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The amount of acetylcholinesterase on the parasite surface reflects the differential sensitivity of schistosome species to metrifonate

Published online by Cambridge University Press:  06 April 2009

M. Camacho
Affiliation:
Wellcome Research Centre for Parasitic Infections, Department of Biology, Imperial College of Science, Technology and Medicine, London, UK
R. Tarrab-Hazdai
Affiliation:
Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel
B. Espinoza
Affiliation:
Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel
R. Arnon
Affiliation:
Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel
A. Agnew
Affiliation:
Wellcome Research Centre for Parasitic Infections, Department of Biology, Imperial College of Science, Technology and Medicine, London, UK

Summary

Acetylcholinesterase (AChE) is present in all stages of the life-cycle of schistosomes and is located in muscle and on the surface of the parasite. Metrifonate is a drug that inhibits AChE. We compared the AChEs from three schistosome species (Schistosoma mansoni, Schistosoma haematobium and Schistosoma bovis) that have different susceptibilities to metrifonate in vivo. Sensitivities to AChE inhibitors were similar. The subunits of AChE were 110 kDa and 76 kDa and the dominant molecular form of AChE was a G2 form in all three species. This was the major form on the tegument while additional molecular forms were associated with the internal tissues. Differences in relative amounts of AChE activity between these species were found in the adults but not in the schistosomula. At the adult stage the major difference between species lay in the relative amounts of AChE activity in their teguments. S. haematobium teguments carried 20 times and S. bovis 6·9 times the activity present on S. mansoni teguments. These quantitative differences associate with the relative sensitivities of these species to metrifonate.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1994

