Postulates for validating TLR4 agonists

European Journal of Immunology

Volumn 45, Issue 2, 2015, Pages 356-370

  Manček Keber, Mateja ^a,b   Jerala, Roman ^a,b  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^b EN FIST CENTRE OF EXCELLENCE   (Slovenia)

Author keywords

Ligand recognition; Molecular mechanism; TLR4 agonists

Indexed keywords

LIPOPOLYSACCHARIDE; PATTERN RECOGNITION RECEPTOR; PROTEIN MD 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 4 AGONIST; TOLL LIKE RECEPTOR 4 ANTAGONIST; TOLL LIKE RECEPTOR AFFECTING AGENT; TOLL LIKE RECEPTOR AGONIST; UNCLASSIFIED DRUG; DIVALENT CATION; IMMUNOLOGIC FACTOR; LIPID A; LY96 PROTEIN, HUMAN; NICKEL; PACLITAXEL; PROTEIN BINDING; TLR4 PROTEIN, HUMAN;

ARTICLE; INNATE IMMUNITY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; AGONISTS; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; GENE EXPRESSION REGULATION; GENETICS; HUMAN; IMMUNOLOGY; SIGNAL TRANSDUCTION;

CATIONS, DIVALENT; GENE EXPRESSION REGULATION; HUMANS; IMMUNOLOGIC FACTORS; LIPID A; LYMPHOCYTE ANTIGEN 96; MODELS, MOLECULAR; NICKEL; PACLITAXEL; PROTEIN BINDING; RECEPTOR CROSS-TALK; SIGNAL TRANSDUCTION; TOLL-LIKE RECEPTOR 4;

EID: 84923093439     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201444462     Document Type: Article

References (134)

1. Tobias, P. S., Soldau, K. and Ulevitch, R. J., Identification of a lipid A binding site in the acute phase reactant lipopolysaccharide binding protein. J. Biol. Chem. 1989. 264: 10867-10871.
2. Wright, S. D., Ramos, R. A., Tobias, P. S., Ulevitch, R. J. and Mathison, J. C., CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 1990. 249: 1431-1433.
3. Tobias, P. S., Soldau, K. and Ulevitch, R. J., Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J. Exp. Med. 1986. 164: 777-793.
4. Taguchi, T., Mitcham, J. L., Dower, S. K., Sims, J. E. and Testa, J. R., Chromosomal localization of TIL, a gene encoding a protein related to the Drosophila transmembrane receptor Toll, to human chromosome 4p14. Genomics 1996. 32: 486-488.
5. Medzhitov, R., PrestonHurlburt, P. and Janeway, C. A., A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997. 388: 394-397.
6. Rock, F. L., Hardiman, G., Timans, J. C., Kastelein, R. A. and Bazan, J. F., A family of human receptors structurally related to Drosophila Toll, Proc. Natl. Acad. Sci. USA 1998. 95: 588-593.
7. Chaudhary, P. M., Ferguson, C., Nguyen, V., Nguyen, O., Massa, H. F., Eby, M., Jasmin, A. et al., Cloning and characterization of two Toll/Interleukin-1 receptor-like genes TIL3 and TIL4: evidence for a multi-gene receptor family in humans. Blood 1998. 91: 4020-4027.
8. Poltorak, A., He, X. L., Smirnova, I., Liu, M. Y., Van Huffel, C., Du, X., Birdwell, D. et al., Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 1998. 282: 2085-2088.
9. Qureshi, S. T., Lariviere, L., Leveque, G., Clermont, S., Moore, K. J., Gros, P. and Malo, D., Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4). J. Exp. Med. 1999. 189: 615-625.
10. Zhang, F. X., Kirschning, C. J., Mancinelli, R., Xu, X. P., Jin, Y. P., Faure, E., Mantovani, A. et al., Bacterial lipopolysaccharide activates nuclear factor-kappa B through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes. J. Biol. Chem. 1999. 274: 7611-7614.
11. Hoebe, K., Du, X., Georgel, P., Janssen, E., Tabeta, K., Kim, S. O., Goode, J. et al., Identification of Lps2 as a key transducer of MyD88-independent TIR signalling. Nature 2003. 424: 743-748.
12. Kagan, J. C. and Medzhitov, R., Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 2006. 125: 943-955.
13. Shimazu, R., Akashi, S., Ogata, H., Nagai, Y., Fukudome, K., Miyake, K. and Kimoto, M., MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 1999. 189: 1777-1782.
