A Toll-like receptor in horseshoe crabs

Immunological Reviews

Volumn 198, Issue , 2004, Pages 106-115

  Inamori, Kei Ichiro ^a,b   Ariki, Shigeru ^a   Kawabata, Shun Ichiro ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; CELL SURFACE RECEPTOR; COMPLEMENTARY DNA; LEUCINE; LIPOPOLYSACCHARIDE RECEPTOR; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; BLOOD CELL; CHEMICAL STRUCTURE; DROSOPHILA; GENE EXPRESSION; GRANULAR BLOOD CELL; IMMUNE SYSTEM; INFECTION; INNATE IMMUNITY; LEUCINE RICH REPEAT; LIMULUS; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGEN ASSOCIATED MOLECULAR PATTERN; PATHOGEN ASSOCIATED MOLECULAR PATTERN BINDING INSERTION; PATTERN RECOGNITION; PRIORITY JOURNAL; REVIEW; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; TACHYPLEUS TRIDENTATUS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DROSOPHILA; DROSOPHILA PROTEINS; HEMOCYTES; HORSESHOE CRABS; IMMUNITY, NATURAL; MAMMALS; MEMBRANE GLYCOPROTEINS; MOLECULAR SEQUENCE DATA; PHYLOGENY; RECEPTORS, CELL SURFACE; RECEPTORS, INTERLEUKIN-1; SIGNAL TRANSDUCTION; TOLL-LIKE RECEPTOR 5; TOLL-LIKE RECEPTORS;

EID: 1642545506     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0105-2896.2004.0131.x     Document Type: Review

References (80)

