[Frontiers in Bioscience 3, d973-984, September 1, 1998]
Reprints
PubMed
CAVEAT LECTOR




Table of Conents
 Previous Section   Next Section

EVOLUTION AND PHYLOGENY OF DEFENSE MOLECULES ASSOCIATED WITH INNATE IMMUNITY IN HORSESHOE CRAB

Sadaaki Iwanaga and Shun-ichiro Kawabata

Department of Biology, Faculty of Science, Kyushu University, Fukuoka 812-8581, Japan

Received 7/13/98 Accepted 8/21/98

6. REFERENCES

1. L. Stormer: Phylogeny and taxonomy of fossil horseshoe crab. J. Paleontol. 26, 630-639 (1952)

2. T. Yamazaki: Taxonomy. In: Biology of Horseshoe Crabs. Ed. Sekiguchi, K., pp. 10-21, Science House Co. Ltd., Tokyo (1988)

3. C. N. Jr. Shuster: Serological correspondence among horseshoe crabs (Limulidae). Zoologica, N Y 47, 1-7 (1962)

4. S. Iwanaga, T. Miyata, F. Tokunaga & T. Muta: Molecular mechanism of hemolymph clotting system in Limulus. Thrombos. Res. 68, 1-32 (1992)

5. S. Iwanaga: The limulus clotting reaction. Curr Opin Immunol 5, 74-82 (1993)

6. S. Iwanaga, T. Muta, T. Shigenaga, Y. Miura, N. Seki, T. Saito & S. Kawabata: Role of hemocyte-derived granular components in invertebrate defense. In: Primordial immunity: Foundations for the vertebrate immune system, Eds: Beck, G., Cooper, E., Habicht, G. S., Marchalonis, J. J. Ann N Y Acad Sci 712, 102-116 (1994)

7. S. Iwanaga, T. Muta, T. Shigenaga, N. Seki, K. Kawano, T. Katsu & S. Kawabata: Structure-function relationships of tachyplesins and their analogues. In: Antimicrobial peptides (Ciba Foundation Symposium 186) pp. 160-175, John Wiley & Sons, NY (1994)

8. T. Muta & S. Iwanaga: Clotting and immune defense in Limulidae. In: Progress in molecular and subcellular biology, invertebrate immunology. Eds: Rinkevich, B., Müller, W. E. G. Vol. 15, pp. 154-189, Springer-Verlag, Berlin (1996)

9. T. Muta & S. Iwanaga: The role of hemolymph coagulation in innate immunity. Curr Opin Immunol 8, 41-47 (1996)

10. S. Kawabata, T. Muta & S. Iwanaga: Clotting cascade and defense molecules found in hemolymph of horseshoe crab. In: New Directions in Invertebrate Immunology. Eds: Söderhäll, K., Iwanaga, S., Vasta, G. R. pp 255-284, SOS Publications, Fair Haven, N.J. (1996)

11. P. B. Armstrong: Immunity in the horseshoe crab. In: Immunology of insects and other arthropods. Ed: Gupta, A. P. pp. 4-17, CRC Press, London (1991)

12. Y. Toh, A. Mizutani, F. Tokunaga, T. Muta & S. Iwanaga: Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances. Cell Tissue Res 266, 137-147 (1991)

13. B. Linzen: Invertebrate Oxygen Carriers, pp. 293-296, Springer-Verlag, Berlin (1986)

14. T.-Y. Liu, C. A. S. Minetti, C. L. FortesDias, T. Lin, L. Lin & Y. Lin: C-reactive proteins, limunectin, lipopolysaccharide-binding protein, and coagulin. Ann N Y Acad Sci 712, 146-154 (1994)

15. J. P. Quigley & P. B. Armstrong: An endopeptidase inhibitor, similar to mammalian a2-macroglobulin, detected in the hemolymph of an invertebrate, Limulus polyphemus. J Biol Chem 258, 7903-7906 (1983)

