Abstract
Perhaps the most tantalizing question to be answered in our pursuit of an in-depth understanding of the evolutionary development of the immune system is that of the origins of adaptive humoral immunity. Immunoglobulins, encoded by sets of rearranging genes, are the mediators of adaptive humoral immunity and these molecules, together with the genes that encode them, have been extensively characterized down to and including the phylogenetic level of the elasmobranchs. Failure to conclusively demonstrate adaptive humoral immune function in the primitive vertebrates and invertebrates raises additional questions about the origins of the rearranging Ig gene system and the humoral defense mechanisms employed by the multitude of species that encompass this group of organisms. The studies described in this chapter deal in part with the latter issue in the phylogenetically primitive vertebrate group, the cyclostomes.
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References
Bogaert T, Brown N, Wilcox M (1987) The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localised to muscle attachments. Cell 51: 929–940
Davis MM, Bjorkman P (1988) T cell antigen receptor genes and T cell recognition. Nature 334: 395–402
Davis MM, Cohen DI, Nielsen EA, DeFranco AL, Paul WE (1982) The isolation of B and T cell-specific genes. In: Vitetta ES, Fox CF (eds) B and T cell tumours. Academic Press, New York, pp 215–220
Farries TC, Atkinson JP (1991) Evolution of the complement system. Immunol Today 12: 295–300
Fearon DT, Wong WW (1983) Complement ligand-receptor interactions that mediate biological responses. Annu Rev Immunol 1: 243–271
Fujii T, Nakamura T, Sekizawa A, Tomonaga S (1992) Isolation and characterisation of a protein from hagfish serum that is homologous to the third component of the mammalian complement system. J Immunol 148: 117–123
Fujii T, Nakamura T, Tomonaga S (1993) Identification and characterisation of a variant of the third component of complement (C3) in hagfish serum. Zool Sci (Suppl) 10: 83
Hagen M, Filosa MF, Youson JH (1985) The immune response in adult sea lamprey, Petromyzon marinus: the effect of temperature. Comp Biochem Physiol 82A: 207–210
Hanley PJ, Seppelt IM, Gooley AA, Hook JW, Raison RL (1990) Distinctive Ig H chains in a primitive vertebrate, Eptatretus stouti. J Immunol 145: 3823–3828
Hanley PJ, Hook JW, Raftos DA, Gooley AA, Trent R and Raison RL (1992) Hagfish humoral defense protein exhibits structural and functional homology with mammalian complement proteins. Proc Natl Acad Sci USA 89; 7910–7914
Harrelson AL, Goodman CS (1988) Growth cone guidance in insects: fasciclin II is a member of the immunoglobulin superfamily. Science 242: 700–703
Hashimoto K, Nakanishi T, Kurosawa Y (1990) Isolation of carp genes encoding major histocompatibility complex antigens. Proc Natl Acad Sci USA 87: 6863–6867
Hashimoto K, Nakanishi T, Kurosawa Y (1992) Identification of a shark sequence resembling the major histocompatibility complex class I a3 domain. Proc Natl Acad Sci USA 89: 2209–2212
Hildemann WH (1981) Immunophylogeny: from sponges to hagfish to mice. In: Hildemann WH (ed) Frontiers in immunogenetics. Elsevier, New York, pp 3–19
Hildemann WH, Thoenes GH (1967) Immunological responses of Pacific hagfish. I. Skin transplantation immunity. Transplantation 7: 506–521
Hildemann WH, Raison RL, Chenung G, Hull CJ, Akaka L and Okamoto J (1977) Immunological specificity and memory in a scleractinian coral. Nature 270: 219–223
Hinds KR, Litman GW (1986) Major reorganisation of immunoglobulin VH segmental elements during vertebrate evolution. Nature 320: 546–549
Hugli, TE (1989) Chemotaxis. Curr Opin Immunol 2: 19–27
Ishiguro H, Kobayashi K, Suzuki M, Titani K, Tomonaga S, Kurosawa Y (1992) Isolation of a hagfish gene that encodes a complement component. EMBO J 11: 829–837
Kobayashi KS, Tomonaga S, Hagiwara K (1985) Isolation and characterisation of immunoglobulin of hagfish, Eptatretus burgeri, a primitive vertebrate. Mol Immunol 22: 1091–1097
