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Acetylcholinesterase in infective-stage larvae of Haemonchus contortus, Ostertagia circumcincta and Trichostrongylus colubriformis resistant and susceptible to benzimidazole anthelmintics

Published online by Cambridge University Press:  06 April 2009

I. A. Sutherland  and
D. L. Lee
I. A. Sutherland
Affiliation:
Department of Pure and Applied Biology, University of Leeds, Leeds LS2 9JT
D. L. Lee
Affiliation:
Department of Pure and Applied Biology, University of Leeds, Leeds LS2 9JT
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Summary

The amounts of acetylcholinesterase (AChE) in homogenates of infective-stage larvae of strains, from different countries, of Haemonchus contortus, Ostertagia circumcincta and Trichostrongylus colubriformis resistant or susceptible to benzi-midazole (BZ) anthelmintics, were compared using a rapid colorimetric assay. The levels of AChE were much greater in those strains which were BZ-resistant than in BZ-susceptible populations. The larvae of susceptible and resistant H. contortus contained less AChE than did the larvae of the other two species. One-way analysis of variance showed that the observed differences between susceptible and resistant strains were significant in each of the species studied. It is suggested that the extra enzyme may act as an anthelmintic-detoxifying enzyme, may inactivate the active site of the anthelmintic or may prevent binding of the anthelmintic to its receptor

Keywords

acetylcholinesterasanthelmintic resistancebenzimidazoleHaemonchus contortusnematodeOstertagia circumcinctathiabendazoleTrichostrongylus colubriformis
Type
Research Article
Information
Parasitology , Volume 107 , Issue 5 , December 1993 , pp. 553 - 557
Copyright
Copyright © Cambridge University Press 1993

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References

REFERENCES

Ellman, G. L., Courtney, K. D., Andres, V. & Featherstone, R. M. (1961). A new and rapid colorimetric determination of acetylcholinesterase activity. Biochemical Pharmacology 7, 88–95.CrossRefGoogle ScholarPubMed
Guzman-varon, R., Monroe, R. J. & Guthrie, F. E. (1974). Evaluation of cholinesterases in strains of Heliothis virescens with widely differing responses to insecticides. Journal of Economic Entomology 67, 187–9.CrossRefGoogle ScholarPubMed
Lacey, E. (1985). The biochemistry of anthelmintic resistance. In Resistance in Nematodes to Anthelmintic Drugs (ed. Anderson, N. & Waller, P. J.), pp. 69–79. Glebe, N.S.W. 2037: C.S.I.R.O./Australian Wool Corporation.Google Scholar
Lacey, E. (1988). The role of the cytoskeletai protein, tubulin, in the mode of action and mechanism of drug-resistance to benzimidazoles. International Journal for Parasitology 18, 885–936.CrossRefGoogle ScholarPubMed
Lacey, E. (1990). Mode of action of benzimidazoles. Parasitology Today 6, 112–15.CrossRefGoogle ScholarPubMed
Lau, P. H. & Sudderuddin, k. I. (1981). Studies on insecticide resistance in a Malaysian strain of Musca domestica L. Southeast Asian Journal of Tropical Medicine and Public Health 12, 213–21.Google Scholar
Miyata, T., Saito, T., Fukamachi, S., Kiritani, K., Kawahara, S., Yoshioka, K., Ozaki, K., Sasaki, Y., Tsubio, A., Hama, H. & Iwata, T. (1981). On the relation between insecticide resistance and aliesterase activity in the green rice leafhopper Nephotettix cincticeps Uhler (Hemiptera: Deltocephalidae). Japanese Journal of Applied Entomology and Zoology 25, 150–5.CrossRefGoogle Scholar
Nie, N. H. (1983). SPSS-X Users Guide. New York: McGraw Hill.Google Scholar
Ogilvie, B. M., Rothwell, T. L. W., Bremner, K. C., Schnitzerling, H. J., Nolan, J. & Keith, R. K. (1973). Acetylcholinesterase secretion by parasitic nematodes. I. Evidence for secretion of the enzyme by a number of species. International Journal for Parasitology 3, 589–97.CrossRefGoogle ScholarPubMed
Roos, M. H. (1990). The molecular nature of benzimidazole resistance in helminths. Parasitology Today 6, 125–7.CrossRefGoogle ScholarPubMed
Roslavtseva, S. A. (1982). The role of esterase barriers in mechanisms of resistance of houseflies to organophosphate insecticides. In Ustoichivost Vreditelei k Khimicheskim Sredstvam Zashchity Rastonii (ed. Zil Bermits, I. V., Smirnova, A. A. & Matov, G. N.), English abstract pp. 89–96.Moscow.Google Scholar
Sanderson, B. E. & Ogilvie, B. M. (1971). A Study of acetylcholinesterase throughout the life-cycle of Nippostrongylus brasiliensis. Parasitology 62, 367–73.CrossRefGoogle ScholarPubMed
Sutherland, I. A. & Lee, D. L. (1990). A larval paralysis assay for the detection of thiabendazole resistance in trichostrongyles. Parasitology 100, 131–5.CrossRefGoogle ScholarPubMed
Sutherland, I. A., Lee, D. L. & Lewis, D. (1988). Detection of benzimidazole resistance in trichostrongylid nematodes. Parasitology Today 4, 22–4.CrossRefGoogle ScholarPubMed
Sutherland, I. A., Lee, D. L. & Lewis, D. (1989). Colorimetric assay for the detection of benzimidazole resistance in trichostrongyles. Research in Veterinary Science 46, 363–6.CrossRefGoogle ScholarPubMed
Waller, P. J. (1985). Resistance to anthelmintics and the implications for animal production. In Resistance in Netnatodes to Anthelmintic Drugs (ed. Anderson, N. & Waller, P. J.), pp. 1–13. Glebe, N.S.W. 2037: C.S.I.R.O./Australian Wool Corporation.Google Scholar
Waller, P. J. (1990). Resistance in nematode parasites of livestock to the benzimidazole anthelmintics. Parasitology Today 6, 127–9.CrossRefGoogle Scholar
Yeoh, C. L., Kuwano, E. & Eto, M. (1981). Studies on the mechanisms of organophosphate resistance in oriental houseflies, Musca domestica vicina Macquart (Diptera: Muscidae). Applied Entomology and Zoology 16, 247–57.CrossRefGoogle Scholar