16. J. Levin & F. B. Bang: The role of endotoxin in the extracellular coagulation of Limulus blood. Bull Johns Hoskins Hosp 115, 265-274 (1964)

17. E. H. Muller, J. Levin & R. Holm: Isolation and studies of the granules of the amebocytes of Limulus polyphemus, the horseshoe crab. J Cell Physiol 86, 533-542 (1975)

18. T. Shigenaga, Y. Takayenoki, S. Kawasaki, N. Seki, T. Muta, Y. Toh, A. Ito, & S. Iwanaga: Separation of large and small granules from horseshoe crab (Tachypleus tridentatus) hemocytes and characterization of their components. J Biochem 114, 307-316 (1993)

19. T. Nakamura, H. Furunaka, T. Miyata, F. Tokunaga, T. Muta, S. Iwanaga, M. Niwa, T. Takao & Y. Shimonishi: Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus): Isolation and chemical structure. J Biol Chem 263, 16709-16713 (1988)

20. T. Miyata, F. Tokunaga, T. Yoneya, K. Yoshikawa, S. Iwanaga, M. Niwa, T. Takao & Y. Shimonishi: Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II. Chemical structures and biological activity. J Biochem 106, 663-668 (1989)

21. T. Muta, T. Fujimoto, H. Nakajima & S. Iwanaga: 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 108, 261-266 (1990)

22. T. Shigenaga, T. Muta, Y. Toh, F. Tokunaga & S. Iwanaga: Antimicrobial tachyplesin peptide precursor: cDNA cloning and cellular localization in the horseshoe crab (Tachypleus tridentatus). J Biol Chem 265, 21350-21354 (1990)

23. T. Katsu, S. Nakao & S. Iwanaga: Mode of action of an antimicrobial peptide, tachyplesin I, on biomembranes. Biol Pharm Bull 16, 178-181 (1993)

24. K. Kawano, T. Yoneya, T. Miyata, K. Yoshikawa, F. Tokunaga, Y. Terada & S. Iwanaga: Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus): NMR determination of the b-sheet structure. J Biol Chem 265, 15365-15367 (1990)

25. N. G. Park, S. Lee, O. Oishi, H. Aoyagi, S. Iwanaga, S. Yamashita, S. & M. Ohno: Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices. Biochemistry 31, 12241-12247 (1992)

26. T. Saito, S. Kawabata, T. Shigenaga, J. Cho, H. Nakajima, M. Hirata & S. Iwanaga: A novel big defensin identified in horseshoe crab hemocytes : Isolation, amino acid sequence and antibacterial activity. J Biochem 117, 1131-1137 (1995)

27. S. Kawabata, R. Nagayama, M. Hirata, T. Shigenaga, K. Lal Agarwala, T. Saito, J. Cho, H. Nakajima, H. & S. Iwanaga: Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity. J Biochem 120, 1253-1260 (1996)

28. S. Kawabata, R. Nagayama, M. Hirata, T. Shigenaga, K. Lal Agarwara, T. Saito, J. Cho, H. Nakajima, T. Takao, Y. Shimonishi, T. Takagi & S. Iwanaga: Tachycitin and tachystatin, novel antimicrobial peptides isolated from horseshoe crab hemocytes. In: Peptide Chemistry. Ed. Kitada, C., pp 97-100, Protein Research Foundation, Osaka (1997)

29. T. Nakamura, T. Morita, & S. Iwanaga: Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes: Isolation and characterization. Eur J Biochem 154, 511-521 (1986)

30. F. Tokunaga, T. Miyata, T. Nakamura, T. Morita, K. Kuma, T. Miyata & S. Iwanaga: Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of horseshoe crab hemocytes: Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease. Eur J. Biochem 167, 405-416 (1987)

31. T. Nakamura, F. Tokunaga, T. Morita & S. Iwanaga: Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem 103, 370-374 (1988)