14. Ohto, U., Fukase, K., Miyake, K. and Shimizu, T., Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2. Proc. Natl. Acad. Sci. USA 2012. 109: 7421-7426.
15. Nishitania, C., Mitsuzawa, H., Hyakushima, N., Sano, H., Matsushima, N. and Kuroki, Y., The Toll-like receptor 4 region Glu(24)-Pro(34) is critical for interaction with MD-2. Biochem. Biophys. Res. Commun. 2005. 328: 586-590.
16. Kim, H. M., Park, B. S., Kim, J. I., Kim, S. E., Lee, J., Oh, S. C., Enkhbayar, P. et al., Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist eritoran. Cell 2007. 130: 906-917.
17. Resman, N., Vasl, J., Oblak, A., Pristovsek, P., Gioannini, T. L., Weiss, J. P. and Jerala, R., Essential roles of hydrophobic residues in both MD-2 and Toll-like receptor 4 in activation by endotoxin. J. Biol. Chem. 2009. 284: 15052-15060.
18. Park, B. S., Song, D. H., Kim, H. M., Choi, B. S., Lee, H. and Lee, J. O., The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 2009. 458: 1191-1195.
19. Jiang, Z. F., Georgel, P., Du, X., Shamel, L., Sovath, S., Mudd, S., Huber, M. et al., CD14 is required for MyD88-independent LPS signaling. Nat. Immunol. 2005. 6: 565-570.
20. Vogel, S., Hirschfeld, M. J. and Perera, P. Y., Signal integration in lipopolysaccharide (LPS)-stimulated murine macrophages. J. Endotoxin. Res. 2001. 7: 237-241.
21. Werts, C., Tapping, R. I., Mathison, J. C., Chuang, T. H., Kravchenko, V., Saint Girons, I., Haake, D. A. et al., Leptospiral lipopolysaccharide activates cells through a TLR2-dependent mechanism. Nat. Immunol. 2001. 2: 346-352.
22. Brandl, K., Gluck, T., Hartmann, P., Salzberger, B. and Falk, W., A designed TLR4/MD-2 complex to capture LPS. J. Endotoxin. Res. 2005. 11: 197-206.
23. Coats, S. R., Reife, R. A., Bainbridge, B. W., Pham, T. T. T. and Darveau, R. P., Porphyromonas gingivalis lipopolysaccharide antagonizes Escherichia coli lipopolysaccharide at toll-like receptor 4 in human endothelial cells. Infect. Immun. 2003. 71: 6799-6807.
24. Hajjar, A. M., Ernst, R. K., Tsai, J. H., Wilson, C. B. and Miller, S. I., Human Toll-like receptor 4 recognizes host-specific LPS modifications. Nat. Immunol. 2002. 3: 354-359.
25. Hajjar, A. M., Ernst, R. K., Fortuno, E. S., Brasfield, A. S., Yam, C. S., Newlon, L. A., Kollmann, T. R. et al., Humanized TLR4/MD-2 mice reveal LPS recognition differentially impacts susceptibility to Yersinia pestis and Salmonella enterica. PLoS Pathog. 2012. 8: e1002963.
26. Marr, N., Novikov, A., Hajjar, A. M., Caroff, M. and Fernandez, R. C., Variability in the lipooligosaccharide structure and endotoxicity among Bordetella pertussis strains. J. Infect. Dis. 2010. 202: 1897-1906.
27. Conde-Alvarez, R., Arce-Gorvel, V., Iriarte, M., Mancek-Keber, M., Barquero-Calvo, E., Palacios-Chaves, L., Chacon-Diaz, C. et al., The lipopolysaccharide core of Brucella abortus acts as a shield against innate immunity recognition. PLoS Pathog. 2012. 8: e1002675.
28. Takeda, K. and Akira, S., Toll-like receptors. Curr. Protoc. Immunol. 2007. Chapter 14: Unit 14.12.
29. Gay, N. J. and Gangloff, M., Structure and function of toll receptors and their ligands. Annu Rev Biochem. 2007. 76: 141-165.
30. Oldenburg, M., Kruger, A., Ferstl, R., Kaufmann, A., Nees, G., Sigmund, A., Bathke, B. et al., TLR13 recognizes bacterial 23S rRNA devoid of erythromycin resistance-forming modification. Science 2012. 337: 1111-1115.
31. Mathur, R., Oh, H., Zhang, D., Park, S. G., Seo, J., Koblansky, A., Hayden, M. S. et al., A mouse model of Salmonella typhi infection. Cell 2012. 151: 590-602.
