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PMID: 18280610, 15208624, 15563593 RNA viruses are efficiently recognized by the cytoplasmic RNA helicases, retinoic acid-inducible gene-I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5). PMID: 18280610 Both of these proteins recognize viral RNA through their helicase domains.

PMID: 18280610, 15208624, 15563593 RNA viruses are efficiently recognized by the cytoplasmic RNA helicases, retinoic acid-inducible gene-I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5). PMID: 18280610 Both of these proteins recognize viral RNA through their helicase domains.

PMID: 18280610, 16125763, 16127453, 16177806 Both RIG-I and MDA5 utilize a common adaptor molecule termed MAVS [29], IPS-1 [30], Cardif [31], or VISA [32], which was independently identified by multiple groups and localizes to the mitochondrial membrane.

PMID: 18280610, 16125763, 16127453, 16177806 Both RIG-I and MDA5 utilize a common adaptor molecule termed MAVS [29], IPS-1 [30], Cardif [31], or VISA [32], which was independently identified by multiple groups and localizes to the mitochondrial membrane.

PMID: 18280610, 16641297 Double stranded RNA intermediates are produced during the replication cycle of most viruses, including viruses with DNA genomes [47], and these RNA secondary structures are thought to be recognized by TLR3.

PMID: 18280610, 16625202, 16714379 It is clear that TLR3 responds to the artificial dsRNA mimic, polyiosinic-polycytidylic acid (polyIC), when it is provided extracellularly.

PMID: 18280610, 11812998 TLR7 was originally shown to be responsible for mediating the antiviral effects induced following delivery of imidazoquinoline compounds.

PMID: 18280610, 15123819 It is now clear that TLR7 and TLR8 recognize single stranded RNA (ssRNA) and induce innate immune responses to ssRNA-viruses. PMID: 18280610, 14976262 TLR7-dependent signaling was also induced following delivery of single stranded RNA oligonucleotides derived from human immunodeficiency virus (HIV) RNA.

PMID: 18280610, 15123819 It is now clear that TLR7 and TLR8 recognize single stranded RNA (ssRNA) and induce innate immune responses to ssRNA-viruses.

PMID: 18280610, 11130078 In this case, it is the recognition of viral DNA that stimulates TLR9. Bacterial DNA sequences containing hypomethylated CpG motifs were first shown to activate TLR9. PMID: 18280610, 12900525 As predicted, this response was dependent upon acidification of the endosome, as treatment with chloroquine or bafilomycin [61] abrogated recognition.

PMID: 18280610, 15815647 Furthermore, Honda et al. demonstrated that the ability of pDCs to retain the TLR9 ligand, CpG DNA, in the endosomal vesicle for long periods of time is critical to recruit a signaling complex containing MyD88 and the transcription factor IRF-7.

PMID: 18280610, 17618271 Recently, Takaoka et al. identified the DAI protein (also known as DLM-1/ZBP1) as a candidate intracellular DNA sensing molecule. PMID: 18280610 DAI physically interacts with the B form of DNA in the cytosol and recruits an anti-viral signaling complex that results in the activation of NF-kappaB and the production of type I IFNs.

PMID: 18280610 DAI physically interacts with the B form of DNA in the cytosol and recruits an anti-viral signaling complex that results in the activation of NF-kappaB and the production of type I IFNs.

Indirect

PMID: 18280610 DAI physically interacts with the B form of DNA in the cytosol and recruits an anti-viral signaling complex that results in the activation of NF-kappaB and the production of type I IFNs.

Indirect

Indirect

PMID: 18280610 DAI physically interacts with the B form of DNA in the cytosol and recruits an anti-viral signaling complex that results in the activation of NF-kappaB and the production of type I IFNs.

PMID: 18280610, 17452530 Recently, Brinkmann et al. demonstrated a physical interaction between wild type, but not mutated, UNC-93B and all three endosomal TLRs (TLR3, 7, and 9).

PMID: 18280610, 17452530 Recently, Brinkmann et al. demonstrated a physical interaction between wild type, but not mutated, UNC-93B and all three endosomal TLRs (TLR3, 7, and 9).

PMID: 18280610, 17452530 Recently, Brinkmann et al. demonstrated a physical interaction between wild type, but not mutated, UNC-93B and all three endosomal TLRs (TLR3, 7, and 9).

PMID: 18280610, 16177057 Of note, an additional report demonstrated that TLR2 induces apoptosis of HSV-infected microgial cells, potentially implicating microglial cells in the regulation of the inflammatory response following HSV infection.