32. T. Nakamura, F. Tokunaga, T. Morita, S. Iwanaga, S. Kusumoto, T. Shiba, T., Kobayashi & K. Inoue: Intracellular serine-protease zymogen, factor C, from horseshoe crab hemocytes. Its activation by synthetic lipid A analogues and acidic phospholipids. Eur J Biochem 176, 89-94 (1988)

33. F. Tokunaga, H. Nakajima & S. Iwanaga: Further studies on lipopolysaccharide-sensitive serine protease zymogen (factor C): Its isolation from Limulus polyphemus hemocytes and identification as an intracellular zymogen activated by alpha-chymotrypsin, not by trypsin. J Biochem 109, 150-157 (1991)

34. T. Muta, T. Miyata, Y. Misumi, F. Tokunaga, T. Nakamura, Y. Toh, Y. Ikehara & S. Iwanaga: Limulus factor C: An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains. J Biol Chem 266, 6554-6561 (1991)

35. S. Nakamura, T. Morita, T. Harada-Suzuki, S. Iwanaga, K. Takahashi & M. Niwa: A clottable enzyme associated with the hemolymph coagulation system of horseshoe crab (Tachypleus tridentatus): Its purification and characterization. J Biochem 92, 781-792 (1982)

36. T. Morita, S. Tanaka, T. Nakamura & S. Iwanaga: A new (1, 3)-b-D-glucan-mediated coagulation pathway found in Limulus amebocytes. FEBS Lett 129, 318-321 (1981)

37. T. Muta, N. Seki, Y. Takaki, R. Hashimoto, T. Oda, A. Iwanaga, F. Tokunaga & S. Iwanaga: Purified horseshoe crab factor G: Reconstitution and characterization of the (1,3)-b-D-glucan-sensitive serine protease cascade. J Biol Chem 270, 892-897 (1995)

38. N. Seki, T. Muta, T. Oda, D. Iwaki, K. Kuma, T. Miyata, T. & S. Iwanaga: Horseshoe crab (1,3)-b-D-glucan-sensitive coagulation factor G. A serine protease zymogen heterodimer with similarities to b-glucan-binding proteins. J Biol Chem 269, 1370-1374 (1994)

39. S. Nakamura, S. Iwanaga, T. Harada & M. Niwa: A clottable protein (coagulogen) from amoebocyte lysate of Japanese horseshoe crab (Tachypleus tridentatus). Its isolation and biochemical properties. J Biochem 80, 1011-1021 (1976)

40. S. Nakamura, T. Takagi, S. Iwanaga, M. Niwa & K. Takahashi:Amino acid sequence studies on the fragments produced from horseshoe crab coagulogen during gel formation: Homologies with primate fibrinopeptide B. Biochem Biophys Res Commun 72, 902-908 (1976)

41. T. Takagi, Y. Hokama, T. Miyata, T. Morita & S. Iwanaga: Amino acid sequence of Japanese horseshoe crab (Tachypleus tridentatus) coagulogen B chain: Completion of the coagulogen sequence. J Biochem 95, 1445-1457 (1984)

42. T. Miyata, M. Hiranaga, M. Umezu & S. Iwanaga: Amino acid sequence of the coagulogen from Limulus polyphemus hemocytes. J Biol Chem 259, 8924-8933 (1984)

43. T. Miyata, K. Usui & S. Iwanaga: The amino acid sequence of coagulogen isolated from Southeast Asian horseshoe crab, Tachypleus gigas. J Biochem 95, 1793-1801 (1984)

44. S. Srimal, T. Miyata, S. Kawabata, T. Morita & S. Iwanaga: The complete amino acid sequence of coagulogen isolated from Southeast Asian horseshoe crab, Carcinoscorpius rotundicauda. J Biochem 98, 305-31837 (1985)

45. T. Miyata, H. Matsumoto, M. Hattori, Y. Sakaki, Y. & S. Iwanaga: Two types of coagulogen mRNAs found in horseshoe crab (Tachypleus tridentatus) hemocytes: Molecular cloning and nucleotide sequences. J Biochem 100, 213-220 (1986)

