Accessory molecules for Toll-like receptors and their function (original) (raw)

• Janeway, C. A. Jr & Medzhitov, R. Introduction: the role of innate immunity in the adaptive immune response. Semin. Immunol. 10, 349–350 (1998).
  Article PubMed Google Scholar
• Bianchi, M. E. DAMPs, PAMPs and alarmins: all we need to know about danger. J. Leukoc. Biol. 81, 1–5 (2007).
  Article CAS PubMed Google Scholar
• Kang, J. Y. & Lee, J.-O. Structural biology of the Toll-like receptor family. Annu. Rev. Biochem. 80, 917–941 (2011).
  Article CAS PubMed Google Scholar
• Kawai, T. & Akira, S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nature Immunol. 11, 373–384 (2010).
  Article CAS Google Scholar
• O'Neill, L. A. & Bowie, A. G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nature Rev. Immunol. 7, 353–364 (2007).
  CAS Google Scholar
• Trinchieri, G. & Sher, A. Cooperation of Toll-like receptor signals in innate immune defence. Nature Rev. Immunol. 7, 179–190 (2007).
  CAS Google Scholar
• Liew, F. Y., Xu, D., Brint, E. K. & O'Neill, L. A. Negative regulation of Toll-like receptor-mediated immune responses. Nature Rev. Immunol. 5, 446–458 (2005).
  Article CAS Google Scholar
• Schroder, K. & Tschopp, J. The inflammasomes. Cell 140, 821–832 (2010).
  Article CAS PubMed Google Scholar
• Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805–820 (2010).
  Article CAS PubMed Google Scholar
• Ting, J. P., Duncan, J. A. & Lei, Y. How the noninflammasome NLRs function in the innate immune system. Science 327, 286–290 (2010).
  Article CAS PubMed PubMed Central Google Scholar
• Tschopp, J. & Schroder, K. NLRP3 inflammasome activation: the convergence of multiple signalling pathways on ROS production? Nature Rev. Immunol. 10, 210–215 (2010).
  Article CAS Google Scholar
• Ulevitch, R. J. & Tobias, P. S. Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu. Rev. Immunol. 13, 437–457 (1995).
  Article CAS PubMed Google Scholar
• Jiang, Z. et al. CD14 is required for MyD88-independent LPS signaling. Nature Immunol. 6, 565–570 (2005).
  Article CAS Google Scholar
• Dziarski, R., Tapping, R. I. & Tobias, P. S. Binding of bacterial peptidoglycan to CD14. J. Biol. Chem. 273, 8680–8690 (1998).
  Article CAS PubMed Google Scholar
• Schroder, N. W. et al. Lipopolysaccharide binding protein binds to triacylated and diacylated lipopeptides and mediates innate immune responses. J. Immunol. 173, 2683–2691 (2004).
  Article PubMed Google Scholar
• Schroder, N. W. et al. Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved. J. Biol. Chem. 278, 15587–15594 (2003).
  Article PubMed Google Scholar
• Jack, R. S. et al. Lipopolysaccharide-binding protein is required to combat a murine Gram-negative bacterial infection. Nature 389, 742–745 (1997).
  Article CAS PubMed Google Scholar
• Weber, J. R. et al. Recognition of pneumococcal peptidoglycan: an expanded, pivotal role for LPS binding protein. Immunity 19, 269–279 (2003).
  Article CAS PubMed Google Scholar
• Shimazu, R. et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 189, 1777–1782 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Nagai, Y. et al. Essential role of MD-2 in LPS responsiveness and TLR4 distribution. Nature Immunol. 3, 667–672 (2002).
  Article CAS Google Scholar
• Park, B. S. et al. The structural basis of lipopolysaccharide recognition by the TLR4–MD-2 complex. Nature 458, 1191–1195 (2009). This paper is the first description of the crystal structure of a TLR in complex with its ligand and an accessory molecule.
  Article CAS PubMed Google Scholar
• Calvo, D., Dopazo, J. & Vega, M. A. The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: cellular distribution, chromosomal location, and genetic evolution. Genomics 25, 100–106 (1995).