32. Rietschel, E. T., Brade, H., Brade, L., Brandenburg, K., Schade, U., Seydel, U., Zahringer, U. et al., Lipid A, the endotoxic center of bacterial lipopolysaccharides: relation of chemical structure to biological activity. Prog. Clin. Biol. Res. 1987. 231: 25-53.
33. Mancek-Keber, M. and Jerala, R., Structural similarity between the hydrophobic fluorescent probe and lipid A as a ligand of MD-2. FASEB J. 2006. 20: 1836-1842.
34. Hailman, E., Lichenstein, H. S., Wurfel, M. M., Miller, D. S., Johnson, D. A., Kelley, M., Busse, L. A. et al., Lipopolysaccharide (Lps)-binding protein accelerates the binding of Lps to Cd14. J. Exp. Med. 1994. 179: 269-277.
35. Tobias, P. S., Soldau, K., Gegner, J. A., Mintz, D. and Ulevitch, R. J., Lipopolysaccharide-binding protein-mediated complexation of lipopolysaccharide with soluble Cd14. Biol. Chem. 1995. 270: 10482-10488.
36. Akashi, S., Ogata, H., Kirikae, F., Kirikae, T., Kawasaki, K., Nishijima, M., Shimazu, R.et al., Regulatory roles for CD14 and phosphatidylinositol in the signaling via toll-like receptor 4-MD-2. Biochem. Biophys. Res. Commun. 2000. 268: 172-177.
37. Gioannini, T. L., Teghanemt, A., Zhang, D., Coussens, N. P., Dockstader, W., Ramaswamy, S. and Weiss, J. P., Isolation of an endotoxin-MD-2 complex that produces Toll-like receptor 4-dependent cell activation at picomolar concentrations. Proc. Natl. Acad. Sci. USA 2004. 101: 4186-4191.
38. Nilsson, R., Bajic, V. B., Suzuki, H., di Bernardo, D., Bjorkegren, J., Katayama, S., Reid, J. F. et al., Transcriptional network dynamics in macrophage activation. Genomics 2006. 88: 133-142.
39. Lu, Y. C., Yeh, W. C. and Ohashi, P. S., LPS/TLR4 signal transduction pathway. Cytokine 2008. 42: 145-151.
40. Tobias, P. and Curtiss, L. K., Paying the price for pathogen protection: toll receptors in atherogenesis. J. Lipid Res. 2005. 46: 404-411.
41. Andreakos, E., Sacre, S., Foxwell, B. M. and Feldmann, M., The toll-like receptor-nuclear factor kappaB pathway in rheumatoid arthritis. Front. Biosci. 2005. 10: 2478-2488.
42. Schmidt, M., Raghavan, B., Muller, V., Vogl, T., Fejer, G., Tchaptchet, S., Keck, S. et al., Crucial role for human Toll-like receptor 4 in the development of contact allergy to nickel. Nat. Immunol. 2010. 11: 814-819.
43. Wu, F. X., Bian, J. J., Miao, X. R., Huang, S. D., Xu, X. W., Gong, D. J., Sun, Y. M. et al., Intrathecal siRNA against Toll-like receptor 4 reduces nociception in a rat model of neuropathic pain. Int. J. Med. Sci. 2010. 7: 251-259.
44. Tsung, A., Hoffman, R. A., Izuishi, K., Critchlow, N. D., Nakao, A., Chan, M. H., Lotze, M. T. et al., Hepatic ischemia/reperfusion injury involves functional TLR4 signaling in nonparenchymal cells. J. Immunol. 2005. 175: 7661-7668.
45. Powers, K. A., Szaszi, K., Khadaroo, R. G., Tawadros, P. S., Marshall, J. C., Kapus, A. and Rotstein, O. D., Oxidative stress generated by hemorrhagic shock recruits Toll-like receptor 4 to the plasma membrane in macrophages. J. Exp. Med. 2006. 203: 1951-1961.
46. Alfonso-Loeches, S., Pascual-Lucas, M., Blanco, A. M., Sanchez-Vera, I. and Guerri, C., Pivotal role of TLR4 receptors in alcohol-induced neuroinflammation and brain damage. J. Neurosci. 2010. 30: 8285-8295.
47. Kolek, M. J., Carlquist, J. F., Muhlestein, J. B., Whiting, B. M., Horne, B. D., Bair, T. L. and Anderson, J. L., Toll-like receptor 4 gene Asp299Gly polymorphism is associated with reductions in vascular inflammation, angiographic coronary artery disease, and clinical diabetes. Am. Heart J. 2004. 148: 1034-1040.