Indirect PMID: 18280610, 16177057 Of note, an additional report demonstrated that TLR2 induces apoptosis of HSV-infected microgial cells, potentially implicating microglial cells in the regulation of the inflammatory response following HSV infection.

PMID: 18280610, 12163593 Recently, Bieback et al. demonstrated that the HA protein of Measles virus induces cytokine secretion in a TLR2-dependent manner.

Indirect

Indirect

PMID: 18280610, 12163593 Recently, Bieback et al. demonstrated that the HA protein of Measles virus induces cytokine secretion in a TLR2-dependent manner.

Indirect

PMID: 18280610, 12163593 Interestingly, this interaction also results in upregulated expression of the MV receptor, CD150, suggesting that HA-TLR2 interactions in fact benefit the virus at the expense of the host unless increased infection can be viewed as an effective antiviral strategy.

PMID: 18280610, 12730691 Likewise, the interaction of the MMTV env protein with TLR4 provides a selective advantage to the virus by promoting infection of target cells, transcription of the viral genome, and release of the immunoregulatory cytokine, IL-10.

Indirect

Indirect

PMID: 18280610, 12730691 Likewise, the interaction of the MMTV env protein with TLR4 provides a selective advantage to the virus by promoting infection of target cells, transcription of the viral genome, and release of the immunoregulatory cytokine, IL-10.

Indirect

PMID: 18280610 For example, the induction of IFNalpha by VSV, SeV, and Flu in pDCs is completely dependent upon TLR7.

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

Indirect

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

Indirect

PMID: 18280610, 15229469 TIR domain-containing adaptor molecules, MyD88, which is utilized by all TLRs except for TLR3, as well as TIRAP, TRIF, and TRAM (for TLR4), are recruited to the receptor and activate a complex containing IRAKs and TRAFs which signal through NF-kappaB.

Indirect

PMID: 18280610 Ultimately, TLR stimulation culminates in the synthesis of antiviral cytokines, such as type I IFNs, IL-1beta, and IL-6, which may directly suppress viral replication.

Indirect

PMID: 18280610 Ultimately, TLR stimulation culminates in the synthesis of antiviral cytokines, such as type I IFNs, IL-1beta, and IL-6, which may directly suppress viral replication.

Indirect

PMID: 18280610 Ultimately, TLR stimulation culminates in the synthesis of antiviral cytokines, such as type I IFNs, IL-1beta, and IL-6, which may directly suppress viral replication.

PMID: 18280610, 14976261, 14976262, 17111347 TLR7 recognition of viral RNA, synthetic polyU RNA, and even non-viral, cellular RNA in the endosome is sufficient to stimulate TLR7-dependent cytokine production.

PMID: 18280610, 14976261, 14976262, 17111347 TLR7 recognition of viral RNA, synthetic polyU RNA, and even non-viral, cellular RNA in the endosome is sufficient to stimulate TLR7-dependent cytokine production.

Indirect

Indirect

PMID: 18280610, 14976261, 14976262, 17111347 TLR7 recognition of viral RNA, synthetic polyU RNA, and even non-viral, cellular RNA in the endosome is sufficient to stimulate TLR7-dependent cytokine production.

Indirect

Indirect

PMID: 18280610, 14976261, 14976262, 17111347 TLR7 recognition of viral RNA, synthetic polyU RNA, and even non-viral, cellular RNA in the endosome is sufficient to stimulate TLR7-dependent cytokine production.

Indirect

Indirect

PMID: 18280610, 14976261, 14976262, 17111347 TLR7 recognition of viral RNA, synthetic polyU RNA, and even non-viral, cellular RNA in the endosome is sufficient to stimulate TLR7-dependent cytokine production.

Indirect

PMID: 18280610, 17653195 The authors demonstrated that cellular RNAs cleaved by the antiviral endoribonuclease, RNaseL, which contain 3' monophosphoryl group, efficiently serve as a ligand for both RIG-I and MDA5.

PMID: 18280610, 17653195 The authors demonstrated that cellular RNAs cleaved by the antiviral endoribonuclease, RNaseL, which contain 3' monophosphoryl group, efficiently serve as a ligand for both RIG-I and MDA5.

PMID: 18280610, 17653195 The authors demonstrated that cellular RNAs cleaved by the antiviral endoribonuclease, RNaseL, which contain 3' monophosphoryl group, efficiently serve as a ligand for both RIG-I and MDA5.