  Article CAS PubMed Google Scholar
• Triantafilou, M. et al. Membrane sorting of Toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers at the cell surface determines heterotypic associations with CD36 and intracellular targeting. J. Biol. Chem. 281, 31002–31011 (2006).
  Article CAS PubMed Google Scholar
• Hoebe, K. et al. CD36 is a sensor of diacylglycerides. Nature 433, 523–527 (2005).
  Article CAS PubMed Google Scholar
• Stuart, L. M. et al. Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain. J. Cell Biol. 170, 477–485 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Stewart, C. R. et al. CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer. Nature Immunol. 11, 155–161 (2010).
  Article CAS Google Scholar
• Tao, N., Wagner, S. J. & Lublin, D. M. CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails. J. Biol. Chem. 271, 22315–22320 (1996).
  Article CAS PubMed Google Scholar
• Baumann, C. L. et al. CD14 is a coreceptor of Toll-like receptors 7 and 9. J. Exp. Med. 207, 2689–2701 (2010).
  Article CAS PubMed PubMed Central Google Scholar
• Hailman, E. et al. Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14. J. Exp. Med. 179, 269–277 (1994).
  Article CAS PubMed Google Scholar
• Lee, H. K., Dunzendorfer, S., Soldau, K. & Tobias, P. S. Double-stranded RNA-mediated TLR3 activation is enhanced by CD14. Immunity 24, 153–163 (2006). This paper provided the first concrete evidence that CD14 is important for endosomal TLRs in addition to surface TLRs.
  Article CAS PubMed Google Scholar
• Nakata, T. et al. CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex. Cell. Microbiol. 8, 1899–1909 (2006).
  Article CAS PubMed Google Scholar
• Kim, J. I. et al. Crystal structure of CD14 and its implications for lipopolysaccharide signaling. J. Biol. Chem. 280, 11347–11351 (2005).
  Article CAS PubMed Google Scholar
• Haziot, A. et al. Resistance to endotoxin shock and reduced dissemination of Gram-negative bacteria in CD14-deficient mice. Immunity 4, 407–414 (1996).
  Article CAS PubMed Google Scholar
• Zanoni, I. et al. CD14 controls the LPS-induced endocytosis of Toll-like receptor 4. Cell 147, 868–880 (2011). This was the first description of LPS-induced trafficking of TLR4 by CD14.
  Article CAS PubMed PubMed Central Google Scholar
• Akashi-Takamura, S. & Miyake, K. TLR accessory molecules. Curr. Opin. Immunol. 20, 420–425 (2008).
  Article CAS PubMed Google Scholar
• da Silva Correia, J., Soldau, K., Christen, U., Tobias, P. S. & Ulevitch, R. J. Lipopolysaccharide is in close proximity to each of the proteins in its membrane receptor complex: transfer from CD14 to TLR4 and MD-2. J. Biol. Chem. 276, 21129–21135 (2001).
  Article CAS PubMed Google Scholar
• Gioannini, T. L. et al. Isolation of an endotoxin–MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations. Proc. Natl Acad. Sci. USA 101, 4186–4191 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Compton, T. et al. Human cytomegalovirus activates inflammatory cytokine responses via CD14 and Toll-like receptor 2. J. Virol. 77, 4588–4596 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Georgel, P. et al. Vesicular stomatitis virus glycoprotein G activates a specific antiviral Toll-like receptor 4-dependent pathway. Virology 362, 304–313 (2007).
  Article CAS PubMed Google Scholar
• Kurt-Jones, E. A. et al. Pattern recognition receptors TLR4 and CD14 mediate response to respiratory syncytial virus. Nature Immunol. 1, 398–401 (2000).
  Article CAS Google Scholar
• Carpenter, S. et al. TRIL, a functional component of the TLR4 signaling complex, highly expressed in brain. J. Immunol. 183, 3989–3995 (2009).
  Article CAS PubMed Google Scholar
• Carpenter, S., Wochal, P., Dunne, A. & O'Neill, L. A. Toll-like receptor 3 (TLR3) signaling requires TLR4 interactor with leucine-rich repeats (TRIL). J. Biol. Chem. 286, 38795–38804 (2011).
  Article CAS PubMed PubMed Central Google Scholar
• Kessenbrock, K. et al. Proteinase 3 and neutrophil elastase enhance inflammation in mice by inactivating antiinflammatory progranulin. J. Clin. Invest. 118, 2438–2447 (2008).
