An ecdysone receptor from the pentatomomorphan, Nezara viridula, shows similar affinities for moulting hormones makisterone A and 20-hydroxyecdysone

Tohidi-Esfahani, Donya; Graham, Lloyd D.; Hannan, Garry N.; Simpson, Ann M.; Hill, Ronald J.

doi:10.1016/j.ibmb.2010.10.002

Cited by 16 publications

(29 citation statements)

References 84 publications

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“…The dissociation constant ( K d =3.0±1.7 nM) for the PxEcRB/USP heterodimer is comparable to EcR/USP complex from other insects, such as in lepidopteran 1.0-2.0 nM [27,44,45], coleopteran 2.8 nM for L. decemlineata [32], dipsteran 0.9-2.8nM [2,46], pentatomomor-phan 6.8 nM for Nezara viridula [47], and orthopteran 1.2 nM for Locusta migratoria [48]. Comparative analysis of receptor-binding affinity among insects sheds light on the divergence of the toxicity of ecdysone agonists.…”

Section: Discussionmentioning

confidence: 96%

Cloning, ligand-binding, and temporal expression of ecdysteroid receptors in the diamondback moth, Plutella xylostella

et al. 2012

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BackgroundThe diamondback moth, Plutella xylostella (L.) (Lepidoptera: Plutellidae), is a devastating pest of cruciferous crops worldwide, and has developed resistance to a wide range of insecticides, including diacylhydrazine-based ecdysone agonists, a highly selective group of molt-accelerating biopesticides targeting the ecdysone receptors.ResultIn this study, we cloned and characterized the ecdysone receptors from P. xylostella, including the two isoforms of EcR and a USP. Sequence comparison and phylogenetic analysis showed striking conservations among insect ecdysone receptors, especially between P. xylostella and other lepidopterans. The binding affinity of ecdysteroids to in vitro-translated receptor proteins indicated that PxEcRB isoform bound specifically to ponasterone A, and the binding affinity was enhanced by co-incubation with PxUSP (Kd =3.0±1.7 nM). In contrast, PxEcRA did not bind to ponasterone A, even in the presence of PxUSP. The expression of PxEcRB were consistently higher than that of PxEcRA across each and every developmental stage, while the pattern of PxUSP expression is more or less ubiquitous.ConclusionsTarget site insensitivity, in which the altered binding of insecticides (ecdysone agonists) to their targets (ecdysone receptors) leads to an adaptive response (resistance), is one of the underlying mechanisms of diacylhydrazine resistance. Given the distinct differences at expression level and the ligand-binding capacity, we hypothesis that PxEcRB is the ecdysone receptor that controls the remodeling events during metamorphosis. More importantly, PxEcRB is the potential target site which is modified in the ecdysone agonist-resistant P. xylostella.

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Section: Discussionmentioning

confidence: 96%

Cloning, ligand-binding, and temporal expression of ecdysteroid receptors in the diamondback moth, Plutella xylostella

et al. 2012

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“…All residues in this region, except Ile227, are strictly conserved across hemipteran, lepidopteran, dipteran, and coleopteran species (see table 2 in 26). The exceptional replacement of Ile227 by a leucine occurs in the southern green stink bug, Nezara viridula, where it correlates with an increased preference for makisterone A relative to 20E (111,112).…”

Section: Structure and Topography Of The Ecdysteroid-binding Pocketmentioning

confidence: 99%

Ecdysone Receptors: From the Ashburner Model to Structural Biology

Hill

Billas

Bonneton

et al. 2013

Annu. Rev. Entomol.

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138

101

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In 1974, Ashburner and colleagues postulated a model to explain the control of the puffing sequence on Drosophila polytene chromosomes initiated by the molting hormone 20-hydroxyecdysone. This model inspired a generation of molecular biologists to clone and characterize elements of the model, thereby providing insights into the control of gene networks by steroids, diatomic gases, and other small molecules. It led to the first cloning of the EcR subunit of the heterodimeric EcR-USP ecdysone receptor. X-ray diffraction studies of the ligand-binding domain of the receptor are elucidating the specificity of receptor-ecdysteroid interactions, the selectivity of some environmentally friendly insecticides, the evolution of the EcR-USP heterodimer, and indeed Ashburner's classical biochemical evidence for the central role of the ecdysone receptor in his model.

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“…The latter is composed of 12 α‐helices (H1 to H12) arranged as an antiparallel three‐layer sandwich associated with a hairpin of two short β‐strands (β1 and β2) in the loop between helices H5 and H6 . The ligand‐binding pocket that holds the cognate ligand is formed by side chains of residues from helices H3, H5, H7, H11 and H12, and the β‐hairpin …”

Section: Introductionmentioning

confidence: 99%

Insect growth regulators as potential insecticides to control olive fruit fly (Bactrocera oleae Rossi): insect toxicity bioassays and molecular docking approach

Bengochea

Christiaens

Amor

et al. 2012

Pest Management Science

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An ecdysone receptor from the pentatomomorphan, Nezara viridula, shows similar affinities for moulting hormones makisterone A and 20-hydroxyecdysone

Cited by 16 publications

References 84 publications

Cloning, ligand-binding, and temporal expression of ecdysteroid receptors in the diamondback moth, Plutella xylostella

Cloning, ligand-binding, and temporal expression of ecdysteroid receptors in the diamondback moth, Plutella xylostella

Ecdysone Receptors: From the Ashburner Model to Structural Biology

Insect growth regulators as potential insecticides to control olive fruit fly (Bactrocera oleae Rossi): insect toxicity bioassays and molecular docking approach

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