46. A. Bergner, V. Oganessyan, T. Muta, S. Iwanaga, D. Typke, R. Huber & W. Bode: Crystal structure of limulus coagulogen: The clotting protein from horseshoe crab, a structural homologue of nerve growth factor. EMBO J 15, 6789-6797 (1996)

47. A. Bergner, T. Muta, S. Iwanaga, H.-G. Beisel, R. Delotto & W. Bode: Horseshoe crab coagulogen is an invertebrate protein with a nerve growth factor-like domain. Biol Chem Hoppe-Seyler 379, 283-287 (1997)

48. F. Shishikura, S. Nakamura, K. Takahashi & K. Sekiguchi: Horseshoe crab phylogeny based on amino acid sequences of the fibrinopeptide-like peptide C. J Exp Zool 223, 89-91 (1982)

49. D. T. Dorai, S. Mohan, S. Srimal & B. K. Bachhawat: On the multispecificity of carcinoscorpin, the sialic acid binding lectin from the horseshoe crab Carcinoscorpius rotundicauda. FEBS Lett 148, 98-102 (1982)

50. D. T. Dorai, B. K. Bachhawat, S. Bishayee, K. Kannan & D. R. Rao: Further characterization of the sialic acid-binding lectin from the horseshoe crab Carcinoscorpius rotundicauda. Arch Biochem Biophys 209, 325-333 (1981)

51. C.N. Jr. Shuster: Horseshoe "crab." Estuarine Bull, Univ. Delaware Marine Lab 5, 1-9 (1960)

52. F. Shishikura, S. Nakamura, K. Takahashi & K. Sekiguchi: Cogaulogen from the four living species of horseshoe crabs (Limuridae). Comparison of their biochemical and immunological properties. J Biochem 94, 1279-1287 (1983)

53. T. Nakamura, T. Horiuchi, T. Morita & S. Iwanaga: Purification and properties of intracellular clotting factor, factor B, from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem 99, 847-857 (1986)

54. T. Muta, T. Oda & S. Iwanaga: Horseshoe crab coagulation factor B: A unique serine protease zymogen activated by cleavage of an Ile-Ile bond. J Biol Chem 268, 21384-21388 (1993)

55. T. Nakamura, T. Morita & S. Iwanaga: Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: Its purification and properties. J Biochem 97, 1561-1574 (1985)

56. T. Muta, R. Hashimoto, T. Miyata, H. Nishimura, Y. Toh & S. Iwanaga: Proclotting enzyme from horseshoe crab hemocytes: cDNA cloning, disulfide locations, and subcellular localization. J Biol Chem 265, 22426-22433 (1990)

57. S. Iwanaga: Primitive coagulation systems and their message to modern biology. Thrombosis and Haemostasis, 70, 48-55 (1993)

58. S. Tomlinson: Complement defense mechanisms. Curr Opin Immunol 5, 83-89 (1993)

59. Y. Miura, S. Kawabata & S. Iwanaga: A limulus intracellular coagulation inhibitor with characteristics of the serpin superfamily. J Biol Chem 269, 542-547 (1994)

60. Y. Miura, S. Kawabata, Y.Wakamiya, T. Nakamura & S. Iwanaga: A limulus intracellular coagulation inhibitor type 2. J Biol Chem 270, 558-565 (1995)

61. K. Lal Agarwala, S. Kawabata, Y. Miura, Y. Kuroki & S. Iwanaga: Limulus intracellular coagulation inhibitor type 3: Purification, characterization, cDNA cloning, and tissue localization. J Biol Chem 271, 23768-23774 (1996)

62. M. R. Kanost & H. Jiang: Proteinase inhibitors in invertebrate immunity. In: New directions in invertebrate immunology. Eds: Söderhäll, K., Iwanaga, S. & Vasta, G. R., pp.153-173, SOS publications, Fair Haven, NJ (1996)

