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PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 15558055, 16424225
TLR3 binds double-stranded (ds) RNA which is found in dsRNA viruses, such as reovirus, or is generated during replication of single-stranded (ss) RNA viruses such as West Nile virus or respiratory syncytial virus or as a by-product of symmetrical transcription of viral DNA, for example from herpes viruses.
PMID: 18086372, 15298172, 10933707
By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
PMID: 18086372
TRIF is recruited to the cytoplasmatic TIR domain of TLR3 and interacts with a set of different signaling molecules and kinases which in turn initiate activation of NFkappaB or IRF3 and IRF7 leading to type I interferon induction.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 14976262, 11812998, 14976261
GU-rich ssRNA sequences of viral or host origin, poly-U RNA and specific siRNA sequences are ligands for both receptors, whereas synthetic imidazoquinoline derivatives have been designed to specifically activate TLR7 or TLR8 or both receptors.
PMID: 18086372, 11607032
Another ligand for TLR3 is poly(I:C) which is a synthetic dsRNA mimicking viral infection.
Indirect
PMID: 18086372
Up-regulation of TLR3 expression by type I IFN amplifies the response to TLR3 ligands.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
Indirect
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
Indirect
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 12885884
Two viral proteins of RSV, NS1 and NS2, are involved in blocking the pathway leading to IRF3 phosphorylation, although the activation of NFkappaB and AP-1 is unaffected.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 16127453
This receptor–adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 16127453
This receptor–adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372
NFkappaB activation by TLR3 ligands is mediated in two ways – via association of TRIF with RIP1 or via interaction of TRIF with TRAF6, which in turn activates TAK1.
PMID: 18086372
NFkappaB activation by TLR3 ligands is mediated in two ways – via association of TRIF with RIP1 or via interaction of TRIF with TRAF6, which in turn activates TAK1.
Indirect
PMID: 18086372
NFkappaB activation by TLR3 ligands is mediated in two ways – via association of TRIF with RIP1 or via interaction of TRIF with TRAF6, which in turn activates TAK1.
Indirect
PMID: 18086372, 15064760, 14530355
Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus.
Indirect
PMID: 18086372, 15064760, 14530355
Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus.
PMID: 18086372, 15064760, 14530355
Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus.
PMID: 18086372
Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
PMID: 18086372
Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
PMID: 18086372, 15064760, 14530355
Both RIP1 and TAK1 mediate activation of canonical IKKs (IKKalpha, IKKbeta) resulting in IkappaB degradation and NFkappaB translocation to the nucleus.
PMID: 18086372
Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
PMID: 18086372, 16127453
This receptor–adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
Indirect
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
Indirect
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
Indirect
PMID: 18086372, 12692549, 12702806, 12855817
Interaction of TRIF with TRAF3 allows complex formation with the non-canonical IKKs-TBK1 and IKK-epsilon leading to the activation of IRF3 and IRF7, which form homo- or heterodimers upon phosphorylation and are then translocated to the nucleus to induce type I IFN and IFN inducible gene expression.
Indirect
PMID: 18086372, 17339430
Interestingly, human lung epithelial cells express proinflammatory cytokines including IL-6 and IL-8 upon infection with influenza A virus in a TLR3-dependent manner , suggesting that TLR3-mediated inflammatory responses may also contribute to influenza virus-induced lung pathology in humans.
Indirect
PMID: 18086372, 17339430
Interestingly, human lung epithelial cells express proinflammatory cytokines including IL-6 and IL-8 upon infection with influenza A virus in a TLR3-dependent manner , suggesting that TLR3-mediated inflammatory responses may also contribute to influenza virus-induced lung pathology in humans.
PMID: 18086372
TLR9 has been described to recognize bacterial DNA or synthetic oligodesoxyribonucleotides (ODN) containing specific unmethylated CpG sequence motifs. These can also be found in the genome of DNA viruses.
PMID: 18086372, 15492225, 15361868
Upon ligand binding the TIR domain of TLR9 recruits MyD88 which forms a supramolecular complex with TRAF6, IRAK1, IRAK4 and IRF7.
PMID: 18086372, 15492225, 15361868
Upon ligand binding the TIR domain of TLR9 recruits MyD88 which forms a supramolecular complex with TRAF6, IRAK1, IRAK4 and IRF7.
PMID: 18086372, 15492225, 15361868
Upon ligand binding the TIR domain of TLR9 recruits MyD88 which forms a supramolecular complex with TRAF6, IRAK1, IRAK4 and IRF7.
