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Hymenolepis diminuta: influence of metacestodes on synthesis and secretion of fat body protein and its ovarian sequestration in the intermediate host, Tenebrio molitor

Published online by Cambridge University Press:  06 April 2009

Hilary Hurd  and
C. Arme
Hilary Hurd
Affiliation:
Parasitology Research Laboratory, Department of Biological Sciences, University of Keele, Keele, Staffordshire ST5 5BG
C. Arme
Affiliation:
Parasitology Research Laboratory, Department of Biological Sciences, University of Keele, Keele, Staffordshire ST5 5BG
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Summary

Female Tenebrio molitor infected with metacestodes of Hymenolepis diminuta exhibit elevated concentrations of female-specific proteins in their haemolymph and the origin of these has been investigated. Following a 4 h in vitro incubation with [14C]leucine, fat bodies from non-infected females secreted 13 times more protein than those from females 12 days post-infection. A comparison of the uptake in vivo of radio-isotope labelled amino acids by ovaries from non-infected and infected beetles of various ages revealed no differences; however, a 51·5% decrease in protein sequestration was detected in females 12 days post-infection. Electrophoresis of homogenates of radio-isotope labelled ovaries demonstrated that the majority of label was associated with vitellin sub-units. It is suggested that the decrease in vitellogenin sequestration associated with infection results in an increase in the haemolymph concentration of these proteins despite a concomitant reduction in their secretion by fat bodies. Both fat body synthesis and ovarian sequestration are under juvenile hormone control and it is proposed that metacestodes of H. diminuta may cause a reduction in the concentration of this hormone in the intermediate host.

Type
Research Article
Information
Parasitology , Volume 93 , Issue 1 , August 1986 , pp. 111 - 120
Copyright
Copyright © Cambridge University Press 1986