48. Apetoh, L., Ghiringhelli, F., Tesniere, A., Obeid, M., Ortiz, C., Criollo, A., Mignot, G. et al., Toll-like receptor 4-dependent contribution of the immune system to anticancer chemotherapy and radiotherapy. Nat. Med. 2007. 13: 1050-1059.
49. Matzinger, P., Tolerance, danger, and the extended family. Annu. Rev. Immunol. 1994. 12: 991-1045.
50. Erridge, C., Attina, T., Spickett, C. M. and Webb, D. J., A high-fat meal induces low-grade endotoxemia: evidence of a novel mechanism of postprandial inflammation. Am. J. Clin. Nutr. 2007. 86: 1286-1292.
51. Dasu, M. R. and Jialal, I., Free fatty acids in the presence of high glucose amplify monocyte inflammation via Toll-like receptors. Am. J. Physiol. Endocrinol. Metab. 2010. 300: E145-E154.
52. Suganami, T., Tanimoto-Koyama, K., Nishida, J., Itoh, M., Yuan, X. M., Mizuarai, S., Kotani, H. et al., Role of the Toll-like receptor 4/NF-kappa B pathway in saturated fatty acid-induced inflammatory changes in the interaction between adipocytes and macrophages. Arterioscler. Thromb. Vasc. Biol. 2007. 27: 84-91.
53. Brunn, G. J., Wijdicks, M. F. and Platt, J. L., Toward a modern concept of sepsis: new answers to ancient questions. Discov. Med. 2006. 6: 11-17.
54. Pal, D., Dasgupta, S., Kundu, R., Maitra, S., Das, G., Mukhopadhyay, S., Ray, S. et al., Fetuin-A acts as an endogenous ligand of TLR4 to promote lipid-induced insulin resistance. Nat. Med. 2012. 18: 1279-1285.
55. Millien, V. O., Lu, W., Shaw, J., Yuan, X. Y., Mak, G., Roberts, L., Song, L. Z. et al., Cleavage of fibrinogen by proteinases elicits allergic responses through Toll-like receptor 4. Science 2013. 341: 792-796.
56. Shichita, T., Hasegawa, E., Kimura, A., Morita, R., Sakaguchi, R., Takada, I., Sekiya, T. et al., Peroxiredoxin family proteins are key initiators of post-ischemic inflammation in the brain. Nat. Med. 2012. 18: 911-917.
57. Midwood, K., Sacre, S., Piccinini, A. M., Inglis, J., Trebaul, A., Chan, E., Drexler, S. et al., Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease. Nat. Med. 2009. 15: U774-U711.
58. Tang, S. C., Lathia, J. D., Selvaraj, P. K., Jo, D. G., Mughal, M. R., Cheng, A., Siler, D. A. et al., Toll-like receptor-4 mediates neuronal apoptosis induced by amyloid beta-peptide and the membrane lipid peroxidation product 4-hydroxynonenal. Exp. Neurol. 2008. 213: 114-121.
59. Lotz, M., Ebert, S., Esselmann, H., Iliev, A. I., Prinz, M., Wiazewicz, N., Wiltfang, J. et al., Amyloid beta peptide 1-40 enhances the action of Toll-like receptor-2 and -4 agonists but antagonizes Toll-like receptor-9-induced inflammation in primary mouse microglial cell cultures. J. Neurochem. 2005. 94: 289-298.
60. Stewart, C. R., Stuart, L. M., Wilkinson, K., van Gils, J. M., Deng, J. S., Halle, A., Rayner, K. J. et al., CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer. Nat. Immunol. 2010. 11: U155-U175.
61. Deguchi, A., Tomita, T., Omori, T., Komatsu, A., Ohto, U., Takahashi, S., Tanimura, N. et al., Serum amyloid A3 binds MD-2 to activate p38 and NF-kappa B pathways in a MyD88-dependent manner. J. Immunol. 2013. 191: 1856-1864.
62. Qiang, X., Yang, W. L., Wu, R., Zhou, M., Jacob, A., Dong, W., Kuncewitch, M. et al., Cold-inducible RNA-binding protein (CIRP) triggers inflammatory responses in hemorrhagic shock and sepsis. Nat. Med. 2013. 19: 1489-1495.
63. Okamura, Y., Watari, M., Jerud, E. S., Young, D. W., Ishizaka, S. T., Rose, J., Chow, J. C. et al., The extra domain A of fibronectin activates toll-like receptor 4. J. Biol. Chem. 2001. 276: 10229-10233.
