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Multiple mechanisms responsible for differential susceptibilities of Sitobion avenae (Fabricius) and Rhopalosiphum padi (Linnaeus) to pirimicarb

Published online by Cambridge University Press:  05 May 2009

Y. Lu  and
X. Gao
Y. Lu*
Affiliation:
Department of Entomology, China Agricultural University, Beijing 100193, China
X. Gao*
Affiliation:
Department of Entomology, China Agricultural University, Beijing 100193, China
*
*Author for correspondence Fax: +86-1-62732974 E-mail: gaoxiwu@263.net.cn
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Abstract

Both Sitobion avenae (Fabricius) and Rhopalosiphum padi (Linnaeus) are the most important pests of wheat in China and usually coexist on the late period of wheat growth. Pirimicarb was introduced into China for wheat aphid control in early 1990s, and differential susceptibilities of Sitobion avenae (Fabricius) and Rhopalosiphum padi (Linnaeus) to pirimicarb have been observed. A bioassay exhibited that Rhopalosiphum padi possessed significantly higher susceptibility to pirimicarb than Sitobion avenae. The addition of synergists DEF, an esterase inhibitor, PBO, a cytochrome P450 monooxygenase inhibitor, and DEM, a glutathione S-transferase inhibitor, resulted in apparent reductions in the differential susceptibilities, suggesting the involvement of the above three detoxification enzymes in the differential susceptibility to pirimicarb between Sitobion avenae and Rhopalosiphum padi. A biochemical analysis showed that the activities of carboxylesterases and glutathione S-transferases were significantly higher in Sitobion avenae than in Rhopalosiphum padi, consistent with the results of synergism. Acetylcholinesterase is the target enzyme of pirimicarb and the sensitivity of acetylcholinesterase to pirimicarb was significantly higher in Rhopalosiphum padi than in Sitobion avenae. The combined results suggest that multiple mechanisms are likely to be responsible for differential susceptibilities to pirimicarb between Sitobion avenae and Rhopalosiphum padi. The results obtained from this study should be helpful in the rational applications of insecticides.

Keywords

Differential susceptibilitySitobion avenaeRhopalosiphum padiacetylcholinesterasecarboxylesteraseglutathione S-transferase
Type
Research Paper
Information
Bulletin of Entomological Research , Volume 99 , Issue 6 , December 2009 , pp. 611 - 617
Copyright
Copyright © Cambridge University Press 2009

