Selective inhibitors of methyl parathion-resistant acetylcholinesterase from Heliothis virescens

Brown, Thomas M.; Bryson, Patricia K.

doi:10.1016/0048-3575(92)90113-e

Cited by 53 publications

(27 citation statements)

References 8 publications

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“…The second approach is the reversion of resistance by designing and using compounds more toxic against resistant individuals. This strategy has been proposed for managing resistance resulting from modification of AChE, because various organophosphates and carbamates have been reported to be more potent against insensitive AChE than against the wild type (Hama and Iwata, 1978;Kyomura and Takahashi, 1979;Brown and Bryson, 1992;Zhu and Clark, 1995;Kato et al, 1999;Villatte et al, 1999). If the in vitro process indeed reflects in vivo negatively correlated cross resistance, it may be possible to use such insecticides in resistance management programs.…”

Section: Discussionmentioning

confidence: 99%

Studies on pirimicarb resistance mechanisms in Iranian populations of the peach-potato aphid, Myzus persicae

Ghadamyari

Mizuno

et al. 2008

Appl. Entomol. Zool.

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Mechanisms of resistance to pirimicarb were surveyed in Iranian populations of the peach-potato aphid, Myzus persicae. Insecticide bioassays were carried out using topical application on three different populations collected from Karaj and Rasht in the Northern provinces. Results of the bioassays indicated that Rasht and Karaj-S populations were susceptible to pirimicarb. A population collected from the college greenhouse (Karaj-R) was resistant to pirimicarb. LD 50 (Ͼ100 ng/insect) of pirimicarb was not calculated for the Karaj-R population due to limited solubility of this insecticide. The activity and PAGE patterns of esterase in resistant (Karaj-R) and susceptible populations showed that one mechanism of resistance to pirimicarb was esterase-based resistance. Esterase activity of the Karaj-R population was 3.25-fold higher than the susceptible population (Karaj-S), and one of the two esterase bands with higher activity in the Karaj-R population showed strong susceptibility to pirimicarb. The acetylcholinesterase (AChE) of the Karaj-R population had lower affinity to artificial substrates, acetylthiocholine, propionylthiocholine and butyrylthiocholine, than Rasht and Karaj-S populations. The I 50 of pirimicarb for Karaj-R, Karaj-S and Rasht populations was 1.89ϫ 10 Ϫ5 M, 1.37ϫ10 Ϫ8 M and 1.37ϫ10 Ϫ8 M, respectively. These results suggest that AChE of the Karaj-R population is insensitive to pirimicarb. Ratios of AChE insensitivity of the Karaj-R population to the Karaj-S population were 1,384.6, 11.8 and 2.7 for pirimicarb, monocrotophos and aldicarb, respectively; however, the ratios were 0.32, 0.15 and 0.10 for carbofuran, propoxure and MTMC, respectively, showing negatively correlated sensitivity to pirimicarbinsensitive AChE.

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Section: Discussionmentioning

confidence: 99%

Studies on pirimicarb resistance mechanisms in Iranian populations of the peach-potato aphid, Myzus persicae

Ghadamyari

Mizuno

et al. 2008

Appl. Entomol. Zool.

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“…Biochemical and pharmacological properties of AChE have been characterized in many insect species (Devonshire, 1975;Devonshire and Moores, 1994a,b;Brestkin et al, 1985Brestkin et al, , 1992Lester and Gilbert, 1987;Gnagey et al, 1987;Lenoir-Rousseaux and Gautron, 1987;Lenoir-Rousseaux et al, 1988;Brown and Bryson, 1992;Zhu and Brindley, 1992a-d;Argentine et al, 1994;Clark, 1994, 1995;Xu and Bull, 1994a,b;Pandey and Sharma, 1996;Guedes et al, 1998). Numerous studies have shown several typical features of insect AChE, including:…”

Section: Introductionmentioning

confidence: 95%

Purification and kinetic analysis of acetylcholinesterase from western corn rootworm,Diabrotica virgifera virgifera (Coleoptera: Chrysomelidae)

Gao

Rao

Wilde

et al. 1998

Arch. Insect Biochem. Physiol.

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“…Target site resistance is well documented, [32][33][34][35] but there is also at least some evidence for esterase-based metabolic resistance in both Hs. virescens and H. armigera.…”

Section: Heliothine Resistance To Cbsmentioning

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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Selective inhibitors of methyl parathion-resistant acetylcholinesterase from Heliothis virescens

Cited by 53 publications

References 8 publications

Studies on pirimicarb resistance mechanisms in Iranian populations of the peach-potato aphid, Myzus persicae

Studies on pirimicarb resistance mechanisms in Iranian populations of the peach-potato aphid, Myzus persicae

Purification and kinetic analysis of acetylcholinesterase from western corn rootworm,Diabrotica virgifera virgifera (Coleoptera: Chrysomelidae)

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

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