64. Lasarte, J. J., Casares, N., Gorraiz, M., Hervas-Stubbs, S., Arribillaga, L., Mansilla, C., Durantez, M. et al., The extra domain A from fibronectin targets antigens to TLR4-expressing cells and induces cytotoxic T cell responses in vivo. J. Immunol. 2007. 178: 748-756.
65. Jou, I., Lee, J. H., Park, S. Y., Yoon, H. J., Joe, E. H. and Park, E. J., Gangliosides trigger inflammatory responses via TLR4 in brain glia. Am. J. Pathol. 2006. 168: 1619-1630.
66. Sohn, D. H., Sokolove, J., Sharpe, O., Erhart, J. C., Chandra, P. E., Lahey, L. J., Lindstrom, T. M. et al., Plasma proteins present in osteoarthritic synovial fluid can stimulate cytokine production via Toll-like receptor 4. Arthritis Res. Ther. 2012. 14: R7.
67. Tewary, P., Yang, D., de la Rosa, G., Li, Y. N., Finn, M. W., Krensky, A. M., Clayberger, C. et al., Granulysin activates antigen-presenting cells through TLR4 and acts as an immune alarmin. Blood 2010. 116: 3465-3474.
68. Figueiredo, R. T., Fernandez, P. L., Mourao-Sa, D. S., Porto, B. N., Dutra, F. F., Alves, L. S., Oliveira, M. F. et al., Characterization of heme as activator of toll-like receptor 4. Biol. Chem. 2007. 282: 20221-20229.
69. Park, J. S., Gamboni-Robertson, F., He, Q. B., Svetkauskaite, D., Kim, J. Y., Strassheim, D., Sohn, J. W. et al., High mobility group box 1 protein interacts with multiple Toll-like receptors. Am. J. Physiol. Cell Physiol. 2006. 290: C917-C924.
70. Yu, M., Wang, H. C., Ding, A. H., Golenbock, D. T., Latz, E., Czura, C. J., Fenton, M. J. et al., HMGB1 signals through toll-like receptor (TLR) 4 and TLR2. Shock 2006. 26: 174-179.
71. Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Bare, O., Auron, P. E., Stevenson, M. A. et al., Novel signal transduction pathway utilized by extracellular HSP70-role of Toll-like receptor (TLR) 2 and TLR4. J. Biol. Chem. 2002. 277: 15028-15034.
72. Termeer, C., Benedix, F., Sleeman, J., Fieber, C., Voith, U., Ahrens, T., Miyake, K. et al., Oligosaccharides of hyaluronan activate dendritic cells via toll-like receptor 4. Exp. Med. 2002. 195: 99-111.
73. Taylor, K. R., Yamasaki, K., Radek, K. A., Di Nardo, A., Goodarzi, H., Golenbock, D., Beutler, B. et al., Recognition of hyaluronan released in sterile injury involves a unique receptor complex dependent on toll-like receptor 4, CD44, and MD-2. Biol. Chem. 2007. 282: 18265-18275.
74. Vogl, T., Tenbrock, K., Ludwig, S., Leukert, N., Ehrhardt, C., van Zoelen, M. A. D., Nacken, W. et al., Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock. Nat. Med. 2007. 13: 1042-1049.
75. Lorne, E., Zmijewski, J. W., Zhao, X., Liu, G., Tsuruta, Y., Park, Y. J., Dupont, H. et al., Role of extracellular superoxide in neutrophil activation: interactions between xanthine oxidase and TLR4 induce proinflammatory cytokine production. Am. J. Physiol. Cell Physiol. 2008. 294: C985-C993.
76. Lee, J. Y., Ye, J. P., Gao, Z. G., Youn, H. S., Lee, W. H., Zhao, L., Sizemore, N. et al., Reciprocal modulation of toll-like receptor-4 signaling pathways involving MyD88 and phosphatidylinositol 3-kinase/AKT by saturated and polyunsaturated fatty acids. J. Biol. Chem. 2003. 278: 37041-37051.
77. Miller, Y. I., Viriyakosol, S., Binder, C. J., Feramisco, J. R., Kirkland, T. N. and Witztum, J. L., Minimally modified LDL binds to CD14, induces macrophage spreading via TLR4/MD-2, and inhibits phagocytosis of apoptotic cells. J. Biol. Chem. 2003. 278: 1561-1568.
78. Geng, H. L., Wang, A. H., Rong, G. H., Zhu, B., Deng, Y., Chen, J. and Zhong, R. Q., The effects of ox-LDL in human atherosclerosis may be mediated in part via the toll-like receptor 4 pathway. Mol. Cell. Biochem. 2010. 342: 201-206.