  CAS PubMed PubMed Central Google Scholar
• Zhu, J. et al. Conversion of proepithelin to epithelins: roles of SLPI and elastase in host defense and wound repair. Cell 111, 867–878 (2002).
  Article CAS PubMed Google Scholar
• Park, B. et al. Granulin is a soluble cofactor for Toll-like receptor 9 signaling. Immunity 34, 505–513 (2011). Here, granulin was shown to have an essential role in ligand delivery for TLR9 activation.
  Article PubMed CAS Google Scholar
• Lotze, M. T. & Tracey, K. J. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nature Rev. Immunol. 5, 331–342 (2005).
  Article CAS Google Scholar
• Andersson, U. & Tracey, K. J. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 29, 139–162 (2011).
  Article CAS PubMed PubMed Central Google Scholar
• Ivanov, S. et al. A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA. Blood 110, 1970–1981 (2007).
  Article CAS PubMed PubMed Central Google Scholar
• Tian, J. et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nature Immunol. 8, 487–496 (2007). This work first reported a role for HMGB1 in delivering DNA to TLR9.
  Article CAS Google Scholar
• Urbonaviciute, V. et al. Induction of inflammatory and immune responses by HMGB1–nucleosome complexes: implications for the pathogenesis of SLE. J. Exp. Med. 205, 3007–3018 (2008).
  Article CAS PubMed PubMed Central Google Scholar
• Leadbetter, E. A. et al. Chromatin–IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors. Nature 416, 603–607 (2002).
  Article CAS PubMed Google Scholar
• Avalos, A. M. et al. RAGE-independent autoreactive B cell activation in response to chromatin and HMGB1/DNA immune complexes. Autoimmunity 43, 103–110 (2010).
  Article CAS PubMed PubMed Central Google Scholar
• Yanai, H. et al. HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses. Nature 462, 99–103 (2009).
  Article CAS PubMed Google Scholar
• Lande, R. et al. Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature 449, 564–569 (2007). This paper demonstrated the role of LL37 in DNA delivery to TLR9 in pDCs.
  Article CAS PubMed Google Scholar
• Gilliet, M. & Lande, R. Antimicrobial peptides and self-DNA in autoimmune skin inflammation. Curr. Opin. Immunol. 20, 401–407 (2008).
  CAS PubMed Google Scholar
• Zanetti, M., Gennaro, R. & Romeo, D. The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils. Ann. NY Acad. Sci. 832, 147–162 (1997).
  Article CAS PubMed Google Scholar
• Ganguly, D. et al. Self-RNA–antimicrobial peptide complexes activate human dendritic cells through TLR7 and TLR8. J. Exp. Med. 206, 1983–1994 (2009).
  Article CAS PubMed PubMed Central Google Scholar
• Yang, Y. & Li, Z. Roles of heat shock protein gp96 in the ER quality control: redundant or unique function? Mol. Cells 20, 173–182 (2005).
  Article CAS PubMed Google Scholar
• Liu, B. & Li, Z. Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin. Blood 112, 1223–1230 (2008).
  Article CAS PubMed PubMed Central Google Scholar
• Randow, F. & Seed, B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nature Cell Biol. 3, 891–896 (2001).
  Article CAS PubMed Google Scholar
• Wanderling, S. et al. GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion. Mol. Biol. Cell 18, 3764–3775 (2007).
  Article CAS PubMed PubMed Central Google Scholar
• Yang, Y. et al. Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages. Immunity 26, 215–226 (2007).
  Article PubMed PubMed Central CAS Google Scholar
• Staron, M. et al. Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex. Blood 117, 7136–7144 (2011).
  Article CAS PubMed PubMed Central Google Scholar
• Liu, B. et al. Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Nature Commun. 1, 79 (2010). This paper shows that GRP94 and PRAT4A work together to chaperone TLRs.
  Article CAS Google Scholar
• Wakabayashi, Y. et al. A protein associated with Toll-like receptor 4 (PRAT4A) regulates cell surface expression of TLR4. J. Immunol. 177, 1772–1779 (2006).
