIRAP for TLR2 and TLR4 signalling. Indirect PMID: 17223959, 10075645, 10601019, 14699155 TRAF6 activates the TAK-1/TAB1/2/3 complex, resulting in downstream cascades that lead ultimately to activation of nuclear factor (NF)-κB [56], and also initiation of distinct parallel signalling pathways leading to mitogen-activated protein (MAP) kinase [57–59] and phosphoinositide 3-kinase (PI3K) [60,61] activation. Indirect PMID: 17223959, 10075645, 10601019, 14699155 TRAF6 activates the TAK-1/TAB1/2/3 complex, resulting in downstream cascades that lead ultimately to activation of nuclear factor (NF)-κB [56], and also initiation of distinct parallel signalling pathways leading to mitogen-activated protein (MAP) kinase [57–59] and phosphoinositide 3-kinase (PI3K) [60,61] activation. Indirect PMID: 17223959, 10075645, 10601019, 14699155 TRAF6 activates the TAK-1/TAB1/2/3 complex, resulting in downstream cascades that lead ultimately to activation of nuclear factor (NF)-κB [56], and also initiation of distinct parallel signalling pathways leading to mitogen-activated protein (MAP) kinase [57–59] and phosphoinositide 3-kinase (PI3K) [60,61] activation. Indirect PMID: 17223959, 10075645, 10601019, 14699155 TRAF6 activates the TAK-1/TAB1/2/3 complex, resulting in downstream cascades that lead ultimately to activation of nuclear factor (NF)-κB [56], and also initiation of distinct parallel signalling pathways leading to mitogen-activated protein (MAP) kinase [57–59] and phosphoinositide 3-kinase (PI3K) [60,61] activation. Indirect PMID: 17223959, 10075645, 10601019, 14699155 TRAF6 activates the TAK-1/TAB1/2/3 complex, resulting in downstream cascades that lead ultimately to activation of nuclear factor (NF)-κB [56], and also initiation of distinct parallel signalling pathways leading to mitogen-activated protein (MAP) kinase [57–59] and phosphoinositide 3-kinase (PI3K) [60,61] activation. PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. Indirect PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. Indirect PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. Indirect PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. PMID: 17223959, 15665823 IRF-5 co-localizes and associates with MyD88 and TRAF-6 and is required for inflammatory cytokine, but not IFN-alpha/beta, production upon stimulation with TLR3, 4, 5, 7/8 and 9 ligands [66]. PMID: 17223959, 16236719 IRF-4 is a negative regulator of the signalling pathway, competing with IRF-5 for association with MyD88 [67]. PMID: 17223959, 16236719 IRF-4 is a negative regulator of the signalling pathway, competing with IRF-5 for association with MyD88 [67]. PMID: 17223959, 14556004 TRIF is recruited selectively by TLR3 and TLR4, although TLR4 requires a fourth adapter molecule, TRAM, to link it to TRIF [70]. PMID: 17223959, 14556004 TRIF is recruited selectively by TLR3 and TLR4, although TLR4 requires a fourth adapter molecule, TRAM, to link it to TRIF [70]. PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. PMID: 17223959, 14556004 TRIF is recruited selectively by TLR3 and TLR4, although TLR4 requires a fourth adapter molecule, TRAM, to link it to TRIF [70]. PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. Indirect PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. Indirect PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. Indirect PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. Indirect PMID: 17223959, 16621716, 11698465 This pathway again utilizes TRAF3, which interacts with TBK-1 and IKK-epsilon to mediate activation of IRF-3 and finally induction of the IFN-beta promoter and several other target genes, for example CXCL10 [71,72]. Indirect Indirect PMID: 17223959, 15064760 TRIF also directly interacts with TRAF6, leading to NF-kappaB and MAP kinase activation, and with receptor-interacting protein (RIP) 1, a kinase thought to play a critical role in NF-kappaB activation [73]. PMID: 17223959, 15064760 TRIF also directly interacts with TRAF6, leading to NF-kappaB and MAP kinase activation, and with receptor-interacting protein (RIP) 1, a kinase thought to play a critical role in NF-kappaB activation [73]. Indirect PMID: 17223959, 15064760 TRIF also directly interacts with TRAF6, leading to NF-kappaB and MAP kinase activation, and with receptor-interacting protein (RIP) 1, a kinase thought to play a critical role in NF-kappaB activation [73]. PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. Indirect PMID: 17223959, 16306937, 16306936, 15361868 In addition, TLR7 and TLR9 signalling via MyD88 can induce the type I interferons (IFNs) in a cascade also involving TRAF3 [62,63] and IFN regulatory factor (IRF)-7, which translocates to the nucleus and induces the IFN-alpha and IFN-beta promoters [64,65]. Indirect PMID: 17223959, 10751418, 9673235 Cytokines such as tumour necrosis factor (TNF)-alpha, interleukin (IL)-1beta and IL-6 are often held to be principal exemplars of the panel of proinflammatory mediators produced in response to TLR stimuli; however, chemokine genes actually show the strongest gene induction [77,80]. Indirect PMID: 17223959, 10751418, 9673235 Cytokines such as tumour necrosis factor (TNF)-alpha, interleukin (IL)-1beta and IL-6 are often held to be principal exemplars of the panel of proinflammatory mediators produced in response to TLR stimuli; however, chemokine genes actually show the strongest gene induction [77,80]. Indirect PMID: 17223959, 10751418, 9673235 Cytokines such as tumour necrosis factor (TNF)-alpha, interleukin (IL)-1beta and IL-6 are often held to be principal exemplars of the panel of proinflammatory mediators produced in response to TLR stimuli; however, chemokine genes actually show the strongest gene induction [77,80]. Indirect PMID: 17223959, 10751418, 8558063, 9242519 CXCL8 and CXCL2/3 are the main CXC family members released in response to TLR activation [77], and are chemotactic primarily for neutrophils augmenting their degranulation, adhesion and microbicidal activity [82]; however, they can also influence T cell, basophil, eosinophil, NK cell and endothelial cell chemotaxis [81]. Indirect PMID: 17223959, 10751418, 8558063, 9242519 CXCL8 and CXCL2/3 are the main CXC family members released in response to TLR activation [77], and are chemotactic primarily for neutrophils augmenting their degranulation, adhesion and microbicidal activity [82]; however, they can also influence T cell, basophil, eosinophil, NK cell and endothelial cell chemotaxis [81]. PMID: 17223959, 16316467 the synthetic viral mimic poly(I:C), which activates TLR3, augments expression of TLR1 and TLR2, receptors that mediate bacterial responses [78]. Indirect PMID: 17223959, 16316467 the synthetic viral mimic poly(I:C), which activates TLR3, augments expression of TLR1 and TLR2, receptors that mediate bacterial responses [78]. Indirect PMID: 17223959, 16316467 the synthetic viral mimic poly(I:C), which activates TLR3, augments expression of TLR1 and TLR2, receptors that mediate bacterial responses [78]. Indirect PMID: 17223959, 10751418, 8558063, 9242519 CXCL8 and CXCL2/3 are the main CXC family members released in response to TLR activation [77], and are chemotactic primarily for neutrophils augmenting their degranulation, adhesion and microbicidal activity [82]; however, they can also influence T cell, basophil, eosinophil, NK cell and endothelial cell chemotaxis [81].