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References

Andrews, M.C., Callaghant, A., Field, L.M., Williamson, M.S. & Moores, G.D. (2004) Identification of mutations conferring insecticide-insensitive AChE in the cotton-melon aphid, Aphis gossypii Glover. Insect Molecular Biology 13, 555–561.CrossRefGoogle ScholarPubMed
Bingham, G., Gunning, R.V., Delogu, G., Borzatta, V., Field, L. & Moores, G.D. (2008) Temporal synergism can enhance carbamate and neonicotinoid insecticidal activity against resistant crop pests. Pest Management Science 64, 81–85.CrossRefGoogle ScholarPubMed
Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of proteindye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle Scholar
Chen, M.H., Han, Z.J., Qiao, X.F. & Qu, M.J. (2007) Resistance mechanisms and associated mutations in acetylcholinesterase genes in Sitobion avenae (Fabricius). Pesticide Biochemistry and Physiology 87, 189–195.CrossRefGoogle Scholar
Ellman, G.L., Courtey, D., Andres, V. & Featherstone, R.M. (1961) A new and rapid colorimetric determination of acetylcholinesterease activity. Biochemical Pharmacology 7, 88–95.CrossRefGoogle Scholar
Gao, J.R. & Zhu, K.Y. (2001) An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics. Insect Biochemistry and Molecular Biology 31, 1095–1104.CrossRefGoogle ScholarPubMed
Gao, J.R. & Zhu, K.Y. (2002) Increased expression of an acetylcholinesterase gene may confer organophosphate resistance in the greenbug, Schizaphis graminun (Homoptera: Aphididae). Pesticide Biochemistry and Physiology 73, 164–173.CrossRefGoogle Scholar
Gao, X.W. (1987) Introduction of Ellman procedure for assay of cholinesterases in crude enzymatic preparations modified by Gorun. Chinese Bulletin of Entomology 33, 245–246.Google Scholar
Gao, X.W. & Zheng, B.Z. (1989) Study on selective mechanism of pirimicarb to Aphis gossypii and Myzus persicae. Agrochemicals 28, 1–2.Google Scholar
Gao, X.W., Wang, Z.G. & Zheng, B.Z. (1990) Selective toxicity of six common insecticides to eight species of aphids. Acta Entomologica Sinica 41, 274–279.Google Scholar
Gao, X.W., Liu, W., Zhao, G.Y. & Zheng, B.Z. (1991) Study on selective mechanism of pirimicarb to Coccinella septempunctata and Sitobion avenae. Agrochemicals 30, 40–41.Google Scholar
Guedes, R.N.C., Zhu, K.Y., Kambhampati, S. & Dover, B.A. (1997) An altered acetylcholinesterase conferring negative cross-insensitivity to different insecticidal inhibitors in organophosphate-resistant lesser grain borer, Rhyzopertha dominica. Pesticide Biochemistry and Physiology 58, 55–62.CrossRefGoogle Scholar
Gunning, R.V., Moores, G.D. & Devonshire, A.L. (1999) Esterase inhibitors synergise the toxicity of pyrethroids in Australian Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae). Pesticide Biochemistry and Physiology 63, 50–62.CrossRefGoogle Scholar
Habig, W.H., Pabst, J. & Jackoby, W.B. (1974) Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry 249, 7130–7139.CrossRefGoogle ScholarPubMed
Hama, H., Miyata, T. & Saito, T. (1980) Some properties of acetylcholinesterase partially purified from susceptible and resistance green rice leafhopper, Nephotettix cincticeps (Uhler) (Hemoptera: Deltocephalidae). Applied Entomology Zoology 15, 249–256.CrossRefGoogle Scholar
Jutsum, A.R., Franz, J.M., Deacon, J.W., Payne, C.C., Lewis, T., Paterson, R.R.M., Waage, J.K. & van Emden, H.F. (1988) Commercial application of biological control: status and prospects. Philosophical Transactions of the Royal Society of London, Series B 318, 357–373.Google Scholar
Liu, A.Z., Ru, T.Q., Wang, X.J. & Li, S.G. (2001) Susceptibity of both aphid species to some insecticides. Plant Protection 39, 20–21.Google Scholar
Liu, N.N. & Yue, X. (2000) Insecticide Resistance and Cross-Resistance in the House Fly (Diptera: Muscidae). Journal of Economic Entomology 93, 1269–1275.CrossRefGoogle ScholarPubMed
Lu, Y.H. & Gao, X.W. (2007) A method for mass culture of wheat aphids. Chinese Bulletin of Entomology 44, 289–290.Google Scholar
Mohammadi, S.M., Hejazi, M.J., Mohammadi, A. & Rashidi, M.R. (2007) Resistance status of the Colorado potato beetle, Leptinotarsa decemlineata, to endosulfan in East Azarbaijan and Ardabil provinces of Iran. Journal of Insect Science 7(31) 7 pp. Available online at http://insectscience.org/7.31/.Google Scholar
Moores, G.D., Devine, G.J. & Devonshire, A.L. (1994) Insecticide-insensitive acetylcholinesterase can enhance esterase-based resistance in Myzus persicae and Myzus nicotianae. Pesticide Biochemistry and Physiology 49, 114–120.CrossRefGoogle Scholar
Moores, G.D., Gao, X.W., Denholm, I. & Devonshire, A.L. (1996) Characterization of insensitive acetylcholinesterase in the insecticide-resistance cotton aphid, Aphis gossypii Glover (Homoperta:Aphidedae). Pesticide Biochemistry and Physiology 56, 102–110.CrossRefGoogle Scholar
Scott, J.G., Foroozesh, M., Hopkins, N.E., Alefantis, T.G. & Alworth, W.L. (2000) Inhibition of cytochrome P450 6D1 by alkynylarenes, methylenedioxyarenes, and other substituted aromatics. Pesticide Biochemistry and Physiology 67, 63–71.CrossRefGoogle Scholar
Shotkoski, F.A., Mayo, Z.B. & Peters, L.L. (1990) Induced disulfoton resistance in greenbugs (Homoptera: Aphididae). Journal of Economic Entomology 83, 2147–2152.CrossRefGoogle Scholar
Shufran, R.A., Wilde, G.E. & Sloderbeck, P.E. (1997) Response of three greenbugs (Homoptera: Aphididae) strains to five organophosphorous and two carbamate insecticides. Journal of Economic Entomology 90, 283–286.CrossRefGoogle Scholar
van Asperen, K. (1962) A study of housefly esterases by means of a sensitive colorimetric method. Journal of Insect Physiology 8, 401–416.CrossRefGoogle Scholar
Yang, X.M., Zhu, K.Y., Buschman, L.L. & Margolies, D.C. (2001) Comparative susceptibility and possible detoxification mechanisms for selected miticides in Banks grass mite and two-spotted spider mite (Acari: Tetranychidae). Experimental and Applied Acarology 25, 293–299.CrossRefGoogle Scholar
Young, S.J., Gunning, R.V. & Moores, G.D. (2005) The effect of piperonyl butoxide on pyrethroid-resistance-associated esterases in Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae). Pest Management Science 61, 397–401.CrossRefGoogle ScholarPubMed
Young, S.J., Gunning, R.V. & Moores, G.D. (2006) Effect of pretreatment with piperonyl butoxide on pyrethroid efficacy against insecticide resistant Helicoverpa armigera (Lepidoptera: Noctuidae) and Bemisia tabaci (Sternorrhyncha: Aleyrodidae). Pest Management Science 62, 114–119.CrossRefGoogle ScholarPubMed
Zhu, K.Y. & He, F.Q. (2000) Elevated esterase exhibiting arylesterase-like characteristics in an organophosphate-resistant clone of the greenbug, Schizaphis graminum (Rondani) (Homoptera: Aphididae). Pesticide Biochemistry and Physiology 67, 155–167.CrossRefGoogle Scholar
Zhu, K.Y., Gao, J.R. & Starkey, S.R. (2000) Organophosphate resistance mediated by alterations of acetylcholinesterase in a resistant clone of the greenbug, Schizaphis graminun (Homoptera: Aphididae). Pesticide Biochemistry and Physiology 68, 138–147.CrossRefGoogle Scholar