Glutathione S–transferase in the defence against pyrethroids in insects

Kostaropoulos, Iason; Papadopoulos, Andrew; Metaxakis, Athanasios; Boukouvala, Evridiki; Papadopoulou‐Mourkidou, Euphemia

doi:10.1016/s0965-1748(00)00123-5

Cited by 266 publications

(187 citation statements)

References 23 publications

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“…The two isoforms present in both species are certainly responsible for the detoxification of common xenobiotics while the isoform only present in the aphidophagous species are probably an adaptation to cope with chemicals specific to its environment and prey. The compounds frequently encountered by S. ribesii include pesticides that are known to induce GST activity (Clark et al, 1986;Hemingway et al, 1991;Kostaropoulos et al, 2001). Other compounds that this species has to face are plant allelochemicals.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of glutathione S-transferases from two syrphid flies (Syrphus ribesii and Myathropa florae)

Vanhaelen

Francis

Haubruge

2004

Comparative Biochemistry and Physiology Part B: Biochemistry an

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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 K and V between the m max 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. ᮊ

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of glutathione S-transferases from two syrphid flies (Syrphus ribesii and Myathropa florae)

Vanhaelen

Francis

Haubruge

2004

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…Aphidophagous species tested are frequently or almost exclusively found in farmland (31). This species might thus often be exposed to pesticides, which are known to induce GST activity (32)(33)(34). Nevertheless, some habitats of saprophagous and coprophagous species might also contain organic compounds and pollutants that could necessitate strong detoxification abilities.…”

Section: Fig 4 Glutathione S-transferase Activity Of Episyrphus Balmentioning

confidence: 99%

Hoverfly Glutathione S-Transferases and Effect of Brassicaceae Secondary Metabolites

Vanhaelen¹,

Haubruge²,

Lognay

et al. 2001

Pesticide Biochemistry and Physiology

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The Episyrphus balteatus hoverfly is commonly found in very diversified biotopes including Brassicaceae crop fields. Glutathione S-transferases (GST) are detoxification enzymes that are involved in the metaboliza-tion of plant allelochemicals such as glucosinolates and related volatile products (mainly isothiocyanates) from Brassica plants. Developmental expression of E. balteatus glutathione S-transferases was studied. With regard to the high level of glutathione S-transferase activity in syrphid adults, the latter stage was also used to assess the glutathione S-transferase distribution in several parts of the insect. Higher glutathione S-transferase activities were found in the thorax (47.5 and 38.5%) followed by the abdomen (32.4 and 32.9%) and the head (20.4 and 28.5%) with l-chloro-2,4-dinitrobenzene, and 2,4-dinitro-l-iodebenzene, respectively. Analysis of Brevicoryne brassicae, the cabbage aphid, by GC-MS revealed the presence of isothiocyanates. The latter are the main degradation products of the glucosinolate from the host plant at neutral pH. Feeding the predators with this aphid species and with the generalist Myzus persicae reared on Brassica napus induced glutathione S-transferase activity. Impact of volatiles from the host plant on the glutathione S-transferase activity was also determined by exposure of syrphid larvae to isothiocyanates (allyl-and benzyl-isothiocyanates). Enzyme inductions were observed only from a 1 ppm concentration. Enzymatic activity evolution was discussed as an adaptation to cope with allelochemicals from plants. Finally, the glutathione 5-transferase activities of several hoverfly species were compared in relation to their feeding behavior (coprophagous, saprophagous, and aphidophagous) at the larval stages. The results seem to indicate quantitative and qualitative differences of glutathione S-transferases according to the feeding behavior of the larvae.

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“…GSTs confer resistance by detoxifying lipid peroxidation products induced by pyrethroids, thereby protecting tissues from oxidative damage (Vontas et al 2001), as well as by binding pyrethroid molecules in a sequestration mechanism, thereby offering passive protection (Kostaropoulos et al 2001). Recently, studies on their roles in mediating oxidative stress responses have been extensively reported (Burmeister et al 2008;Kampkotter et al 2003;Li et al 2008;Meng et al 2009;Umasuthan et al 2012;Yang et al 2012), and these studies have shown that GSTs reduce lipid hydroperoxides through a selenium-independent pathway.…”

Section: Introductionmentioning

confidence: 99%

Identification, genomic organization, and oxidative stress response of a sigma class glutathione S-transferase gene (AccGSTS1) in the honey bee, Apis cerana cerana

Yan

Jia

Gao

et al. 2013

Cell Stress and Chaperones

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Glutathione S-transferases (GSTs) are members of a multifunctional antioxidant enzyme superfamily that play pivotal roles in both detoxification and protection against oxidative damage caused by reactive oxygen species. In this study, a complementary DNA (cDNA) encoding a sigma class GST was identified in the Chinese honey bee, Apis cerana cerana (AccGSTS1). AccGSTS1 was constitutively expressed in all tissues of adult worker bees, including the brain, fat body, epidermis, muscle, and midgut, with particularly robust transcription in the fat body. Relative messenger RNA expression levels of AccGSTS1 at different developmental stages varied, with the highest levels of expression observed in adults. The potential function of AccGSTS1 in cellular defenses against abiotic stresses (cold, heat, UV, H 2 O 2 , HgCl 2 , and insecticides) was investigated. AccGSTS1 was significantly upregulated in response to all of the treatment conditions examined, although the induction levels were varied. Recombinant AccGSTS1 protein showed characteristic glutathione-conjugating catalytic activity toward 1-chloro-2,4-dinitrobenzene. Functional assays revealed that AccGSTS1 could remove H 2 O 2 , thereby protecting DNA from oxidative damage. Escherichia coli overexpressing AccGSTS1 showed long-term resistance under conditions of oxidative stress. Together, these results suggest that AccGSTS1 is a crucial antioxidant enzyme involved in cellular antioxidant defenses and honey bee survival.

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Glutathione S–transferase in the defence against pyrethroids in insects

Cited by 266 publications

References 23 publications

Purification and characterization of glutathione S-transferases from two syrphid flies (Syrphus ribesii and Myathropa florae)

Purification and characterization of glutathione S-transferases from two syrphid flies (Syrphus ribesii and Myathropa florae)

Hoverfly Glutathione S-Transferases and Effect of Brassicaceae Secondary Metabolites

Identification, genomic organization, and oxidative stress response of a sigma class glutathione S-transferase gene (AccGSTS1) in the honey bee, Apis cerana cerana

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