ArticleThe Journal of biological chemistry2012
Targeting Toll-like receptor (TLR) signaling by Toll/interleukin-1 receptor (TIR) domain-containing adapter protein/MyD88 adapter-like (TIRAP/Mal)-derived decoy peptides.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 70 citations in OpenAlex.
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- TLR5-Derived, TIR-Interacting Decoy Peptides to Inhibit TLR Signaling.Journal of immunology (Baltimore, Md. : 1950) · 2023Article
- Molecular mechanisms of lidocaine.Annals of medicine and surgery (2012) · 2021Review
- Targeting TLR4 Signaling to Blunt Viral-Mediated Acute Lung Injury.Frontiers in immunology · 2021Review
- Frontline Science: Targeting the TLR7 signalosome assembly.Journal of leukocyte biology · 2020Article
- A survey of TIR domain sequence and structure divergence.Immunogenetics · 2020Article
- A peptide derived from the core β-sheet region of TIRAP decoys TLR4 and reduces inflammatory and autoimmune symptoms in murine models.EBioMedicine · 2020Article
- Lipoproteins Contribute to the Anti-inflammatory Capacity ofFrontiers in microbiology · 2020Article
- Targeting the TLR signalosome with TIR domain-derived cell-permeable decoy peptides: the current state and perspectives.Innate immunity · 2020Review
- Select targeting of intracellular Toll-interleukin-1 receptor resistance domains for protection against influenza-induced disease.Innate immunity · 2020Article
- TIR/BB-loop mimetic AS-1 protects vascular endothelial cells from injury induced by hypoxia/reoxygenation.Journal of biomedical research · 2019Article
- Bacterial TIR domain-derived peptides inhibit innate immune signaling and catabolic responses in chondrocyte.Molecular biology reports · 2019Article
- INH14, a Small-Molecule Urea Derivative, Inhibits the IKKα/β-Dependent TLR Inflammatory Response.Chembiochem : a European journal of chemical biology · 2019Article
- Blocking TIR Domain Interactions in TLR9 Signaling.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- Computational Insight Into the Structural Organization of Full-Length Toll-Like Receptor 4 Dimer in a Model Phospholipid Bilayer.Frontiers in immunology · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Toll/interleukin-1 receptor (TIR) domain-containing adapter protein/MyD88 adapter-like (TIRAP/Mal) is an adapter protein that facilitates recruitment of MyD88 to TLR4 and TLR2 signaling complexes. We previously generated a library of cell-permeating TLR4 TIR-derived decoy peptides fused to the translocating segment of the Drosophila Antennapedia homeodomain and examined each peptide for the ability to inhibit TLR4 signaling (Toshchakov, V. Y., Szmacinski, H., Couture, L. A., Lakowicz, J. R., and Vogel, S. N. (2011) J. Immunol. 186, 4819-4827). We have now expanded this study to test TIRAP decoy peptides. Five TIRAP peptides, TR3 (for TIRAP region 3), TR5, TR6, TR9, and TR11, inhibited LPS-induced cytokine mRNA expression and MAPK activation. Inhibition was confirmed at the protein level; select peptides abolished the LPS-induced cytokine production measured in cell culture 24 h after a single treatment. Two of the TLR4 inhibitory peptides, TR3 and TR6, also inhibited cytokine production induced by a TLR2/TLR1 agonist, S-(2,3-bis(palmitoyloxy)-(2R,2S)-propyl)-N-palmitoyl-(R)-Cys-Ser-Lys(4)-OH; however, a higher peptide concentration was required to achieve comparable inhibition of TLR2 versus TLR4 signaling. Two TLR4 inhibitory peptides, TR5 and TR6, were examined for the ability to inhibit TLR4-driven cytokine induction in mice. Pretreatment with either peptide significantly reduced circulating TNF-α and IL-6 in mice following LPS injection. This study has identified novel TLR inhibitory peptides that block cellular signaling at low micromolar concentrations in vitro and in vivo. Comparison of TLR4 inhibition by TLR4 and TIRAP TIR-derived peptides supports the view that structurally diverse regions mediate functional interactions of TIR domains.
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