Indirect
PMID: 18086372
CpG ODN class A, B and C have been designed to trigger primarily type I IFN response (A) or costimulatory molecule expression and inflammatory cytokine production (B) or both (C) in pDCs.
PMID: 18086372, 16864658
Induction of type I IFNs by TLR9 ligands in pDCs depends on retention of the ligand–receptor complex within early endosomes at a pH value between 6.2 and 5.5.
Indirect
PMID: 18086372
CpG ODN class A, B and C have been designed to trigger primarily type I IFN response (A) or costimulatory molecule expression and inflammatory cytokine production (B) or both (C) in pDCs.
PMID: 18086372, 16864658
Delivery of TLR9 ligands to late endosome with lower pH values (<4.5) impairs the induction of type I IFNs and promotes inflammatory cytokine and costimulatory molecule expression in pDCs.
Indirect
PMID: 18086372
CpG ODN class A, B and C have been designed to trigger primarily type I IFN response (A) or costimulatory molecule expression and inflammatory cytokine production (B) or both (C) in pDCs.
PMID: 18086372, 16864658
Delivery of TLR9 ligands to late endosome with lower pH values (<4.5) impairs the induction of type I IFNs and promotes inflammatory cytokine and costimulatory molecule expression in pDCs.
Indirect
PMID: 18086372
During the second phase secreted type I IFNs signal via type I IFN receptor in an autocrine and paracrine manner.
PMID: 18086372
During the second phase secreted type I IFNs signal via type I IFN receptor in an autocrine and paracrine manner.
Indirect
Indirect
PMID: 18086372
Downstream signaling of the type I IFN receptor induces a strong up-regulation of IRF7 production leading to full expression of type I IFN genes (positive feedback loop).
Indirect
PMID: 18086372, 17018642, 17273999
In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1−/− mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
Indirect
PMID: 18086372, 17018642, 17273999
In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1−/− mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
Indirect
PMID: 18086372, 17018642, 17273999
In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1−/− mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
Indirect
PMID: 18086372, 17018642, 17273999
In myeloid DCs IRF1 plays a crucial role in the downstream signaling of TLR9. IRF1−/− mice show an impaired induction of IFN-beta, iNOS and IL-12p35 upon stimulation with TLR9 ligand CpG-B, whereas type I interferon response of pDCs is not affected by lack of IRF1.
Indirect
Indirect
PMID: 18086372
In the very early phase of systemic MCMV infection pDCs and conventional DCs release the first wave of type I interferons and inflammatory cytokines including IL-12.
PMID: 18086372, 8557990
Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
Indirect
PMID: 18086372, 8557990
Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
Indirect
Indirect
PMID: 18086372, 8557990
Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
PMID: 18086372, 8557990
Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
Indirect
Indirect
PMID: 18086372, 8557990
Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
Indirect
PMID: 18086372, 8557990
Control of viral replication and clearance of the virus from infected organs during the first week of MCMV infection relies mostly on NK cells, which produce IFN-gamma (mediated by IL-12 and IL-18) and kill infected cells.
PMID: 18086372
The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
PMID: 18086372
The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
PMID: 18086372
The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
PMID: 18086372
The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
PMID: 18086372
The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
PMID: 18086372
The MyD88-dependent signal transduction pathway downstream of TLR7 and 8 is very similar to TLR9-mediated signaling.
PMID: 18086372
In addition to the TLRs, a new family of viral pattern recognition receptors consisting of RNA helicases retinoic acid inducible gene I (RIG-I), melanoma differentiation antigen 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) – was discovered and characterized in the last 3 years.
PMID: 18086372, 17190814
Saito et al. also identified an analogous RD within the C terminus of LGP2 suggesting that LGP2 might inhibit RIG-I through their RD interactions.
PMID: 18086372, 15298172, 10933707
By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
PMID: 18086372
In addition to the TLRs, a new family of viral pattern recognition receptors consisting of RNA helicases retinoic acid inducible gene I (RIG-I), melanoma differentiation antigen 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) – was discovered and characterized in the last 3 years.
PMID: 18086372, 15298172, 10933707
By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
PMID: 18086372, 15563593, 17049367
The V proteins of this diverse group of viruses bind MDA5 via their highly conserved cysteine-rich C-terminal domain.This suggests that paramyxoviruses use this interaction to reduce the amount of IFN released by infected cells.
PMID: 18086372
In addition to the TLRs, a new family of viral pattern recognition receptors consisting of RNA helicases retinoic acid inducible gene I (RIG-I), melanoma differentiation antigen 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) – was discovered and characterized in the last 3 years.
