Mini reviewThe molecular basis of two contrasting metabolic mechanisms of insecticide resistance
Introduction
Resistance to organochlorine, organophosphate and carbamate insecticides is conferred by a limited number of mechanisms in all insects analysed to date. These mechanisms predominantly involve either metabolic detoxification of the insecticide before it reaches its target site, or changes in sensitivity of the target site so that it is no longer susceptible to insecticide inhibition. The most common metabolic resistance mechanisms involve esterases, glutathione S-transferases or monooxygenases (the latter has been the subject of a recent review by Scott et al., 1998). In most, but not all, instances of metabolic resistance, individual resistant insects can be detected through increased quantities of enzyme compared to their susceptible counterparts (Brown and Brogdon, 1987, Hemingway, 1989, Hemingway et al., 1995). Over the last decade the molecular basis of these resistance mechanisms has gradually been elucidated, opening up the exciting possibility of manipulation of these enzyme systems in the long term to restore insecticide susceptibility by manipulation of their expression patterns. The esterase and glutathione S-transferase (GST)-based insecticide resistance mechanisms in a range of insects present a number of contrasting ways in which metabolically-based resistance has been selected for at the molecular level.
Section snippets
Esterase-based resistance
Esterase-based resistance to organophosphorus and carbamate insecticides is common in a range of different insect pests (Field et al., 1988, Hemingway and Karunaratne, 1998). The esterases either produce broad spectrum insecticide resistance through rapid-binding and slow turnover of insecticide, i.e. sequestration, or narrow spectrum resistance through metabolism of a very restricted range of insecticides containing a common ester bond (Herath et al., 1987, Karunaratne et al., 1995). The
GST-based resistance
The glutathione S-transferases (GSTs) belong to a superfamily which currently has almost 100 sequences. There are at least 25 groups (families) of GST-like proteins, with one well supported large clade containing currently recognised mammalian, arthropod, helminth, nematode and mollusc GST classes (Snyder and Maddison, 1997). GSTs can produce resistance to a range of insecticides by conjugating reduced glutathione (GSH) to the insecticide or its primary toxic metabolic products. The majority of
Conclusions
The last decade has seen large advances in our understanding of the molecular basis of insecticide resistance. The structural genes coding for the enzymes, which are elevated in a number of insect species, have been cloned and characterized. Our understanding of how these genes are regulated will form another major advance in our understanding of such systems, moving us closer to the goal of manipulating pest insect species with the aim of restoring insecticide susceptibility.
Acknowledgements
The electron micrographs reported in this review would not have been possible without the expert technical assistance of Mrs C. Winters at the Cardiff School of Biosciences.
References (46)
- et al.
Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina
Insect Biochem. Mol. Biol.
(1998) - et al.
The same amino acid substitution in orthologous esterases confers organophosphate resistance in the housefly and a blowfly
Ins. Biochem. Mol. Biol.
(1999) - et al.
Insecticide metabolism by multiple glutathione S-transferases in two strains of the house fly, Musca domestica (L)
Pesticide Biochemistry and Physiology
(1986) - et al.
Evidence that DDT-dehydrochlorinase from the house fly is a glutathione S-transferase
Pesticide Biochemistry and Physiology
(1984) - et al.
Changes in DNA methylation are associated with loss of insecticide resistance in the peach-potato aphid Myzus persicae (Sulz)
FEBS Letters
(1989) - et al.
Glutathione S-transferase 1 and 2 in susceptible and insecticide resistant Aedes aegypti
Pesticide Biochemistry and Physiology
(1989) - et al.
A possible novel link between organophosphorus and DDT insecticide resistance genes in Anopheles: supporting evidence from fenitrothion metabolism studies
Pesticide Biochemistry and Physiology
(1991) - et al.
The detection and characterization of malathion resistance in field populations of Anopheles culicifacies B in Sri Lanka
Pesticide Biochemistry and Physiology
(1987) - et al.
Kinetic and molecular differences in the amplified and non-amplified esterases from insecticide-resistant and susceptible Culex quinquefasciatus mosquitoes
Journal of Biological Chemistry
(1995) - et al.
Interstrain comparison of glutathione-dependent reactions in susceptible and resistant houseflies
Pesticide Biochemistry and Physiology
(1975)
Genetic studies on glutathione-dependent reactions in resistant strains of the house fly, Musca domestica L
Pesticide Biochemistry and Physiology
Partial purification and characterization of glutathione S-transferase involved in DDT resistance from the mosquito Anopheles gambiae
Pesticide Biochemistry and Physiology
Cloning, expression and characterization of an insect class I glutathione S-transferase from Anopheles dirus species B
Insect Biochemistry and Molecular Biology
Insect cytochromes P450: diversity, insecticide resistance and tolerance to plant toxins
Comparative Biochemistry and Physiology C
Differential glycosylation produces heterogeneity in elevated esterases associated with insecticide resistance in the brown planthopper Nilaparvata lugens Stal
Ins. Biochem. Mol. Biol.
The glutathione S-transferase D genes: a divergently organized, intronless gene family in Drosophila melanogaster
Journal of Biological Chemistry
Mosquito carboxylesterase Estα21 (A2). Cloning and sequence of the full length cDNA for a major insecticide resistance gene worldwide in the mosquito Culex quinquefasciatus
Journal of Biological Chemistry
Serum esterases. 1. Two types of esterases (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination
Biochemical Journal
The Drosophila ZESTE protein binds co-operatively to sites in many gene regulatory regions — implications for transvection and gene regulation
Embo Journal
Variation in the chromosomal distribution of amplified esterase (FE4) genes in Greek field populations of Myzus persicae (Sulzer)
Heredity
Improved detection of insecticide resistance through conventional and molecular techniques
Annual Review of Entomology
The evolution of insecticide resistance in the peach-potato aphid, Myzus persicae
Phil. Trans. Roy. Soc. B
Insect P450 enzymes
Ann. Rev. Ent.
Cited by (251)
The effect of chlorogenic acid, a potential botanical insecticide, on gene transcription and protein expression of carboxylesterases in the armyworm (Mythimna separata)
2023, Pesticide Biochemistry and PhysiologyTranscriptomic and physiological analysis of the effect of octanoic acid on Meloidogyne incognita
2023, Pesticide Biochemistry and PhysiologyBiochemical and molecular diagnosis of different tomato cultivars susceptible and resistant to Tuta absoluta (Meyrick) infestation: Biochemical and molecular diagnosis of different tomato cultivars susceptible and resistant to Tuta absoluta
2022, Saudi Journal of Biological SciencesCitation Excerpt :These results were indicated by the electrophoretic results (native- PAGE). These results are agreement with (Devonshire et al., 1993; Hemingway, 2000; Saad et al., 2021d), who reported that overexpression of PODs enzymes through gene amplification in Myzus persicae. Various natural compounds can be used to enhance tomato resistance against Tuta absoluta, these compounds such as bioactive peptides which El-Saadony et al., (2021a, b) reported their activities, additionally, essential oils (El-Tarabily et al., 2021; Abd El-Hack et al., 2021a, b; Alagawany et al., 2021).