Abstract
Antibodies have not been identified in invertebrates. It appears that rearranging immunoglobulin (Ig) genes and clonal selection arose in vertebrates after their evolutionary divergence from the invertebrates (Marchalonis and Schluter 1990). However, insects have been shown to mount a humoral response to bacterial infections, which includes the synthesis and secretion of a battery of antibacterial proteins (Dunn 1990; Hultmark 1993). It has recently been recognized through analysis of amino acid sequences deduced from cloned cDNAs that one of the hemolymph proteins induced by bacteria in the lepidopteran insects Hyalophora cecropia and Manduca sexta is a member of the Ig superfamily (Sun et al. 1990; Ladendorff and Kanost 1991). This protein, which has been named hemolin (previously known as P4), has no direct antibacterial activity but may function in recognition of bacteria and/or in modulation of the adhesive properties of hemocytes. Hemolin is composed of four Ig domains (see Sect. 4) which have more similarity in amino acid sequence to Ig domains from cell adhesion molecules than to those from antibodies. We will review the short history of research on hemolin and pose some hypotheses regarding the functions of hemolin in insect immunity.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Andersson K, Steiner H (1987) Structure and properties of protein P4, the major bacteriainducible protein in pupae of Hyalophora cecropia. Insect Biochem 17: 133–140
Barthels D, Santoni MJ, Wille W, Ruppert C, Chaix JC, Hirsch MR, Fontecilla-Camps JC, Goridis C (1987) Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a Mr 79,000 polypeptide without a membrane-spanning region. EMBO J 6: 907–914
Dunn PE (1990) Humoral immunity in insects. Bioscience 40: 738–744
Faye I, Pye A, Rasmuson T, Boman HG, Boman IA (1975) Insect immunity II. Simultaneous induction of antibacterial activity and selective synthesis of some hemolymph proteins in diapausing pupae of Hyalophora cecropia and Samia cynthia. Infect Immun 12: 1426–1438
Feng D-F, Doolittle RF (1990) Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol 183: 375–387
Grumet M, Mauro V, Burgoon MP, Edelman GM, Cunningham BA (1991) Structure of a new nervous system glycoprotein, Nr-CAM, and its relationship to subgroups of neural cell adhesion molecules. J Cell Biol 113: 1399–1412
Hughes JA, Hurlbert RE, Rupp RA, Spence KD (1983) Bacteria-induced haemolymph proteins of Manduca sexta pupae and larvae. J Insect Physiol 29: 625–632
Hultmark D (1993) Immune reactions in Drosophila and other insects: a model for innate immunity. Trends Genet 9: 178–183
Hunkapiller T, Hood L (1989) Diversity of the immunoglobulin gene superfamily. Adv Immunol 44: 1–63
Hunkapiller T, Goverman J, Koop BF, Hood L (1989) Implications of the diversity of the immunoglobulin gene superfamily. Cold Spring Harbor Symp Quant Biol 54: 15–29
Hurlbert RE, Karlinsey JE, Spence KD (1985) Differential synthesis of bacteria-induced proteins of Manduca sexta larvae and pupae. J Insect Physiol 31: 205–215
Kanost MR, Zepp MK, Ladendorff NE, Andersson LA (1994) Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae. Arch Insect Biochem Physiol 27: 123–136
Ladendorff NE, Kanost MR (1990) Isolation and characterization of bacteria-induced protein P4 from hemolymph of Manduca sexta. Arch Insect Biochem Physiol 15: 33–41
Ladendorff NE, Kanost MR (1991) Bacteria-induced protein P4 (hemolin) from Manduca sexta: a member of the immunoglobulin superfamily which can inhibit hemocyte aggregation. Arch Insect Biochem Physiol 18: 285–300
Marchalonis JJ, Schluter SF (1990) Origins of immunoglobulins and immune recognition molecules. Bioscience 40: 758–768
Rasmuson T, Boman HG (1979) Insect immunity V. Purification and some properties of immune protein P4 from hemolymph of Hyalophora cecropia. Insect Biochem 9: 259–264
Ryan RO, Cole KD, Kawooya JK, Wells MA, Law JH (1988) Identification and characterization of a novel postlarval hemolymph protein from Manduca sexta. Arch Insect Biochem Physiol 9: 81–90
Schmidt O, Faye I, Lindstrom-Dinnetz I, Sun S-C (1993) Specific immune recognition of insect hemolin. Dev Comp Immunol 17: 195–200
Springer TA (1990) Adhesion receptors of the immune system. Nature 346: 425–434
Sun S-C, Faye I (1992) Cecropia immunoresponsive factor, an insect immunoresponsive factor with DNA-binding properties similar to nuclear-factor KB. Eur J Biochem 204: 885–892
Sun SC, Lindström I, Boman HG, Faye I, Schmidt O (1990) Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science 250: 1729–1732
Trenczek T (1988) Injury and immunity in insects. In: Sehnal F, Zabza A, Denlinger DL (eds) Endocrinological frontiers in physiological insect ecology. Wroclaw Tech Univ Press, Wroclaw, pp 369–378
Trenczek T, Faye I (1988) Synthesis of immune proteins in primary cultures of fat body from Hyalophora cecropia. Insect Biochem 18: 299–312
Volkmer H, Hassel B, Wolff JM, Frank R, Rathjen FG (1992) Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily. J Cell Biol 118: 149–161
Wang Y, Willott E, Kanost MR (1995) Organization and expression of the hemolin gene, a member of the immunoglobulin superfamily in an insect, Manduca sexta. Insect Mol Biol 4: 113–123
Williams AF, Barclay AN (1988) The immunoglobulin superfamily — domains for cells surface recognition. Annu Rev Immunol 6: 381–405
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Kanost, M.R., Zhao, L. (1996). Insect Hemolymph Proteins from the Ig Superfamily. 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_7
Download citation
DOI: https://doi.org/10.1007/978-3-642-79693-7_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-79695-1
Online ISBN: 978-3-642-79693-7
eBook Packages: Springer Book Archive