[en] Glutathione S-transferases (GST) play an important role in the detoxification of many substances including organic pollutants and plant secondary metabolites. We compared the GST of two syrphid species, the aphidophagous Syrphus ribesii and the saprophagous Myathropa florea to assess the relation between feeding type and GST patterns. Differences between the GST of the hoverfly species were observed after purification by affinity chromatography, SDS-PAGE and kinetic studies. While the specific activities of the purified enzymes were different, the purification yields were similar. The variation in specific activities was related to the presence of different isoenzymes in both syrphid species by SDS-PAGE. While two bands of 24 and 32 kDa were observed for M. florea, one more band of 26 kDa was present in S. ribesii. When a range of substrate and glutathione concentrations was tested, differences in Km and Vmax between the glutathione S-transferases from both hoverfly species were also observed. These results are discussed in terms of adaptations to the feeding habit and the habitat of the two syrphid species.
Boyland E., Chasseaud L.E. The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis. Adv. Enzymol. 32:1969;173.
Clark A.G., Shamaan N.A. Evidence that DDT-dehydrochlorinase from the house fly is a glutathione S-transferase. Pest. Biochem. Physiol. 22:1984;249-261.
Clark A.G., Shamaan N.A., Dauterman W.C., Hayaoka T. Characterization of multiple glutathione S-transferases from the housefly, Musca domestica (L). Pest. Biochem. Physiol. 22:1984;51-59.
Clark A.G., Shamaan N.A., Sinclair M.D., Dauterman W.C. Insecticide metabolism by multiple glutathione S-transferases in two strains of the housefly, Musca domestica (L). Pest. Biochem. Physiol. 25:1986;1969.
Dobler S. Evolutionary aspects of defense by recycled plant compounds in herbivorous insects. Basic Appl. Ecol. 2:2001;15-26.
Emrich B.H. Erworbene Toxizität bei der Lupinenblattlaus Macrosiphum albifrons und ihr Einfluss auf die aphidophagen Prädatoren Coccinella septempunctata, Episyrphus balteatus und Chrysoperla carnea. Zeit. Pflanzenk. Pflanzen. 98:1991;398-404.
Fournier D., Bride J.M., Poirie M., Bergé J.B., Plapp F. Glutathione S-transferase. Biochemical characteristics of major form from houseflies susceptible and resistant to insecticides. J. Biol. Chem. 267:1992;1840-1845.
Francis, F., 1999. Conséquences évolutives des relations entre le puceron et son prédateur en présence de substances allélochimiques chez les Brassicaceae. 5ème Conférence Internationale sur les ravageurs en agriculture, Montpellier, France, ANPP.
Francis F., Broon D., Haubruge E. Studies of the glutathione S-transferases activities and their localisation in Adalia bipunctata (Coleoptera: Coccinellidae). Med. Fac. Landbouww. Univ. Gent. 64/3a:1999;349-355.
Francis F., Haubruge E., Gaspar C. Influence of host plants on specialist/generalists aphids and on the development of Adalia bipunctata (Coleoptera: Coccinellidae). Eur. J. Entomol. 97:2000;481-485.
Francis F., Lognay G., Wathelet J.P., Haubruge E. Effects of allelochemicals from first (Brassicaceae) and second (Myzus persicae and Brevicoryne brassicae) trophic levels on Adalia bipunctata. J. Chem. Ecol. 27:2001;243-256.
Francis F., Haubruge E., Dierickx P. Glutathione S-transferase isoenzymes in the two-spot ladybird, Adalia bipunctata (Coleoptera: Coccinellidae). Arch. Insect Biochem. Physiol. 49:2002;158-166.
Gilbert F.S. Hoverflies. 1986;Cambridge University Press, Cambridge.
Grant D.F., Matsumura F. Glutathione S-transferase 1 and 2 in susceptible and insecticide resistant Aedes aegypti. Pest. Biochem. Physiol. 33:1989;132-143.
Habig W.H., Pabst M.J., Jakoby W.B. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:1974;30-71.
Hemingway J., Miyamoto J., Herath P.R.J. A possible novel link between organophosphorous and DDT insecticide resistance genes in Anopheles supporting evidence from fenitrothion metabolism studies. Pest. Biochem. Physiol. 39:1991;49-56.
Kostaropoulos I., Mantzari A.E., Papadopoulos A.I. Alterations of some glutathione S-transferase characteristics during the development of Tenebrio molitor (Insecta: Coleoptera). Insect Biochem. Mol. Biol. 26:1996;963-969.
Kostaropoulos I., Papadopoulos A.I., Metaxakis A., Boukouvala E., Papadopoulos-Mourkidou E. Glutathione S-transferase in defence against pyretroids in insects. Insect Biochem. Mol. Biol. 31:2001;313-319.
Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
Prapanthadara L., Koottathep S., Promtet N., Hemingway J., Ketterman A.J. Purification and characterization of a major glutathione S-transferase from the mosquito Anopheles dirus (Species B). Insect Biochem. Mol. Biol. 26:1996;277-285.
Ranson H., Prapanthadara L.A., Hemingway J. Cloning and characterisation of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae. Biochem. J. 324:1997;97-102.
Vanhaelen N., Haubruge E., Lognay G., Francis F. Hoverfly glutathione S-transferases and effect of Brassicaceae secondary metabolites. Pest. Biochem. Physiol. 71:2001;170-177.
Vanhaelen N., Gaspar C., Francis F. Influence of prey host plant on a generalist aphidophagous predator: Episyrphus balteatus (Diptera: Syrphidae). Eur. J. Entomol. 99:2002;561-564.
Vontas J.G., Small G.J., Nikou D.C., Ranson H., Hemingway J. Purification, molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from rice brown planthopper, Nilaparvata lugens. Biochem. J. 362:2002;329-337.
Yu S.J. Host plant induction of glutathione S-transferases in the fall armyworm. Pest. Biochem. Physiol. 17:1982;59-66.
Yu S.J. Purification and characterization of glutathione S-transferases from five Phytophagous Lepidoptera. Pest. Biochem. Physiol. 35:1989;97-105.
Yu S.J. Substrate specificity of glutathione S-transferases from the fall armyworm. Pest. Biochem. Physiol. 74:2002;41-51.