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, D
dc.contributor.author Lawrence, MC
dc.contributor.author Graham, LD
dc.contributor.author Hannan, GN
dc.contributor.author Simpson, AM
dc.contributor.author Hill, RJ
dc.date.accessioned 2012-10-12T03:33:05Z
dc.date.issued 2011-11
dc.identifier.citation Pest management science, 2011, 67 (11), pp. 1457 - 1467
dc.identifier.issn 1526-498X
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18038
dc.description.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 > α-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 hormone makisterone A.
dc.format Print-Electronic
dc.language eng
dc.relation.isbasedon 10.1002/ps.2200
dc.title Isoforms of the heteropteran Nezara viridula ecdysone receptor: protein characterisation, RH5992 insecticide binding and homology modelling.
dc.type Journal Article
dc.parent Pest management science
dc.journal.volume 11
dc.journal.volume 67
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 0502 Environmental Science and Management
dc.for 0608 Zoology
dc.personcode 940084
dc.personcode 0000067884
dc.personcode 0000067885
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 Animals
dc.description.keywords Heteroptera
dc.description.keywords Hydrazines
dc.description.keywords Ecdysterone
dc.description.keywords Ligands
dc.description.keywords Insecticides
dc.description.keywords Sequence Analysis, Protein
dc.description.keywords Protein Binding
dc.description.keywords Amino Acid Sequence
dc.description.keywords Mass Spectrometry
dc.description.keywords Molecular Sequence Data
dc.description.keywords Electrophoresis, Gel, Two-Dimensional
dc.description.keywords Protein Isoforms
dc.description.keywords Receptors, Steroid
dc.description.keywords Ecdysteroids
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - Health Technologies
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true
utslib.collection.history Closed (ID: 3)
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)


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