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References

Anderson, L. M. & Telfer, W. H. (1970). Extracellular concentrations of protein in the cecropia moth follicle. Journal of Cell Physiology 76, 37–54.CrossRefGoogle ScholarPubMed
Arme, C., Bridges, J. F. & Hoole, D. (1983). Pathology of cestode infections in the vertebrate host. In Biology of the Eucestoda, vol. 2 (ed. Arme, C. and Pappas, P. W.), pp. 499–539. London: Academic Press.Google Scholar
Davey, K. G. (1981). Hormonal control of vitellogenin uptake in Rhodnius prolixus Stal. American Zoologist 21, 701–5.Google Scholar
Della-Cioppa, G. & Englemann, F. (1980). Juvenile hormone stimulated proliferation of endoplasmic reticulum in fat body cells of a vitellogenic insect Leucophaea maderae (Blattaria). Biochemical and Biophysical Research Communications 93, 825–32.CrossRefGoogle ScholarPubMed
Dortland, J. F. & Esch, Th. H. (1979). A fine structural survey of the development of the adult fat body of Leptinotarsa decemlineata. Cell and Tissue Research 20, 421–30.Google Scholar
Englemann, F. (1979). Insect vitellogenin: identification, biosynthesis and role in vitellogenesis. Advances in Insect Physiology 14, 49–108.CrossRefGoogle Scholar
Englemann, F. (1980). Endocrine control of vitellogenin synthesis. In Insect biology in the future (ed. Locke, M. and Smith, D. S.), pp. 311–324. New York: Academic Press.CrossRefGoogle Scholar
Freeman, R. S. (1983). Pathology of the invertebrate host–metacestode relationship. In Biology of the Eucestoda, vol. 2 (ed. Arme, C. and Pappas, P. W.) pp. 441–449. London and New York: Academic Press.Google Scholar
Gordon, R., Condon, W. J., Edgar, W. J. & Babie, S. J. (1978). Effects of mermithid parasitism on the haemolymph composition of the larval blackflies Proximulium mixtum-fuscum and Simulium venustum. Parasitology 77, 367–74.CrossRefGoogle Scholar
Gordon, R. & Webster, J. M. (1971). Mermis nigrescens: Physiological relationships with its host, the adult locust Schistocerca gregaria. Experimental Parasitology 29, 66–79.CrossRefGoogle ScholarPubMed
Gordon, R., Webster, J. M. & Hislop, T. G. (1973). Mermithid parasitism, protein turnover and vitellogenesis in the desert locust, Schistocerca gregaria Forskal. Comparative Biochemistry and Physiology 46B, 575–93.Google Scholar
Hagedorn, H. H. & Kunkel, J. G. (1979). Vitellogenin and vitellin in insects. Annual Review of Entomology 24, 475–505.CrossRefGoogle Scholar
Harnish, D. G. & White, B. N. (1982). Insect vitellins: Identification, purification and characterization from eight orders. Journal of Experimental Zoology 220, 1–10.Google Scholar
Hurd, H. & Arme, C. (1984 a). Tenebrio molitor (Coleoptera): effect of metacestodes of Hymenolepis diminuta (Cestoda) on haemolymph amino acids. Parasitology 89, 245–51.Google Scholar
Hurd, H. & Arme, C. (1984 b). Pathology of Hymenolepis diminuta infections in Tenebrio molitor: effect of parasitism on haemolymph proteins. Parasitology 89, 253–262.Google Scholar
Hurd, H., Browne, P. & Arme, C. (1982). Changes in the haemolymph composition of Tenebrio molitor infected with cysticercoid larvae of Hymenolepis diminuta. Parasitology 84, 65.Google Scholar
Jutsum, A. R. & Goldsworthy, G. J. (1974). Some effects of mermithid infection on metabolic reserves and flight in Locusta. International Journal for Parasitology 4, 625–30.Google Scholar
Lange, A. B. & Loughton, B. G. (1981). The selective accumulation of vitellogenin in the locust oocyte. Experientia 37, 273–4.Google Scholar
Laverdure, A.-M. (1970). Action de l'ecdysone et de l'ester methylique du farnesol sur l'ovaire nymphal de Tenebrio molitor (Coléoptère) cultive in vitro. Annales D'Endocrinologie 31, 516–24.Google Scholar
Lieutier, F. (1984). Ovarian and fat body concentrations in Ips sexdentatus (Coleoptera: Scolytidae) parasitized by nematodes. Journal of Invertebrate Pathology 43, 21–31.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–75.CrossRefGoogle ScholarPubMed
Pratt, G. E. & Davey, K. G. (1972). Corpus allatum and oogenesis in Rhodnius prolixus (Stal). 1. The effects of allatectomy. Journal of Experimental Biology 56, 201–14.Google Scholar
Reid, P. C. & Chen, T. T. (1981). Juvenile hormone controlled vitellogenin synthesis in the fat body of the locust Locusta migratoria: Isolation and characterization of vitellogenin polysomes and their induction in vivo. Insect Biochemistry 2, 297–305.CrossRefGoogle Scholar
Shigematsu, H. (1958). Synthesis of blood protein by the fat body in the silkworm, Bombyx mori. Nature, London 182, 880–2.Google Scholar
Thompson, S. N. (1983). Biochemical and physiological effects of metazoan endoparasites on their host species. Comparative Biochemistry and Physiology 74B, 183–211.Google Scholar
Thong, C. H. S. & Webster, J. M. (1975). Effects of Contortylenchus reversus (Nematoda: Sphaerulariidae) on haemolymph composition and oocyte development in the beetle Dendroctonus pseudotsugae (Coleoptera: Scolytidae). Journal of Invertebrate Pathology 26, 91–8.Google Scholar
Ullmann, S. L. (1973). Oogenesis in Tenebrio molitor: Histological and autoradiographical observations on pupal and adult ovaries. Journal of Embryology and Experimental Morphology 30, 179–217.Google Scholar
Voge, M. & Heyneman, D. (1957). Development of Hymenolepis nana and Hymenolepis diminuta (Cestoda: Hymenolepididae) in the intermediate host Tribolium confusum. University of California Publications in Zoology 59, 549–80.Google Scholar
Weaver, R. J., Pratt, G. E., Hamnett, A. F. & Jennings, R. C. (1980). The influence of incubation conditions on the rates of juvenile hormone biosynthesis by the corpora allata, isolated from adult females of the beetle Tenebrio molitor. Insect Biochemistry 10, 245–54.Google Scholar
Weber, K. & Osborn, M. (1969). The reliability of molecular weight determination by dodecylsulphate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244, 4406–12.Google Scholar
Wyatt, G. R. (1980). The fat body as a protein factory. In Insect Biology in the Future, (ed. Locke, M. and Smith, D. S.), pp. 201–227. New York: Academic Press.CrossRefGoogle Scholar