  Article CAS PubMed Google Scholar
• Takahashi, K. et al. A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is required for TLR-dependent immune responses. J. Exp. Med. 204, 2963–2976 (2007).
  Article CAS PubMed PubMed Central Google Scholar
• Kiyokawa, T. et al. A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors. Int. Immunol. 20, 1407–1415 (2008).
  Article CAS PubMed Google Scholar
• Tabeta, K. et al. The Unc93b1 mutation 3d disrupts exogenous antigen presentation and signaling via Toll-like receptors 3, 7 and 9. Nature Immunol. 7, 156–164 (2006).
  Article CAS Google Scholar
• Casrouge, A. et al. Herpes simplex virus encephalitis in human UNC-93B deficiency. Science 314, 308–312 (2006).
  Article CAS PubMed Google Scholar
• Brinkmann, M. M. et al. The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling. J. Cell Biol. 177, 265–275 (2007).
  Article CAS PubMed PubMed Central Google Scholar
• Kim, Y. M., Brinkmann, M. M., Paquet, M. E. & Ploegh, H. L. UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes. Nature 452, 234–238 (2008). This paper provides evidence for the role of UNC93B1 in the trafficking of endosomal TLRs.
  Article CAS PubMed Google Scholar
• Fukui, R. et al. Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic cells toward DNA- but against RNA-sensing. J. Exp. Med. 206, 1339–1350 (2009).
  Article CAS PubMed PubMed Central Google Scholar
• Fukui, R. et al. Unc93B1 restricts systemic lethal inflammation by orchestrating Toll-like receptor 7 and 9 trafficking. Immunity 35, 69–81 (2011).
  Article CAS PubMed Google Scholar
• Nakatsu, F. & Ohno, H. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct. Funct. 28, 419–429 (2003).
  Article CAS PubMed Google Scholar
• Sasai, M., Linehan, M. M. & Iwasaki, A. Bifurcation of Toll-like receptor 9 signaling by adaptor protein 3. Science 329, 1530–1534 (2010). This study was the first to demonstrate that AP3 has a role in TLR9-dependent IFN responses.
  Article CAS PubMed PubMed Central Google Scholar
• Blasius, A. L. et al. Slc15a4, AP-3, and Hermansky-Pudlak syndrome proteins are required for Toll-like receptor signaling in plasmacytoid dendritic cells. Proc. Natl Acad. Sci. USA 107, 19973–19978 (2010).
  Article CAS PubMed PubMed Central Google Scholar
• Guiducci, C. et al. Properties regulating the nature of the plasmacytoid dendritic cell response to Toll-like receptor 9 activation. J. Exp. Med. 203, 1999–2008 (2006).
  Article CAS PubMed PubMed Central Google Scholar
• Honda, K. et al. Spatiotemporal regulation of MyD88–IRF-7 signalling for robust type-I interferon induction. Nature 434, 1035–1040 (2005).
  Article CAS PubMed Google Scholar
• Ewald, S. E. et al. The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor. Nature 456, 658–662 (2008).
  Article CAS PubMed PubMed Central Google Scholar
• Park, B. et al. Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9. Nature Immunol. 9, 1407–1414 (2008). References 79 and 80 demonstrate the cleavage requirement for TLR9 activation by CpG DNA.
  Article CAS Google Scholar
• Asagiri, M. et al. Cathepsin K-dependent Toll-like receptor 9 signaling revealed in experimental arthritis. Science 319, 624–627 (2008).
  Article CAS PubMed Google Scholar
• Matsumoto, F. et al. Cathepsins are required for Toll-like receptor 9 responses. Biochem. Biophys. Res. Commun. 367, 693–699 (2008).
  Article CAS PubMed Google Scholar
• Sepulveda, F. E. et al. Critical role for asparagine endopeptidase in endocytic Toll-like receptor signaling in dendritic cells. Immunity 31, 737–748 (2009). This is the first demonstration of a role for AEP in TLR9 activation in primary DCs.
  Article CAS PubMed Google Scholar
• Ewald, S. E. et al. Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase. J. Exp. Med. 208, 643–651 (2011).
