Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina

Campbell, Peter M.; Newcomb, Richard D.; Russell, Robyn J.; Oakeshott, John G.

doi:10.1016/s0965-1748(97)00109-4

Cited by 138 publications

(145 citation statements)

References 27 publications

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“…Nor have any of the resistances reviewed here been subject to any of the detailed toxicological analyses that have been done on, for example OP resistance in the higher Diptera. 93,127) With so little biochemical data available, it is not possible at this stage to ascertain the relative importance of hydrolysis and sequestration to the various resistances seen.…”

Section: Discussionmentioning

confidence: 99%

Esterase-based metabolic resistance to insecticides in heliothine and spodopteran pests

Farnsworth

Teese

Yuan

et al. 2010

Journal of Pesticide Science

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IntroductionCarboxylesterases have been implicated in metabolic resistance to several classes of insecticide in a wide variety of pest insect species. [1][2][3] The classes most commonly involved are synthetic pyrethroids (SPs) and organophosphates (OPs), and carbamates (CBs) are also involved in several cases. There are also occasional reports of carboxylesterase phenotypes associated with resistance to benzoylureas, the oxadiazine indoxacarb, the diacylhydrazine tebufenozide, the organochlorine endosulfan and the proteinaceous Cry1Ac toxin of Bacillus thuringiensis that is expressed in transgenic crops. Figure 1 gives structures for some key compounds among these various classes of insecticide.It might be expected that carboxylesterases would be involved in SP resistance because the great majority of SPs are carboxylesters. However, no precise molecular mechanisms for esterase-based SP resistance have yet been elucidated in any insect. OPs are generally phosphotriesters rather than carboxylesters but nevertheless they bind many carboxylesterases with high affinity and this provides a basis for two forms of resistance, both now elucidated at a molecular level in several species. One form involves substantial overexpression of the esterase, allowing for effective sequestration of the insecticide. The other involves specific mutations in the active site of the enzyme which convert it to an OP hydrolase (the so-called "mutant ali-esterase" mechanism). CBs are carbamic acid (NH 2 COOH) derivatives, in which a functional group has been added as an ester; these esters are chemically similar to carboxylesters. Carbamates bind carboxylesterases with quite high affinity, but as yet the molecular mechanisms by which a (mutant) carboxylesterase confers CB resistance have not been elucidated in any species. Of the other insecticide classes occasionally linked to esterase-based resistance only indoxacarb has ester bonds (two Elevated esterase activities and increased band intensities of multiple esterase isozymes after electrophoresis are commonly associated with resistance to organophosphate, pyrethroid and carbamate insecticides in various heliothine and spodopteran pests. One possible explanation for this involves a 'master regulator' mutation in a more general chemical stress response. An association between elevated esterase activities and isozyme intensities has also been reported for resistance to the Cry1Ac toxin of Helicoverpa armigera. The basis for this is unclear albeit some involvement of esterases could be mediated by the toxin's affinity for N-acetyl galactosamine glycans on certain gut-expressed esterases in this species.

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Section: Discussionmentioning

confidence: 99%

Esterase-based metabolic resistance to insecticides in heliothine and spodopteran pests

Farnsworth

Teese

Yuan

et al. 2010

Journal of Pesticide Science

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“…This latter conclusion is reinforced by two facts: the presence, in C. hominivorax samples from South America, of another mutation in the E3 esterase (G137D) (de Carvalho et al, 2006), also associated with OP resistance, and the absence of mutations, associated with OP resistance, in the acetylcholinesterase gene in almost all samples of the same localities investigated herein, with only two mutant individuals found in Pinheiro Machado (Brazil) (Silva NM, Carvalho RA, Azeredo-Espin AML, unpublished results). Since these same amino acid substitutions are also found in the E3 orthologous genes of L. cuprina and M. domestica (Campbell et al, 1998;Taskin and Kence, 2004), this indicates that these mutations may be a common mechanism of resistance, at least, in the order Diptera.…”

Section: Resultsmentioning

confidence: 67%

“…All mutant individuals showed the same substitution (guanine to cytosine in the second position), causing a change of tryptophan (W) to serine (S) in the respective codon. Mutations of tryptophan to leucine or serine in this residue, related to OP resistance, especially malathion, are well characterized in L. cuprina (Campbell et al, 1998) and M. domestica (Taskin and Kence, 2004), respectively.…”

Section: Resultsmentioning

confidence: 99%

“…Carboxylesterase E3 variants from resistant strains of the sheep blowfly Lucilia cuprina (Calliphoridae) have shown a substitution of glycine to aspartate at residue 137 (G137D), which enhances OP hydrolase activity, mainly for diethyl-OP. Substitution of tryptophan by leucine or serine at residue 251 (W251L or W251S) also confers resistance to OP, mainly dimethyl-OP (Campbell et al, 1998 lanogaster, produced by in vitro mutagenesis, also confer pyrethroid-hydrolyzing capacity (Heidari et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Investigation of mutations associated with pyrethroid resistance in populations of the New World Screwworm fly, Cochliomyia hominivorax (Diptera: Calliphoridae)

Silva¹,

Azeredo-Espin²

2009

Genet. Mol. Res.

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ABSTRACT. Cochliomyia hominivorax larvae are known for their parasitic habit in living vertebrates, causing considerable economic losses to livestock industry. This ectoparasite has been controlled mainly by applying insecticides, but this method usually results in the selection of resistant individuals. The resistance mechanism known as knockdown resistance (kdr) is a generic term for amino acid substitutions in the sodium channel associated with pyrethroid resistance, and substitutions in residue 251 of the carboxylesterase E3 have been associated with organophosphate and pyrethroid hydrolysis. We looked for L1014F kdr and W251S mutations in the sodium channel and E3 genes, respectively, in C. hominivorax populations. Ten populations obtained from its current distribution were investigated using the polymerase chain reaction-restriction fragment length polymorphism technique. No mutant individuals were found for the kdr mutation. However, the W251S mutation was found in all populations investigated. Results from This correlation was not significant at the highest concentration tested (P = 0.221). We suggest that the W251S mutation in the C. hominivorax carboxylesterase E3 is also associated with pyrethroid hydrolysis. This information may contribute to the elaboration of improved management programs for this ectoparasite.

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“…Resistance to diazinon and malathion is primarily due to two point mutations (Gly137Asp and Trp251Leu) in a carboxylesterase gene (LcE7), encoding both OP hydrolase and malathion carboxylesterase (MCE) activities (Campbell et al, 1997;Campbell et al, 1998).…”

Section: Esterase Gene In the Sheep Blow Fly Lucilia Cuprinamentioning

confidence: 99%

Gene Duplication in Insecticide Resistance

Lee¹,

Kwon²

2011

Gene Duplication

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Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina

Cited by 138 publications

References 27 publications

Esterase-based metabolic resistance to insecticides in heliothine and spodopteran pests

Esterase-based metabolic resistance to insecticides in heliothine and spodopteran pests

Investigation of mutations associated with pyrethroid resistance in populations of the New World Screwworm fly, Cochliomyia hominivorax (Diptera: Calliphoridae)

Gene Duplication in Insecticide Resistance

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