63. R. W. Carrell & D. R. Boswell: Serpins: The superfamily of plasma serine proteinase inhibitors. In: Proteinase inhibitors. Eds: Barrett, A. J. & Salvesen, G., pp. 403420, Elsevier, NY (1986)

64. S. Tanaka, T. Nakamura, T. Morita & S. Iwanaga: Limulus anti-LPS factor: An anticoagulant which inhibits the endotoxin-mediated activation of limulus coagulation system. Biochem Biophys Res Commun 105, 717-723 (1982)

65. K. Ohashi, M. Niwa, T. Nakamura, T. Morita & S. Iwanaga: Anti-LPS factor in the horseshoe crab, Tachypleus tridentatus. Its hemolytic activity on the red blood cell sensitized with lipopolysaccharide. FEBS Lett 176, 207-210 (1984)

66. T. Morita, S. Ohtsubo, T. Nakamura, S. Tanaka, S. Iwanaga, K. Ohashi, K. & M. Niwa: Isolation and biological activities of Limulus anticoagulant (anti-LPS factor) which interact with lipopolysaccharide (LPS). J Biochem 97, 1611-1620 (1985)

67. J. Aketagawa, T. Miyata, S. Ohtsubo, T. Nakamura, T. Morita, H. Hayashida, T. Miyata, S. Iwanaga, T. Takao & Y. Shimonishi: Primary structure of limulus anticoagulant anti-lipopolysaccharide factor. J Biol Chem 261, 7357-7365 (1986)

68. T. Muta, T. Miyata, F. Tokunaga, T. Nakamura & S. Iwanaga: Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. J Biochem 101, 1321-1330 (1987)

69. T. Muta, T. Nakamura, H. Furunaka, F. Tokunaga, T. Miyata, M. Niwa & S. Iwanaga: Primary structures and functions of anti-lipopolysaccharide factor and tachyplesin peptide found in horseshoe crab hemocytes. Adv Exp Med Biol 256, 273-285 (1990)

70. S. Kawabata, T. Saito, K. Saeki, N. Okino, A. Mizutani, Y. Toh & S. Iwanaga: cDNA cloning, tissue distribution, and subcellular localization of horseshoe crab big defensin. Biol Chem Hoppe-Seyler 378, 289-292 (1997)

71. R. U. Lehrer, T. Ganz & M. E. Selsted: Defensins: Endogenous antibiotic peptides of animal cells. Cell 64, 229-230 (1991)

72. T. Ganz & R. I. Lehrer: Defensins. Curr Opin Immunol 6, 584-589 (1994)

73. J. Lambert, E. Keppi, J.-L. Dimarcq, C. Wicker, J.-M. Reichhart, B. Dunbar, P. Lepage, A. V. Dorsselaer, J. Hoffmann, J. Fothergill & D. Hoffmann: Insect immunity: Isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. Proc Natl Acad Sci USA 86, 262-266 (1989)

74. K. Ando, M. Okada & S. Natori: Purification of sarcotoxin II, antibacterial proteins of Sarcophaga peregrina (flesh fly) larvae. Biochemistry 26, 226-230 (1987)

75. K. Matsuyama & S. Natori: Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina. J Biol Chem 263, 17112-17116 (1988)

76. J. E. Gabay & R. P. Almeida: Antibiotic peptides and serine protease homologs in human polymorphonuclear leukocytes: defensins and azurocidin. Curr Opin Immunol 5, 97-102 (1993)

77. G. Diamond, M. Zasloff, H. Eck, M. Brasseur, W. E. Maloy & C. L. Bevins: Tacheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal muscosa: Peptide isolation and cloning of cDNA. Proc Natl Acad Sci USA 88, 3952-3956 (1991)

78. D. E. Jones & C. L. Bevins: Paneth cells of the human small intestine express an antimicrobial peptide gene. J Biol Chem 267, 23216-23225 (1992)