79. Walton, K. A., Hsieh, X., Gharavi, N., Wang, S., Wang, G., Yeh, M., Cole, A. L. et al., Receptors involved in the oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero3-phosphorylcholine-mediated synthesis of interleukin-8-a role for toll-like receptor 4 and a glycosylphosphatidylinositol-anchored protein. J. Biol. Chem. 2003. 278: 29661-29666.
80. Jeon, Y. J., Han, S. B., Ahn, K. S. and Kim, H. M., Differential activation of murine macrophages by angelan and LPS. Immunopharmacology 2000. 49: 275-284.
81. Kim, J. Y., Yoon, Y. D., Ahn, J. M., Kang, J. S., Park, S. K., Lee, K., Bin Song, K. et al., Angelan isolated from Angelica gigas Nakai induces dendritic cell maturation through toll-like receptor 4. Int. Immunopharmacol. 2007. 7: 78-87.
82. Trompette, A., Divanovic, S., Visintin, A., Blanchard, C., Hegde, R. S., Madan, R., Thorne, P. S. et al., Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein. Nature 2009. 457: 585-588.
83. Mossman, K. L., Mian, A. F., Lauzon, N. M., Gyles, C. L., Lichty, B., Mackenzie, R., Gill, N. et al., Cutting edge: FimH adhesin of type 1 fimbriae is a novel TLR4 ligand. J. Immunol. 2008. 181: 6702-6706.
84. Debierre-Grockiego, F., Campos, M. A., Azzouz, N., Schmidt, J., Bieker, U., Resende, A. G., Santos Mansur, D. et al., Activation of TLR2 and TLR4 by glycosylphosphatidylinositols derived from Toxoplasma gondii. J. Immunol. 2007. 179: 1129-1137.
85. Basu, S., Pathak, S. K., Chatterjee, G., Pathak, S., Basu, J. and Kundu, M., Helicobacter pylori protein HP0175 transactivates epidermal growth factor receptor through TLR4 in gastric epithelial cells. J. Biol. Chem. 2008. 283: 32369-32376.
86. Bulut, Y., Faure, E., Thomas, L., Karahashi, H., Michelsen, K. S., Equils, O., Morrison, S. G. et al., Chlamydial heat shock protein 60 activates macrophages and endothelial cells through toll-like receptor 4 and MD2 in a MyD88-dependent pathway. J. Immunol. 2002. 168: 1435-1440.
87. Bergner, P. M., Mundinano, J., Piazzon, I. and Goldbaum, F. A., A polymeric bacterial protein activates dendritic cells via TLR4. J. Immunol. 2006. 176: 2366-2372.
88. Tada, H., Nemoto, E., Shimauchi, H., Watanabe, T., Mikami, T., Matsumoto, T., Ohno, N. et al., Saccharomyces cerevisiae- and Candida albicans-derived mannan induced production of tumor necrosis factor alpha by human monocytes in a CD14-and Toll-like receptor 4-dependent manner. Microbiol. Immunol. 2002. 46: 503-512.
89. Nagai, Y., Akashi, S., Nagafuku, M., Ogata, M., Iwakura, Y., Akira, S., Kitamura, T. et al., Essential role of MD-2 in LPS responsiveness and TLR4 distribution. Nat. Immunol. 2002. 3: 667-672.
90. Pantel, A., Cheong, C., Dandamudi, D., Shrestha, E., Mehandru, S., Brane, L., Ruane, D. et al., A new synthetic TLR4 agonist, GLA, allows dendritic cells targeted with antigen to elicit Th1 T-cell immunity in vivo. Eur. J. Immunol. 2012. 42: 101-109.
91. Orr, M. T., Duthie, M. S., Windish, H. P., Lucas, E. A., Guderian, J. A., Hudson, T. E., Shaverdian, N. et al., MyD88 and TRIF synergistic interaction is required for TH1-cell polarization with a synthetic TLR4 agonist adjuvant. Eur. J. Immunol. 2013. 43: 2398-2408.
92. Rachmawati, D., Bontkes, H. J., Verstege, M. I., Muris, J., von Blomberg, B. M. E., Scheper, R. J. and van Hoogstraten, I. M. W., Transition metal sensing by Toll-like receptor-4: next to nickel, cobalt and palladium are potent human dendritic cell stimulators. Contact Dermatitis 2012. 68: 331-338.
