Pyrethroid resistance and esterase activity in three strains of the cotton bollworm, Helicoverpa armigera (Hübner)

El-latif, Ashraf Oukasha Abd; Subrahmanyam, B.

doi:10.1016/j.pestbp.2009.11.004

Cited by 19 publications

(13 citation statements)

References 21 publications

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“…The association is particularly strong in data for populations from Australia, [39][40][41][42] south and southeast Asia [43][44][45][46][47][48][49][50][51] and central Africa 52,53) and is also significant in Chinese populations, 46,54,55) although it has not been found in west African populations. [56][57][58] Whether this geographic variation in the strength of the associations reflects genetic differences among populations or methodological differences among investigators is moot, although some effect of genetic differences seems likely.…”

Section: Heliothine Resistance To Spsmentioning

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 Spsmentioning

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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“…While target site insensitivity is clearly also involved, enhanced detoxification is consistently implicated in the resistance, including both oxidative and hydrolytic metabolism, mediated by cytochrome P450s (P450s) and carboxyl/cholinesterases (CCEs) respectively (McCaffery, 1998). However the relative importance of the two detoxification systems appears to vary among populations from Australia, Asia and Africa (Gunning et al, 1996(Gunning et al, , 1999Martin et al, 2002;Yang et al, 2004;Achaleke et al, 2009;Abd El-Latif and Subrahmanyam, 2009;Farnsworth et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Overexpressed esterases in a fenvalerate resistant strain of the cotton bollworm, Helicoverpa armigera

Yang

Yuan

et al. 2011

Insect Biochemistry and Molecular Biology

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“…To date, the overwhelming majority of studies of esterase contributions to xenobiotic metabolism have focused on their role in resistance to organophosphate (Srigiriraju et al, 2009;Rose et al, 2011) and other insecticides (Abd El-Latif and Subrahmanyam, 2010;Farnsworth et al, 2010;Feng et al, 2011). Contributions of esterases to host plant utilization by insect herbivores have been largely overlooked.…”

Section: Discussionmentioning

confidence: 99%

Aliphatic Esters as Targets of Esterase Activity in the Parsnip Webworm (Depressaria pastinacella)

et al. 2012

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As a specialist on the reproductive structures of Pastinaca sativa and species in the related genus Heracleum, the parsnip webworm (Depressaria pastinacella) routinely encounters a distinctive suite of phytochemicals in hostplant tissues. Little is known, however, about the detoxification mechanisms upon which this species relies to metabolize these compounds. In this study, larval guts containing hostplant tissues were homogenized, and metabolism was determined by incubating reactions with and without NADPH and analyzing for substrate disappearance and product appearance by gas chromatography-mass spectrometry. Using this approach, we found indications of carboxylesterase activity, in the form of appropriate alcohol metabolites for three aliphatic esters in hostplant tissues-octyl acetate, octyl butyrate, and hexyl butyrate. Involvement of webworm esterases in hostplant detoxification subsequently was confirmed with metabolism assays with pure compounds. This study is the first to implicate esterases in lepidopteran larval midgut metabolism of aliphatic esters, ubiquitous constituents of flowers and fruits. In addition, this method confirmed that webworms detoxify furanocoumarins and myristicin in their hostplants via cytochrome P450-mediated metabolism, and demonstrated that these enzymes also metabolize the coumarin osthol and the fatty acid derivative palmitolactone.

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Pyrethroid resistance and esterase activity in three strains of the cotton bollworm, Helicoverpa armigera (Hübner)

Cited by 19 publications

References 21 publications

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

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

Overexpressed esterases in a fenvalerate resistant strain of the cotton bollworm, Helicoverpa armigera

Aliphatic Esters as Targets of Esterase Activity in the Parsnip Webworm (Depressaria pastinacella)

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