The acetylcholinesterase gene and organophosphorus resistance in the Australian sheep blowfly, Lucilia cuprina

Chen, Zhenzhong; Newcomb, Richard D.; Forbes, Emma; McKenzie, John A.; Batterham, Philip

doi:10.1016/s0965-1748(00)00186-7

Cited by 115 publications

(73 citation statements)

References 44 publications

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“…virescens 11,12) but its high K m for OPs (Ͼ700 mM, c.f. Ͻ Ͻ1 mM for the dipteran esterases that confer OP resistance 13,14) ) casts doubt on its physiological relevance. And there are at least two genetic mechanisms by which detoxifying enzymes not causally involved in a particular resistance could nevertheless show an association with resistance.…”

Section: Heliothine Resistance To Opsmentioning

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: Heliothine Resistance To Opsmentioning

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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“…An insect AChE gene (Ace) was first analyzed from Drosophila melanogaster (Hall and Spierer, 1986) and several amino acid substitutions conferring insecticide insensitivity were first identified from this species (Mutero et al, 1994). Subsequently, amino acid substitutions were identified in the Cyclorrhapha fly species, Musca domestica (Huang et al, 1997;Kozaki et al, 2001;Walsh et al, 2001), Lucilia cuprina (Chen et al, 2001), and Bactrocera oleae (Vontas et al, 2002); however, no insecticide insensitivity-attributable mutation was found in Ace orthologues of the resistant strains of other insect species such as Culex pipiens (Malcolm et al, 1998), Cx. tritaeniorhynchus (Mori et al, 2001), Nephotettix cincticeps (Tomita et al, 2000) and Plutella xylostella (Ni et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Differential tissue distribution of two acetylcholinesterase transcripts in the German cockroach, Blattella germanica

Mizuno

Komagata

et al. 2007

Appl. Entomol. Zool.

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Recent studies have revealed that non-Cyclorrhapha insects possess two acetylcholinesterases (AChEs): Drosophila Ace-orthologous (o-Ace) and -paralogous (p-Ace) forms. In these insects, p-Ace is considered as a neural target of insecticides because mutations conferring insecticide insensitivity have been consistently identified in equivalent forms from various insects. To clarify the functional differentiation between the two AChE isoforms, we characterized the expression of two AChE genes in nerve cell-rich and -poor tissues of German cockroaches. The two AChE genes were expressed at comparable levels in both the nerve cord and head. Two AChE isoforms with mutually discriminatory fenitroxon sensitivities were exhibited in the nerve cord, indicating that o-Ace and p-Ace function in the neurons. pAce was mainly expressed in the nerve cord and head, while o-Ace was ubiquitously expressed at a comparable level. Moreover, o-Ace transcripts as well as AChE activity were detected in the fat body where no nervous tissue is observed. No AChE activity was detected in the hemolymph. These results show that p-Ace is better as an insecticidal target because of its abundant transcripts in nervous tissue. In addition, the roles of o-Ace, which is present ubiquitously without secretion into the hemolymph in insects, are discussed.

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“…The G353A mutation was also found in AChE from the fruit fly (G324A) (7), the house fly (G262A) (8), Lucilia cuprina (G303A) (11), and Plutella xylostella AChE1 (G324A) (12). Initial modeling of these mutations within the Drosophila structure revealed that G324A is located close to the active-site triad at the base of the gorge, with G324A likely to interact with gorge residues, which affects the orientation of the catalytic serine (ser-200 in Torpedo) and possibly plays a role in influencing inhibitor sensitivity (13,14).…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization and inhibition analysis of the acetylcholinesterase gene from the silkworm maggot, Exorista sorbillans

Lang¹,

Zhang²,

Li³

et al. 2010

BMB Reports

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The acetylcholinesterase gene and organophosphorus resistance in the Australian sheep blowfly, Lucilia cuprina

Cited by 115 publications

References 44 publications

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

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

Differential tissue distribution of two acetylcholinesterase transcripts in the German cockroach, Blattella germanica

Molecular characterization and inhibition analysis of the acetylcholinesterase gene from the silkworm maggot, Exorista sorbillans

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