PMID: 18086372, 16116171
LGP2 is a close relative of RIG-I, which lacks the CARDs, but is capable of binding dsRNA.
PMID: 18086372, 15298172, 10933707
By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
PMID: 18086372
The binding of dsRNA to the helicase domain of RIG-I likely induces a conformational change that exposes the N-terminal CARD domains to recruit its signaling adaptor IPS-1.
PMID: 18086372, 16301520, 16177806
Hepatitis C virus (HCV) encodes the protease NS3/4A which targets IPS-1 by cleaving it at position Cys-508, thereby dislocating it from the mitochondrial membrane and thus abrogating further downstream signaling to type I IFN and NFkappaB-dependent target gene expression.
Indirect
Indirect
PMID: 18086372
These molecules, which are localized in the cytosol, bind specific RNA molecules derived from the genome of different RNA viruses and, with the exception of LGP2 which does not signal itself, trigger a signaling cascade leading to the production of type I IFNs and of proinflammatory cytokines in response to viral infection.
Indirect
Indirect
PMID: 18086372
These molecules, which are localized in the cytosol, bind specific RNA molecules derived from the genome of different RNA viruses and, with the exception of LGP2 which does not signal itself, trigger a signaling cascade leading to the production of type I IFNs and of proinflammatory cytokines in response to viral infection.
PMID: 18086372, 17190814
Saito et al. also identified an analogous RD within the C terminus of LGP2 suggesting that LGP2 might inhibit RIG-I through their RD interactions.
PMID: 18086372, 16153868
Coimmunoprecipitation experiments suggest that IPS-1 interacts with TBK1 and recruits endogenous IRF3 in a virus-inducible manner.
PMID: 18086372, 17079289
Furthermore, it was observed that NS1 colocalizes with RIG-I (Mibayashi et al., 2007), suggesting that NS1 forms a complex with RIG-I and IPS-1 during viral infection, resulting in inhibition of further downstream signaling.
PMID: 18086372, 16153868
Coimmunoprecipitation experiments suggest that IPS-1 interacts with TBK1 and recruits endogenous IRF3 in a virus-inducible manner.
PMID: 18086372, 16127453
This receptor–adapter interaction results in the activation of the noncanonical kinases TBK1/IKK-epsilon, which in turn induces dimerization of phosphorylated IRF3 and IRF7 and translocation to the nucleus where they activate the transcription of type I IFN genes.
PMID: 18086372, 12885884
Two viral proteins of RSV, NS1 and NS2, are involved in blocking the pathway leading to IRF3 phosphorylation, although the activation of NFkappaB and AP-1 is unaffected.
PMID: 18086372, 15919920
IRF3 phosphorylation by TBK1 was identified as target of the Rabies virus phosphoprotein P.
PMID: 18086372, 16858409
Recently, TRAF3 was shown to be critically involved in IPS-1-mediated IFN-alpha production and antiviral responses through a direct interaction between the TRAF domain of TRAF3 and a TRAF interaction motif within IPS-1.
Indirect
Indirect
PMID: 18086372, 16858409
Recently, TRAF3 was shown to be critically involved in IPS-1-mediated IFN-alpha production and antiviral responses through a direct interaction between the TRAF domain of TRAF3 and a TRAF interaction motif within IPS-1.
PMID: 18086372, 15549108
RIP1 and FADD are additional molecules that have been reported to be required for type I IFN production in response to dsRNA.
Indirect
Indirect
PMID: 18086372, 15549108
RIP1 and FADD are additional molecules that have been reported to be required for type I IFN production in response to dsRNA.
Indirect
Indirect
PMID: 18086372, 17327220
There is evidence that the TBK1/IKK-epsilon adaptor protein TANK plays a role in IPS-1-TRAF3-mediated activation of TBK1/IKK-epsilon.
PMID: 18086372, 16125763, 16153868
IPS-1 binds to TRAF6 upon overexpression in mammalian cells and in a yeast-two hybrid screen reported that endogenous IPS-1 also interacts with TRAF6.
Indirect
PMID: 18086372
Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
Indirect
PMID: 18086372
Another branch of IPS-1 signaling leads to the activation of the IKK complex resulting in activation of NFkappaB that controls the expression of genes encoding inflammatory responses, but also expression of IFN-beta.
PMID: 18086372, 17038590
Taken together, the results of Hornung et al.(2006) show that RIG-I directly recognizes 5′-triphosphate single stranded or double stranded RNA independently of viral replication.