1. Janeway Jr CA. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 1989;54:1-13.
2. Sōderhāll K, Cerenius L. Role of the prophenoloxidase- activating system in invertebrate immunity. Curr Opin Immunol 1998;10:23-28.
3. Ashida M, Brey PT. Recent advance in research on the insect prophenoloxidase cascade. In: Brey PT, Hultmark D, eds. Molecular Mechanisms of Immune Responses in Insects. London: Chapman & Hall, 1998:135-172.
4. Hoffmann JA, Kafatos FC, Janeway CA, Ezekowitz RAB. Phylogenetic perspectives in innate immunity. Science 1999;284:1313-1318.
5. Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996;86:973-983.
6. Medzhitov R, Preston-Hurlburt P, Janeway Jr CA. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997;388:394-397.
7. Anderson KV, Nüsslein-Volhard C. Information for the dorsal-ventral pattern of the Drosophila embryo is stored as maternal mRNA. Nature 1984;311:223-227.
8. LeMosy EK, Hong CC, Hashimoto C. Signal transduction by a protease cascade. Trends Cell Biol 1999;9:102-107.
9. Ligoxygakis P, Pelte N, Hoffmann JA, Reichhart JM. Activation of Drosophila Toll during fungal infection by a blood serine protease. Science 2002;297:114-116.
10. Hoffmann JA, Reichhart JM. Drosophila innate immunity: an evolutionary perspective. Nat Immunol 2002;3:121-126.
11. Levashina EA, et al. Constitutive activation of Toll-mediated antifungal defense in serpin-deficient Drosophila Science 1999;285:1917-1919.
12. Leulier F, et al. The Drosophila immune system detects bacteria through specific peptidoglycan recognition. Nat Immunol 2003;4:478-484.
13. Takehana A, et al. Overexpression of a pattern-recognition receptor, peptidoglycan-recognition protein-LE, activates imd/relish-mediated antibacterial defense and the prophenoloxidase cascade in Drosophila larvae. Proc Natl Acad Sci USA 2002;99:13705-13710.
14. Akira S, Takeda K, Kaisho T. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat Immunol 2001;2:675-680.
15. Medzhitov R, Janeway CA. Decoding the patterns of self and nonself by the innate immune system. Science 2002;296:298-300.
16. Rowley AF, Ratcliffe NA. Insects. In: Ratcliffe NA, Rowley AF, eds. Invertebrate Blood Cells 2. London: Academic Press, 1981:421-488.
17. Iwanaga S, Kawabata S, Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem 1998;123:1-15.
18. Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr Opin Immunol 2002;14:87-95.
19. Kawabata S, Tsuda R. Molecular basis of non-self recognition by the horseshoe crab tachylectins. Biochim Biophys Acta 2002;1572:414-421.
20. Armstrong PB. Adhesion and motility of the blood cells of Limulus. In: Cohen WD, ed. Blood Cells of Marine Invertebrates: Experimental Systems in Cell Biology and Comparative Physiology. New York: Alan R. Liss, 1985:77-124.
21. Nakamura T, Morita T, Iwanaga S. Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes. Isolation and characterization. Eur J Biochem 1986;154:511-521.
22. Morita T, Tanaka S, Nakamura T, Iwanaga S. A new 1,3-β-D-glucan- mediated coagulation pathway found in Limulus amebocytes. FEBS Lett 1981;129:318-321.
23. Muta T, et al. Purified horseshoe crab factor G. Reconstitution and characterization of the 1,3-β-D-glucan-sensitive serine protease cascade. J Biol Chem 1995;270:892-897.
24. Furie B, Furie BC. The molecular basis of blood coagulation. Cell 1988;53:505-518.
25. Gokudan S, et al. Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen. Proc Natl Acad Sci USA 1999;96:10086-10091.
26. Kairies N, et al. The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems. Proc Natl Acad Sci USA 2001;98:13519-13524.
27. Kawasaki H, Nose T, Muta T, Iwanaga S, Shimohigashi Y, Kawabata S. Head-to-tail polymerization of coagulin, a clottable protein of the horseshoe crab. J Biol Chem 2000;275:35297-35301.
28. Tokunaga F, et al. Limulus hemocyte transglutaminase. Its purification and characterization, and identification of the intracellular substrates. J Biol Chem 1993;268:252-261.
29. Osaki T, Okino N, Tokunaga F, Iwanaga S, Kawabata S. Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin. J Biol Chem 2002;277:40084- 40090.
30. Saito T, Kawabata S, Hirata M, Iwanaga S. A novel type of Limulus lectin-L6. Purification, primary structure, and antibacterial activity. J Biol Chem 1995;270:14493-14499.
31. Okino N, Kawabata S, Saito T, Hirata M, Takagi T, Iwanaga S. Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes. J Biol Chem 1995;270:31008-31015.
32. Inamori K, et al. A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides. J Biol Chem 1999;274:3272-3278.
33. Saito T, Hatada M, Iwanaga S, Kawabata S. A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J Biol Chem 1997;272:30703-30708.
34. Iwaki D, Osaki T, Mizunoe Y, Wai SN, Iwanaga S, Kawabata S. Functional and structural diversities of C-reactive proteins present in horseshoe crab hemolymph plasma. Eur J Biochem 1999;264:314-332.
35. Tanaka S, Nakamura T, Morita T, Iwanaga S. Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system. Biochem Biophys Res Commun 1982;105:717-723.
36. Ohashi K, Niwa M, Nakamura T, Morita T, Iwanaga S. Anti-LPS factor in the horseshoe crab, Tachypleus tridentatus. Its hemolytic activity on the red blood cell sensitized with lipopolysaccharide. FEBS Lett 1984;176:207-210.
37. Morita T, et al. Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). J Biochem 1985;97:1611-1620.
38. Nakamura T, et al. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J Biol Chem 1988;263:16709-16713.
39. Muta T, Fujimoto T, Nakajima H, Iwanaga S. Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor. J Biochem 1990;108:261-266.
40. Shigenaga T, Muta T, Toh Y, Tokunaga F, Iwanaga S. Antimicrobial tachyplesin peptide precursor. cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus). J Biol Chem 1990;265:21350-21354.