93. Okamoto, M., Oshikawa, T., Tano, T., Ahmed, S. U., Kan, S., Sasai, A., Akashi, S. et al., Mechanism of anticancer host response induced by OK-432, a streptococcal preparation, mediated by phagocytosis and Toll-like receptor 4 signaling. J. Immunother. 2006. 29: 78-86.
94. Kawasaki, K., Gomi, K. and Nishijima, M., Cutting edge: Gln22 of mouse MD-2 is essential for species-specific lipopolysaccharide mimetic action of taxol. J. Immunol. 2001. 166: 11-14.
95. Kawasaki, K., Nogawa, H. and Nishijima, M., Identification of mouse MD-2 residues important for forming the cell surface TLR4-MD-2 complex recognized by anti-TLR4-MD-2 antibodies, and for conferring LPS and taxol responsiveness on mouse TLR4 by alanine-scanning mutagenesis. J. Immunol. 2003. 170: 413-420.
96. Spiller, S., Dreher, S., Meng, G., Grabiec, A., Thomas, W., Hartung, T., Pfeffer, K. et al., Cellular recognition of trimyristoylated peptide or enterobacterial lipopolysaccharide via both TLR2 and TLR4. J. Biol. Chem. 2007. 282: 13190-13198.
97. Yuan, A., Pardy, R. L. and Chia, C. P., Nonspecific interactions alter lipopolysaccharide patterns and protein mobility on sodium dodecyl sulfate polyacrylamide gels. Electrophoresis 1999. 20: 1946-1949.
98. Vasl, J., Oblak, A., Gioannini, T. L., Weiss, J. P. and Jerala, R., Novel roles of lysines 122, 125, and 58 in functional differences between human and murine MD-2. J. Immunol. 2009. 183: 5138-5145.
99. Hasday, J. D., Bascom, R., Costa, J. J., Fitzgerald, T. and Dubin, W., Bacterial endotoxin is an active component of cigarette smoke. Chest 1999. 115: 829-835.
100. Gao, B. and Tsan, M. F., Recombinant human heat shock protein 60 does not induce the release of tumor necrosis factor alpha from murine macrophages. J. Biol. Chem. 2003. 278: 22523-22529.
101. Bausinger, H., Lipsker, D., Ziylan, U., Manie, S., Briand, J. P., Cazenave, J. P., Muller, S. et al., Endotoxin-free heat-shock protein 70 fails to induce APC activation. Eur. J. Immunol. 2002. 32: 3708-3713.
102. Erridge, C., Endogenous ligands of TLR2 and TLR4: agonists or assistants? J. Leukoc. Biol. 2010. 87: 989-999.
103. Zhang, G. H., Mann, D. M. and Tsai, C. M., Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide. Infect. Immun. 1999. 67: 1353-1358.
104. Pristovsek, P. and Kidric, J., Solution structure of polymyxins B and E and effect of binding to lipopolysaccharide: an MMR and molecular modeling study. J. Med. Chem. 1999. 42: 4604-4613.
105. Gao, B. and Tsan, M. F., Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor alpha release by murine macrophages. J. Biol. Chem. 2003. 278: 174-179.
106. Triantafilou, M. and Triantafilou, K., Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide. Biochem. Soc. Trans. 2004. 32: 636-639.
107. Byrd, C. A., Bornmann, W., Erdjument-Bromage, H., Tempst, P., Pavletich, N., Rosen, N., Nathan, C. F. et al., Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide. Proc. Natl. Acad. Sci. USA 1999. 96: 5645-5650.
108. Herre, J., Gronlund, H., Brooks, H., Hopkins, L., Waggoner, L., Murton, B., Gangloff, M. et al., Allergens as immunomodulatory proteins: the cat dander protein Fel d 1 enhances TLR activation by lipid ligands. J. Immunol. 2013. 191: 1529-1535.
109. Taylor, K. E., Giddings, J. C. and van den Berg, C. W., C-reactive protein-induced in vitro endothelial cell activation is an artefact caused by azide and lipopolysaccharide. Arterioscler. Thromb. Vasc. Biol. 2005. 25: 1225-1230.
110. Walsh, C., Gangloff, M., Monie, T., Smyth, T., Wei, B., McKinley, T. J., Maskell, D. et al., Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa. J. Immunol. 2008. 181: 1245-1254.
111. Re, F. and Strominger, J. L., Separate functional domains of human MD-2 mediate toll-like receptor 4-binding and lipopolysaccharide responsiveness. J. Immunol. 2003. 171: 5272-5276.