Indirect
PMID: 18086372, 12015121
It was reported in a previous publication, that MDA5, which was then called Helicard, is cleaved by caspases upon induction of apoptosis, thereby separating the CARD domains from the C-terminal helicase domain, which localizes to the nucleus where it is involved in DNA degradation and nuclear remodelling during apoptotic cell death.
Indirect
PMID: 18086372, 12015121
It was reported in a previous publication, that MDA5, which was then called Helicard, is cleaved by caspases upon induction of apoptosis, thereby separating the CARD domains from the C-terminal helicase domain, which localizes to the nucleus where it is involved in DNA degradation and nuclear remodelling during apoptotic cell death.
Indirect
PMID: 18086372, 12015121
It was reported in a previous publication, that MDA5, which was then called Helicard, is cleaved by caspases upon induction of apoptosis, thereby separating the CARD domains from the C-terminal helicase domain, which localizes to the nucleus where it is involved in DNA degradation and nuclear remodelling during apoptotic cell death.
Indirect
PMID: 18086372
MDA5 is ubiquitously expressed in low abundance and similarly to RIG-I and LGP2 its expression is induced by type I IFN.
Indirect
PMID: 18086372
MDA5 is ubiquitously expressed in low abundance and similarly to RIG-I and LGP2 its expression is induced by type I IFN.
Indirect
PMID: 18086372
MDA5 is ubiquitously expressed in low abundance and similarly to RIG-I and LGP2 its expression is induced by type I IFN.
PMID: 18086372
Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
PMID: 18086372, 16301520, 16177806
Hepatitis C virus (HCV) encodes the protease NS3/4A which targets IPS-1 by cleaving it at position Cys-508, thereby dislocating it from the mitochondrial membrane and thus abrogating further downstream signaling to type I IFN and NFkappaB-dependent target gene expression.
Indirect
PMID: 18086372
Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
PMID: 18086372
Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
Indirect
PMID: 18086372
Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
Indirect
PMID: 18086372
Like RIG-I, MDA5 interacts with the adapter protein IPS-1 upon ligand binding leading to activation of protein kinases that subsequently activate transcription factors IRF3, IRF7 and NFkappaB, respectively.
PMID: 18086372, 12885884
Two viral proteins of RSV, NS1 and NS2, are involved in blocking the pathway leading to IRF3 phosphorylation, although the activation of NFkappaB and AP-1 is unaffected.
PMID: 18086372, 15919920
IRF3 phosphorylation by TBK1 was identified as target of the Rabies virus phosphoprotein P.
Indirect
PMID: 18086372
In addition, it was shown that MDA5 might also play a role in the measles virus (MV) induced activation of IFN-beta mRNA synthesis since A549 cells transfected with MDA5 showed a strong activation of the IFN-beta promoter upon infection with MV.
PMID: 18086372, 15298172, 10933707
By binding to dsRNA NS1 disguises the viral dsRNA pattern from the cytoplasmic receptors and inhibits IFN-alpha/INF-beta induction via IRF3.
PMID: 18086372, 17079289
Furthermore, it was observed that NS1 colocalizes with RIG-I (Mibayashi et al., 2007), suggesting that NS1 forms a complex with RIG-I and IPS-1 during viral infection, resulting in inhibition of further downstream signaling.
PMID: 18086372, 15563593, 17049367
The V proteins of this diverse group of viruses bind MDA5 via their highly conserved cysteine-rich C-terminal domain.This suggests that paramyxoviruses use this interaction to reduce the amount of IFN released by infected cells.
Indirect
Indirect
PMID: 18086372
Degradation of MDA5 in poliovirus-infected cells occurs in a proteasome- and caspase-dependent manner and correlates with the induction of apoptosis in poliovirus-infected cells.
Indirect
PMID: 18086372, 16301520, 16177806
Hepatitis C virus (HCV) encodes the protease NS3/4A which targets IPS-1 by cleaving it at position Cys-508, thereby dislocating it from the mitochondrial membrane and thus abrogating further downstream signaling to type I IFN and NFkappaB-dependent target gene expression.
Indirect
PMID: 18086372
Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
Indirect
PMID: 18086372
Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
Indirect
Indirect
PMID: 18086372
Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.
Indirect
Indirect
PMID: 18086372
Apart from activating the NFkappaB and MAPK signaling pathways leading to inflammatory cytokine and chemokine production as well as costimulatory molecule expression, the intracellularly localized nucleic acid recognition receptors TLR3, 7, 8 and 9 specifically trigger type I interferon production via MyD88- and TRIF-dependent signaling pathways.