Larsen GL, Henson PM (1983) Mediators of inflammation. Annu Rev Immunol 1: 335–360
Law SJC, Levine RP (1981) Binding reaction between the third human complement protein and small molecules. Biochemistry 20: 7457–7463
Linthicum DS, Hildemann WH (1970) Immunologic responses of Pacific hagfish. III. Serum antibodies to cellular antigens. J Immunol 105: 912–918
Litman GW, Frommel D, Finstad J, Howell J, Pollara BW, Good RA (1970) The evolution of the immune response. VIII. Structural studies of the lamprey immunoglobulin. J Immunol 105: 1278–1285
Marchalonis JJ, Cone RE (1973) The phylogenetic emergence of vertebrate immunity. Aust J Exp Biol Med Sci 51: 461–488
Marchalonis JJ, Edelman GM (1968) Phylogenetic origins of antibody structure. III. Antibodies in the primary immune response of the sea lamprey, Petromyzon marinus. J Exp Med 127: 891–914
Newton RA, Raftos DA, Raison RL, Geczy CL (1994) Chemotactic responses of hagfish ( Vertebrata, Agnatha) leukocytes. Dev Comp Immunol 18: 295–304
Nonaka M, Fuji T, Kaidoh T, Natsuume-Sakai S, Nonaka M, Yamaguchi N, Takahashi M (1984) Purification of a lamprey complement protein homologous to the third component of the mammalian complement system. J Immunol 133: 3242–3249
Obenauf SD, Hyder-Smith S (1985) Chemotaxis of nurse shark leukocytes. Dev Comp Immunol 9: 221–230
Pollara BW, Litman GW, Finstad J, Howell J, Good RA (1970) The evolution of the immuneresponse. VII. Antibody formation to human “O” cells and properties of the immunoglobulin in lamprey. J Immunol 105: 738–745
Raftos DA, Briscoe DA, Tait NN (1988) Mode of recognition of allogeneic tissue in the solitary urochordate, Styela plicata. Transplantation 45: 1123–1126
Raftos DA, Hook JW, Raison RL (1992) Complement-like protein from the phylogenetically primitive vertebrate, Eptatretus stouti, is a humoral opsonin. Comp Biochem Physiol 103B: 379–384
Raison RL, Hull CJ, Hildemann WH (1978a) Production and specificity of antibodies to streptococci in the Pacific hagfish, Eptatretus stouti. Dev Comp Immunol 2: 253–262
Raison RL, Hull CJ, Hildemann WH (1978b) Characterisation of immunoglobulin from the Pacific hagfish, a primitive vertebrate. Proc Natl Acad Sci USA 75: 5679–5682
Raison RL, Gilbertson P, Wotherspoon J (1987) Cellular requirements for mixed leukocyte reactivity in the cyclostome, Eptatretus stouti. Immunol Cell Biol 65: 183–188
Raison RL, Coverley J, Hook JW, Towns P, Weston KM, Raftos DA (1994) A cell-surface opsonic receptor on leukocytes from the phylogenetically primitive vertebrate, Eptatretus stouti. Immunol Cell Biol 72: 326–332
Seeger MA, Haffley L, Kaufman TC (1988) Characterization of amalgam: a member of the immunoglobulin superfamily from Drosophila. Cell 55: 589–600
Sun S-C, Lindstrom I, Boman HG, Faye I, Schmidt O (1990) Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science 250: 1729–1732
Thoenes GH, Hildemann WH (1969) Immunologic responses of Pacific hagfish. II. Serum antibody production to soluble antigens. In: Sterzl J, Riha I (eds) Developmental aspects of antibody formation and structure. Czech Acad Sci Prague, pp 711–721
Varner J, Neame P, Litman GW (1991) A serum heterodimer from hagfish (Eptatretus stouti) exhibits structural similarity and partial sequence identity with immunoglobulin. Proc Natl Acad Sci USA 88: 1746–1750
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© 1996 Springer-Verlag Berlin Heidelberg
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Raison, R.L. (1996). The Interface Between Invertebrates and Vertebrates: Complement vs Ig. In: Cooper, E.L. (eds) Invertebrate Immune Responses. Advances in Comparative and Environmental Physiology, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79693-7_8
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DOI: https://doi.org/10.1007/978-3-642-79693-7_8
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