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References

REFERENCES

Barker, L. R., Bueding, E. & Timms, A. R. (1966). The possible role of acetylcholine in Schistosoma mansoni. British Journal of Pharmacology 26, 656–65.Google ScholarPubMed
Bloom, A. (1981). Studies of the mode of action of metrifonate and DDVP in schistosomes-cholinesterase activity and the hepatic shift. Acta Pharmacologica et Toxicologica 49, (Suppl. V), 109–13.Google Scholar
Bolton, A. E. & Hunter, W. M. (1973). The labeling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. The Biochemical Journal 133, 529–38.CrossRefGoogle ScholarPubMed
Bueding, E., Liun, C. L. & Rogers, S. H. (1972). Inhibition by metrifonate and dichlorvos of cholinesterases in schistosomiasis. British Journal of Pharmacology 46, 480–7.CrossRefGoogle Scholar
Bushara, H. O., Hussein, M. A., Majid, M. A. & Taylor, M. G. (1982). Effects of praziquantel and metrifonate on Schistosoma bovis infections in Sudanese cattle. Researches in Veterinary Science 33, 125.CrossRefGoogle ScholarPubMed
Denham, D. A. & Holdsworth, R. J. (1971). The effect of metrifonate in-vitro on Schistosoma haematobium and Schistosoma mansoni adults. Transactions of the Royal Society of Tropical Medicine and Hygiene 65, 696.CrossRefGoogle Scholar
Dinnick, N. N. (1968). The effect of Neguvon on Schistosoma rodhaini and Schistosoma bovis in hamsters. Veterinary and Medical Review 1, 30–9.Google Scholar
Espinoza, B., Tarrab-Hazdai, R., Silman, I. & Arnon, R. (1988). Acetylcholinesterase in Schistosoma mansoni is anchored to the membrane via covalently attached phosphatidylinositol. Molecular and Biochemical Parasitology 29, 171–9.CrossRefGoogle Scholar
Espinoza, B., Silman, I., Arnon, R. & Tarrab-Hazdai, R. (1991 a). Phosphatidylinositol-specific phospholipase C induces biosynthesis of acetylcholinesterase via diacylglycerol in Schistosoma mansoni. European Journal of Biochemistry 195, 863–70.CrossRefGoogle ScholarPubMed
Espinoza, B., Tarrab-Hazdai, R., Himmeloch, S. & Arnon, R. (1991 b). Acetylcholinesterase from Schistosoma mansoni: immunological characterization. Immunological Letters 28, 167–74.CrossRefGoogle ScholarPubMed
Eshhar, Z., Ofarim, M. & Waks, T. (1980). Generation of hybridomas secreting murine reaginic antibodies with anti-DNP specificity. Journal of Immunology 124, 775–80.CrossRefGoogle ScholarPubMed
Gear, N. R. & Fripp, P. J. (1974). Comparison of the characteristics of acetylcholinesterase present in four species of schistosoma. Comparative Biochemistry and Physiology 47B, 743–52.Google ScholarPubMed
Goldlust, A., Arnon, R., Silman, I. & Tarrab-Hazdai, R. (1986). Acetylcholinesterase of Schistosoma mansoni. Purification and characterization. Journal of Neuroscience Research 15, 569–81.Google Scholar
James, C., Webbe, G. & Preston, J. (1972). A comparison of the susceptibility to metrifonate of Schistosoma haematobium, S. mattheei and S. mansoni in hamsters. Annals of Tropical Medicine and Parasitology 66, 467.CrossRefGoogle ScholarPubMed
Johnson, C. D. & Russell, R. L. (1975). A rapid, radiometric assay for cholinesterase, suitable for multiple determinations. Analytical Biochemistry 64, 229–38.CrossRefGoogle ScholarPubMed
Levi-Schaffer, F., Tarrab-Hazdai, R., Schryer, M. D., Arnon, R. & Smolarsky, M. (1984 a). Isolation and partial characterization of the tegumental outer membrane of schistosomula of Schistosoma mansoni. Molecular and Biochemical Parasitology 3, 283300.CrossRefGoogle Scholar
Levi-Shaffer, F., Schryer, M. D. & Smolarsky, M. (1982). The resistance of schistosomula of Schistosoma mansoni to antibodies and complement in-vitro does not correlate with the binding of the antibodies to the surface of the parasite. Journal of Immunology 129, 2744–51.CrossRefGoogle Scholar
Levi-Schaffer, F., Tarrab-Hazdai, R., Meshulam, H. & Arnon, R. (1984 b). Effect of phosphonium salts and phosphoranes on the acetylcholinesterase activity on the viability of Schistosoma mansoni parasite. International Journal of Immunopharmacology 6, 619–27.CrossRefGoogle Scholar
Marshall, I. (1987). Experimental chemotherapy. In The Biology of Schistosomiasis. From Genes to Latrines (ed. Rollinson, D. & Simpson, A. G.), pp. 399430. London: Academic Press.Google Scholar
Massoulie, J., Pezzementi, L., Bon, S., Krejci, E. & Valletes, F-M. (1993). Molecular and cellular biology of cholinesterases. Progress in Neurobiology 41, 3191.CrossRefGoogle ScholarPubMed
Pax, R. A., Siefker, C. & Bennett, J. L. (1984). Schistosoma mansoni: differences in acetylcholine, dopamine and serotonin control of circular and longitudinal parasite muscles. Experimental Parasitology 58, 314–24.Google Scholar
Reiner, E. (1981). Esterases in schistosomes. Reaction with substrates and inhibitors. Acta Pharmacologica et Toxicologica 49 (Suppl. V) 72–8.Google Scholar
Simpson, A. J. G., Schryer, M. D., Cesari, I. M., Evans, W. H. & Smithers, S. R. (1981). Isolation and partial purification of the tegumental outer membrane of adult Schistosoma mansoni. Parasitology 83, 163.CrossRefGoogle Scholar
Smithers, S. R. & Terry, R. J. (1965). The infection of laboratory hosts with cercariae of S. mansoni and the recovery of adult worms. Parasitology 55, 695700.CrossRefGoogle Scholar
Tarrab-Hazdai, R., Levi-Schaffer, F., Gonzalez, G. & Arnon, R. (1984 a). Acetylcholinesterase of Schistosoma mansoni molecular forms of solubilized enzyme. Biochimica et Biophysica Acta 790, 61–9.Google Scholar
Tarrab-Hazdai, R., Levi-Schaffer, F., Smolarsky, M. & Arnon, R. (1984 b). Acetylcholinesterase of Schistosoma mansoni: antigenic cross-reactivity with Electrophorus electricus and its functional implications. European Journal of Immunology 14, 205–20.CrossRefGoogle ScholarPubMed
Tarrab-Hazdai, R., Levi-Schaffer, F., Brenner, V., Horowitz, S., Eshar, Z. & Arnon, R. (1985). Protective monoclonal antibody against Schistosoma mansoni: Antigen isolation, characterization and suitability for active immunization. Journal of Immunology 135, 2772–9.CrossRefGoogle Scholar