112. Rallabhandi, P., Bell, J., Boukhvalova, M. S., Medvedev, A., Lorenz, E., Arditi, M., Hemming, V. G. et al., Analysis of TLR4 polymorphic variants: New insights into TLR4/MD-2/CD14 stoichiometry, structure, and signaling. J. Immunol. 2006. 177: 322-332.
113. Muroi, M. and Tanamoto, K., Structural regions of MD-2 that determine the agonist-antagonist activity of lipid IVa. Biol. Chem. 2006. 281: 5484-5491.
114. Resman, N., Gradisar, H., Vasl, J., Keber, M. M., Pristovsek, P. and Jerala, R., Taxanes inhibit human TLR4 signaling by binding to MD-2. FEBS Lett. 2008. 582: 3929-3934.
115. Kharroubi, I., Ladriere, L., Cardozo, A. K., Dogusan, Z., Cnop, M. and Eizirik, D. L., Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappaB and endoplasmic reticulum stress. Endocrinology 2004. 145: 5087-5096.
116. Wen, H. T., Gris, D., Lei, Y., Jha, S., Zhang, L., Huang, M. T. H., Brickey, W. J. et al., Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling. Nat. Immunol. 2011. 12: 408-U461.
117. Erridge, C. and Samani, N. J., Saturated fatty acids do not directly stimulate Toll-like receptor signaling. Arterioscler. Thromb. Vasc. Biol. 2009. 29: 1944-1949.
118. Erridge, C., Webb, D. J. and Spickett, C. M., Toll-like receptor 4 signalling is neither sufficient nor required for oxidised phospholipid mediated induction of interleukin-8 expression. Atherosclerosis 2007. 193: 77-85.
119. Zimmer, S. M., Liu, J., Clayton, J. L., Stephens, D. S. and Snyder, J. P., Paclitaxel binding to human and murine MD-2. J. Biol. Chem. 2008. 283: 27916-27926.
120. Mancek-Keber, M., Gradisar, H., Inigo Pestana, M., Martinez de Tejada, G. and Jerala, R., Free thiol group of MD-2 as the target for inhibition of the lipopolysaccharide-induced cell activation. J. Biol. Chem. 2009. 284: 19493-19500.
121. Gradisar, H., Keber, M. M., Pristovsek, P. and Jerala, R., MD-2 as the target of curcumin in the inhibition of response to LPS. J. Leukoc. Biol. 2007. 82: 968-974.
122. Shirey, K. A., Lai, W., Scott, A. J., Lipsky, M., Mistry, P., Pletneva, L. M., Karp, C. L. et al., The TLR4 antagonist Eritoran protects mice from lethal influenza infection. Nature 2013. 497: 498-502.
123. Tan, Y. and Kagan, J. C., A cross-disciplinary perspective on the innate immune responses to bacterial lipopolysaccharide. Mol. Cell 2014. 54: 212-223.
124. Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K. and Miao, E. A., Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science 2013. 341: 1250-1253.
125. Kayagaki, N., Wong, M. T., Stowe, I. B., Ramani, S. R., Gonzalez, L. C., Akashi-Takamura, S., Miyake, K. et al., Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 2013. 341: 1246-1249.
126. Petrilli, V., Papin, S., Dostert, C., Mayor, A., Martinon, F. and Tschopp, J., Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ. 2007. 14: 1583-1589.
127. Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S. J., Dolinay, T., Lam, H. C., Englert, J. A. et al., Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat. Immunol. 2011. 12: 222-U257.
128. Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P. et al., Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 2006. 440: 228-232.
129. Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A. et al., Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 2008. 9: 847-856.
130. Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A. et al., The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat. Immunol. 2008. 9: 857-865.
131. Hafner-Bratkovic, I., Bencina, M., Fitzgerald, K. A., Golenbock, D. and Jerala, R., NLRP3 inflammasome activation in macrophage cell lines by prion protein fibrils as the source of IL-1 beta and neuronal toxicity. Cell. Mol. Life Sci. 2012. 69: 4215-4228.
132. Lee, G. S., Subramanian, N., Kim, A. I., Aksentijevich, I., Goldbach-Mansky, R., Sacks, D. B., Germain, R. N. et al., The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP. Nature 2012. 492: 123-127.
133. Munoz-Planillo, R., Kuffa, P., Martinez-Colon, G., Smith, B. L., Rajendiran, T. M. and Nunez, G., K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 2013. 38: 1142-1153.
134. Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C. and Ferrin, T. E., UCSF chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 2004. 25: 1605-1612.