41. Muta T, et al. Primary structures and functions of anti- lipopolysaccharide factor and tachyplesin peptide found in horseshoe crab hemocytes. Adv Exp Med Biol 1990;256:273-285.
42. Katsu T, Nakao S, Iwanaga S. Mode of action of an antimicrobial peptide, tachyplesin I, on biomembranes. Biol Pharm Bull 1993;16:178-181.
43. Hoess A, Watson S, Siber GR, Liddington R. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution. EMBO J 1993;12:3351-3356.
44. Kawano K, et al. Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus): NMR determination of the β-sheet structure. J Biol Chem 1990;265:15365-15367.
45. Park NG, et al. Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices. Biochemistry 1992;31:12241-12247.
46. Saito T, et al. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity. J Biochem 1995;117:1131-1137.
47. Kawabata S, et al. Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity. J Biochem 1996;120:1253-1260.
48. Osaki T, et al. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins. J Biol Chem 1999;274:26172-26178.
49. Kawabata S, et al. Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity. FEBS Lett 1996;398:146-150.
50. Belvin MP, Anderson KV. A conserved signaling pathway - the Drosphila Toll-dorsal pathway. Annu Rev Cell Dev Biol 1996;12:393-416.
51. DeLotto Y, DeLotto R. Proteolytic processing of the Drosophila Spätzle protein by Easter generates a dimeric NGF-like molecule with ventralising activity. Mech Dev 1998;72:141-148.
52. Bergner A, Muta T, Iwanaga S, Beisel H-G, Delotto R, Bode W. Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain. Biol Chem 1997;378:283-287.
53. Bergner A, et al. Crystal structure of Limulus coagulogen: the clotting protein from horseshoe crab, a structural homologue of nerve growth factor. EMBO J 1996;15:6789-6797.
54. Smith CL, DeLotto R. A common domain within the proenzyme regions of the Drosophila snake and easter proteins and Tachypleus proclotting enzyme defines a new subfamily of serine proteases. Protein Sci 1992;1:1225-1226.
55. Smith CL, DeLotto R. Ventralizing signal determined by protease activation in Drosophila embryogenesis. Nature 1994;368:548-551.
56. Nagai T, Kawabata S. A link between blood coagulation and prophenol oxidase activation in arthropod host defense. J Biol Chem 2000;275:29264-29267.
57. Nagai T, Osaki T, Kawabata S. Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J Biol Chem 2001;276:27166-27170.
58. Ratcliffe NA, Rowley AF, Fitzgerald SW, Rhodes CP. Invertebrate immunity: basic concepts and recent advances. Int Rev Cytol 1985;97:183-350.
59. Sugumaran M. Roles of the insect cuticle in host defense reactions. In: Söderhäll K, Iwanaga S, Vasta GR, eds. New Directions in Invertebrate Immunology. Fair Haven: SOS Publications, 1996;355-374.
60. Muta T, Oda T, Iwanaga S. Horseshoe crab coagulation factor B: a unique serine protease zymogen activated by cleavage of an Ile-Ile bond. J Biol Chem 1993;268:21384-21388.
61. Muta T, Hashimoto R, Miyata T, Nishimura H, Toh Y, Iwanaga S. Proclotting enzyme from horseshoe crab hemocytes: cDNA cloning, disulfide locations, and subcellular localization. J Biol Chem 1990;265:22426-22433.
62. Lee SY, et al. Molecular cloning of cDNA for pro-phenol-oxidase- activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem 1998;257:615-621.
63. Jiang HB, Wang Y, Kanost MR. Pro-phenol oxidase activating proteinase from an insect, Manduca sexta - a bacteria-inducible protein similar to Drosophila easter. Proc Natl Acad Sci USA 1998;95:12220-12225.
64. Satoh D, Horii A, Ochiai M, Ashidi M. Prophenoloxidase-activating enzyme of the silkworm, Bombyx mon. Purification, characterization, and cDNA cloning. J Biol Chem 1999;274:7441-7453.
65. Inamori K, Koori K, Mishima C, Muta T, Kawabata S. A horseshoe crab receptor structurally related to Drosophila Toll. J Endotoxin Res 2000;6:397-399.
66. Rock FL, Hardiman G, Timans JC, Kistelein RA, Bazan JF. A family of human receptors structurally related to Drosophila Toll. Proc Natl Acad Sci USA 1998;95:588-593.
67. Tauszig S, Jouanguy E, Hoffmann JA, Imler J-L. Toll-related receptors and the control of antimicrobial peptide expression in Drosophila. Proc Natl Acad Sci USA 2000;97:10520-10525.
68. Poltorak A, et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutation in Tlr4 gene. Science 1998;282:2085-2088.
69. Kobe B, Deisenhofer J. Crystal stricture of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 1993;366:751-756.
70. Huizinga EG, et al. Structures of glycoprotein Ibα and its complex with von Willebrand factor A1 domain. Science 2002;297:1176-1179.
71. Schubert WD, et al. Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human recep tor E-cadherin. Cell 2002;111:825-836.
72. He XL, et al. Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition. Neuron 2003;38:177-185.
73. Bell JK, Mullen GED, Leifer CA, Mazzoni A, Davies DR, Segal DM. Leucine-rich repeats and pathogen recognition in Toll-like receptors. Trends Immunol 2003;24:528-533.
74. Shimazu R, et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J Exp Med 1999;189:1777-1782.
75. Arbour NC, et al. TLR4 mutations are associated with endotoxin hyporesponsiveness in humans. Nat Genet 2000;25:187-191.
76. Hemmi H, et al. A Toll-like receptor recognizes bacterial DNA. Nature 2000;408:740-745.
77. Lee JH, Voo KS, Skalnik DG. Identification and characterization of the DNA binding domain of CpG-binding protein. J Biol Chem 2001;276:44669-44676.
78. Ariki S, Koori K, Osaki T, Motoyama K, Inamori K, Kawabata S. A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides. Proc Natl Acad Sci USA 2004;101:953-958.
79. Lemmon MA, Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem Sci 1994;19:459-463.
80. Kawabata S, et al. cDNA cloning, tissue distribution, and subcellular localization of horseshoe crab big defensin. Biol Chem 1997;378:289-292.