Isoforms Of The Heteropteran Nezara Viridula Ecdysone Receptor: Protein Characterisation, Rh5992 Insecticide Binding And Homology Modelling

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dc.contributor.author Tohidi-Esfahani, Donya en_US
dc.contributor.author Lawrence, M.C. en_US
dc.contributor.author Graham, Lloyd en_US
dc.contributor.author Hannan, G en_US
dc.contributor.author Simpson, Ann en_US
dc.contributor.author Hill, Ron en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-10-12T03:33:05Z
dc.date.available 2012-10-12T03:33:05Z
dc.date.issued 2011 en_US
dc.identifier 2011003497 en_US
dc.identifier.citation Tohidi-Esfahani Donya et al. 2011, 'Isoforms Of The Heteropteran Nezara Viridula Ecdysone Receptor: Protein Characterisation, Rh5992 Insecticide Binding And Homology Modelling', John Wiley & Sons, vol. 67, no. 11, pp. 1457-1467. en_US
dc.identifier.issn 1526-498X en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18038
dc.description.abstract Abstract: BACKGROUND: Certain bisacylhydrazine compounds such as tebufenozide (RH5992) have been shown to act as order-specific insecticides. Their compatibility with predatory Heteroptera, which are used as biological control agents, has also been demonstrated. However, the molecular mode of action of these ecdysone agonists has not been explored in a heteropteran, much less one that is a significant agricultural pest, such as Nezara viridula. RESULTS: Alternatively spliced ligand-binding regions of the N. viridula ecdysone receptor were expressed, purified and characterised by 2D gel analysis, mass spectrometry, homology modelling and competitive binding of a bisacylhydrazine insecticidal compound (RH5992) and various ecdysteroids. Ligand binding by the two splice isoforms was indistinguishable, and relative affinities were found to occur in the order muristerone A > ponasterone A > 20-hydroxyecdysone > inokosterone > RH5992 > alpha-ecdysone. CONCLUSION: The predicted difference in amino acid sequence between the ligand-binding domains of the N. viridula ecdysone receptor splice variants was verified by mass spectrometry. Both splice variant isoforms exhibit a greater affinity for the bisacylhydrazine insecticide RH5992 than do the other hemipteran ecdysone receptors characterised to date. Their affinities for a range of ecdysteroids also distinguish them from the ecdysone receptors of other Hemiptera characterised thus far. Homology models of both N. viridula receptor isoforms provide further insight into the bisacylhydrazine- and ecdysteroid-binding properties of these receptors, including their similar affinity for 20-hydroxyecdysone and the postulated pentatomomorphan moulting hormonemakisterone A. en_US
dc.language en_US
dc.publisher John Wiley & Sons en_US
dc.relation.isbasedon http://dx.doi.org/10.1002/ps.2200 en_US
dc.title Isoforms Of The Heteropteran Nezara Viridula Ecdysone Receptor: Protein Characterisation, Rh5992 Insecticide Binding And Homology Modelling en_US
dc.parent Pest Management Science en_US
dc.journal.volume 67 en_US
dc.journal.number 11 en_US
dc.publocation Chichester, UK en_US
dc.identifier.startpage 1457 en_US
dc.identifier.endpage 1467 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 050200 en_US
dc.personcode 96111327 en_US
dc.personcode 0000075526 en_US
dc.personcode 0000067884 en_US
dc.personcode 0000067885 en_US
dc.personcode 940084 en_US
dc.personcode 0000030809 en_US
dc.percentage 50 en_US
dc.classification.name Environmental Science and Management en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords Bisacylhydrazine; Ecdysone; Heteroptera; Homology modelling; Receptor; Tebufenozide en_US


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