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The role of glutathione S-transferases in the detoxification of some organophosphorus insecticides in larvae and pupae of the yellow mealworm, Tenebrio molitor (Coleoptera: Tenebrionidae)

The correlation between the natural levels of glutathione S‐transferase (GST) and the tolerance to the organophosphorus insecticides parathion‐methyl and paraoxon‐methyl, as well as the interaction of affinity‐purified enzyme and the insecticides were investigated in order to collect further informa...

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Published in:Pest management science 2001-06, Vol.57 (6), p.501-508
Main Authors: Kostaropoulos, Iason, Papadopoulos, Athanasios I, Metaxakis, Athanasios, Boukouvala, Evridiki, Papadopoulou-Mourkidou, Euphemia
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description The correlation between the natural levels of glutathione S‐transferase (GST) and the tolerance to the organophosphorus insecticides parathion‐methyl and paraoxon‐methyl, as well as the interaction of affinity‐purified enzyme and the insecticides were investigated in order to collect further information on the role of the glutathione S‐transferase system as a mechanism of defence against insecticides in insects. The studies were carried out on the larvae and pupae of the coleopteran Tenebrio molitor L, which exhibit varying natural levels of GST activity. Stage‐dependent susceptibility of the insect against insecticides was observed during the first 24 h. However, 48 h after treatment, the KD50 value increased significantly due to the recovery of some individuals. Simultaneous injection of insecticide with compounds which inhibit GST activity in vitro caused an alteration in susceptibility of insects 24 or 48 h post‐treatment, depending on stage and insecticide used. Inhibition studies combined with competitive fluorescence spectroscopy revealed that the insecticides probably bind to the active site of the enzyme, thus inhibiting its activity towards 1‐chloro‐2,4‐dinitrobenzene in a competitive manner. High‐performance liquid chromatography and gas chromatography revealed that T molitor GST catalyses the conjugation of the insecticides studied to a reduced form of glutathione (GSH). From the above experimental results, it is considered that GST offers a protection against the organophosphorus insecticides studied by active site binding and subsequent conjugation with GSH. © 2001 Society of Chemical Industry
doi_str_mv 10.1002/ps.323
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Manag. Sci</addtitle><description>The correlation between the natural levels of glutathione S‐transferase (GST) and the tolerance to the organophosphorus insecticides parathion‐methyl and paraoxon‐methyl, as well as the interaction of affinity‐purified enzyme and the insecticides were investigated in order to collect further information on the role of the glutathione S‐transferase system as a mechanism of defence against insecticides in insects. The studies were carried out on the larvae and pupae of the coleopteran Tenebrio molitor L, which exhibit varying natural levels of GST activity. Stage‐dependent susceptibility of the insect against insecticides was observed during the first 24 h. However, 48 h after treatment, the KD50 value increased significantly due to the recovery of some individuals. 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Invertebrates</topic><topic>Pupa - enzymology</topic><topic>Pupa - growth &amp; development</topic><topic>Spectrometry, Fluorescence</topic><topic>Tenebrio - enzymology</topic><topic>Tenebrio - growth &amp; development</topic><topic>Tenebrio molitor</topic><topic>Tenebrionidae</topic><topic>transferase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kostaropoulos, Iason</creatorcontrib><creatorcontrib>Papadopoulos, Athanasios I</creatorcontrib><creatorcontrib>Metaxakis, Athanasios</creatorcontrib><creatorcontrib>Boukouvala, Evridiki</creatorcontrib><creatorcontrib>Papadopoulou-Mourkidou, Euphemia</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><jtitle>Pest management science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kostaropoulos, Iason</au><au>Papadopoulos, Athanasios I</au><au>Metaxakis, Athanasios</au><au>Boukouvala, Evridiki</au><au>Papadopoulou-Mourkidou, Euphemia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of glutathione S-transferases in the detoxification of some organophosphorus insecticides in larvae and pupae of the yellow mealworm, Tenebrio molitor (Coleoptera: Tenebrionidae)</atitle><jtitle>Pest management science</jtitle><addtitle>Pest. Manag. Sci</addtitle><date>2001-06</date><risdate>2001</risdate><volume>57</volume><issue>6</issue><spage>501</spage><epage>508</epage><pages>501-508</pages><issn>1526-498X</issn><eissn>1526-4998</eissn><coden>PMSCFC</coden><abstract>The correlation between the natural levels of glutathione S‐transferase (GST) and the tolerance to the organophosphorus insecticides parathion‐methyl and paraoxon‐methyl, as well as the interaction of affinity‐purified enzyme and the insecticides were investigated in order to collect further information on the role of the glutathione S‐transferase system as a mechanism of defence against insecticides in insects. The studies were carried out on the larvae and pupae of the coleopteran Tenebrio molitor L, which exhibit varying natural levels of GST activity. Stage‐dependent susceptibility of the insect against insecticides was observed during the first 24 h. However, 48 h after treatment, the KD50 value increased significantly due to the recovery of some individuals. Simultaneous injection of insecticide with compounds which inhibit GST activity in vitro caused an alteration in susceptibility of insects 24 or 48 h post‐treatment, depending on stage and insecticide used. Inhibition studies combined with competitive fluorescence spectroscopy revealed that the insecticides probably bind to the active site of the enzyme, thus inhibiting its activity towards 1‐chloro‐2,4‐dinitrobenzene in a competitive manner. High‐performance liquid chromatography and gas chromatography revealed that T molitor GST catalyses the conjugation of the insecticides studied to a reduced form of glutathione (GSH). From the above experimental results, it is considered that GST offers a protection against the organophosphorus insecticides studied by active site binding and subsequent conjugation with GSH. © 2001 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>11407025</pmid><doi>10.1002/ps.323</doi><tpages>8</tpages></addata></record>
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identifier ISSN: 1526-498X
ispartof Pest management science, 2001-06, Vol.57 (6), p.501-508
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source Wiley
subjects Animals
Binding Sites
Biological and medical sciences
Chemical control
Chromatography, Gas
Chromatography, High Pressure Liquid
Control
Dinitrochlorobenzene - antagonists & inhibitors
Fundamental and applied biological sciences. Psychology
glutathione S-transferases
Glutathione Transferase - chemistry
Glutathione Transferase - metabolism
inhibitors
Insecticide Resistance
Insecticides
insects
Kinetics
Larva - enzymology
Larva - growth & development
Malathion - analogs & derivatives
Methyl Parathion
organophosphates
Oxidation-Reduction
Paraoxon
Phytopathology. Animal pests. Plant and forest protection
Protozoa. Invertebrates
Pupa - enzymology
Pupa - growth & development
Spectrometry, Fluorescence
Tenebrio - enzymology
Tenebrio - growth & development
Tenebrio molitor
Tenebrionidae
transferase
title The role of glutathione S-transferases in the detoxification of some organophosphorus insecticides in larvae and pupae of the yellow mealworm, Tenebrio molitor (Coleoptera: Tenebrionidae)
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