  Article CAS PubMed PubMed Central Google Scholar
• Saitoh, T. et al. Antiviral protein Viperin promotes Toll-like receptor 7- and Toll-like receptor 9-mediated type I interferon production in plasmacytoid dendritic cells. Immunity 34, 352–363 (2011).
  Article CAS PubMed Google Scholar
• Gerold, G. et al. A Toll-like receptor 2–integrin β3 complex senses bacterial lipopeptides via vitronectin. Nature Immunol. 9, 761–768 (2008).
  Article CAS Google Scholar
• Kagan, J. C. & Medzhitov, R. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 125, 943–955 (2006).
  Article CAS PubMed Google Scholar
• Gantner, B. N., Simmons, R. M., Canavera, S. J., Akira, S. & Underhill, D. M. Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. J. Exp. Med. 197, 1107–1117 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Nagai, Y. et al. The radioprotective 105/MD-1 complex links TLR2 and TLR4/MD-2 in antibody response to microbial membranes. J. Immunol. 174, 7043–7049 (2005).
  Article CAS PubMed Google Scholar
• Divanovic, S. et al. Negative regulation of Toll-like receptor 4 signaling by the Toll-like receptor homolog RP105. Nature Immunol. 6, 571–578 (2005).
  Article CAS Google Scholar
• Blumenthal, A. et al. RP105 facilitates macrophage activation by Mycobacterium tuberculosis lipoproteins. Cell Host Microbe 5, 35–46 (2009).
  Article CAS PubMed PubMed Central Google Scholar
• Uccellini, M. B. et al. Autoreactive B cells discriminate CpG-rich and CpG-poor DNA and this response is modulated by IFN-α. J. Immunol. 181, 5875–5884 (2008).
  Article CAS PubMed Google Scholar
• Viglianti, G. A. et al. Activation of autoreactive B cells by CpG dsDNA. Immunity 19, 837–847 (2003).
  Article CAS PubMed Google Scholar
• Lau, C. M. et al. RNA-associated autoantigens activate B cells by combined B cell antigen receptor/Toll-like receptor 7 engagement. J. Exp. Med. 202, 1171–1177 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Chaturvedi, A., Dorward, D. & Pierce, S. K. The B cell receptor governs the subcellular location of Toll-like receptor 9 leading to hyperresponses to DNA-containing antigens. Immunity 28, 799–809 (2008).
  Article CAS PubMed PubMed Central Google Scholar
• Avalos, A. M. et al. Differential cytokine production and bystander activation of autoreactive B cells in response to CpG-A and CpG-B oligonucleotides. J. Immunol. 183, 6262–6268 (2009).
  Article CAS PubMed Google Scholar
• Hori, O. et al. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system. J. Biol. Chem. 270, 25752–25761 (1995).
  Article CAS PubMed Google Scholar
• Bierhaus, A. et al. Understanding RAGE, the receptor for advanced glycation end products. J. Mol. Med. 83, 876–886 (2005).
  Article CAS PubMed Google Scholar
• Boullier, A. et al. The binding of oxidized low density lipoprotein to mouse CD36 is mediated in part by oxidized phospholipids that are associated with both the lipid and protein moieties of the lipoprotein. J. Biol. Chem. 275, 9163–9169 (2000).
  Article CAS PubMed Google Scholar
• Coraci, I. S. et al. CD36, a class B scavenger receptor, is expressed on microglia in Alzheimer's disease brains and can mediate production of reactive oxygen species in response to β-amyloid fibrils. Am. J. Pathol. 160, 101–112 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Jimenez-Dalmaroni, M. J. et al. Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands and acts as a co-receptor for TLR2. PLoS ONE 4, e7411 (2009).
  Article PubMed PubMed Central CAS Google Scholar
• Yang, R. B., Mark, M. R., Gurney, A. L. & Godowski, P. J. Signaling events induced by lipopolysaccharide-activated Toll-like receptor 2. J. Immunol. 163, 639–643 (1999).
  CAS PubMed Google Scholar
• Muta, T. & Takeshige, K. Essential roles of CD14 and lipopolysaccharide-binding protein for activation of Toll-like receptor (TLR)2 as well as TLR4 reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations. Eur. J. Biochem. 268, 4580–4589 (2001).
  Article CAS PubMed Google Scholar