79. D. F. Mosher, P. E. Schad. & J. M. Vann: Cross-linking of collagen and fibrinogen by factor XIIIa. Locarization of participating glutaminyl residues to a tryptic fragment of fibronectin. J Biol Chem 255, 1181-1188 (1980)

80. C. S. Greenberg, PJ. Brickbichler & R. H. Rice: Transglutaminase. Multifunctional cross-linking enzymes that stabilize tissue. FASEB J 5, 3071-3077 (1991)

81. M. A. Phillips, B. E. Stewart & R. H. Rice: Genomic structure of keratinocyte transglutaminase. J Biol Chem 267, 2282-2286 (1992)

82. J. E. Folk & J. S. Finlayson: The e(g-gulutamyl)lysine crosslinkand the catalytic role of transglutaminase. Adv Protein Chem 31, 1-133 (1977)

83. F. Tokunaga, M. Yamada, T. Miyata, Y.-L. Ding, M. Hiranaga-Kawabata, T. Muta, A. Ichinose, E. W. Davie & S. Iwanaga: Limulus hemocyte transglutaminase: Its purification and characterization, and identification of the intracellular substrates. J Biol Chem. 268, 252-261 (1993)

84. F. Tokunaga, T. Muta, S. Iwanaga, A. Ichinose, E. W. Davie, K. Kuma, T. Miyata: Limulus hemocyte transglutaminase: cDNA cloning, amino acid sequence, and tissue localization. J Biol Chem 268, 262-268 (1993)

85. G. M. Fuller & R. F. Doolittle: Studies on invertebrate fibrinogen. Purification and characterization of fibrinogen from spiny lobster. Biochemistry 10, 1305-1311 (1971)

86. K. Söderhäll, S. Iwanaga & G. R. Vasta: New Directions in Invertebrate Immunology, SOS Publications, Fair Haven, New Jersey (1996)

87. M. W. Johansson & K. Söderhäll: The prophenoloxidase activating system and associated proteins in invertebrates. In: Progress in Molecular and Subcellular Biology, Invertebrate Immunology. Eds: Rinkevich B., Müller W. E. G., Vol. 15, pp. 46-66, Springer-Verlag, Berlin (1996)

88. P. B. Armstrong, S. Swarnakar, S. Srimal, S. Misquith, E. A. Hahn, R. T. Aimes & J. P. Quigley: A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins. J Biol Chem 271, 14717-14721 (1996)

89. N. Y. Nguyen, A. Suzuki, R. A. Boykins & T.-Y. Liu: Amino acid sequence of Limulus C-reactive protein: Evidence of polymorphism. J Biol Chem 261, 10456-10465 (1986)

90. R. Melchior, J. P. Quigley & P. B. Armstrong: a2-Macroglobulin-mediated clearance of proteases from the plasma of the American horseshoe crab, Limulus polyphemus. J Biol Chem 270, 13496-13502 (1995)

91. D. Iwaki, S. Kawabata, Y. Miura, A. Kato, P. B. Armstrong, J. P. Quigley, K. L. Nielsen, K. Dolmer, L. Sottrup-Jensen & S. Iwanaga: Molecular cloning of limulus a2-macroglobulin. Eur J Biochem 242, 822-831 (1996)

92. P. B. Armstrong, L. Sottrup-Jensen, A. Ikai, S. Srimal, & J. P. Quigley: a2-M in the horseshoe crab. Ann N Y Acad Sci 737, 188-201 (1994)

93. F. A. Robey & T.-Y. Liu: Limulin: A C-reactive protein from Limulus polyphemus. J Biol Chem 256, 969-975 (1981)

94. S. Iwanaga, S. Kawabata & T. Muta: New types of clotting factors and defense molecules found in horseshoe crab hemolymph. Their stuructures and functions (JB review). J Biochem 123, 1-15 (1998)