0000000000123864

AUTHOR

Nadine Bautsoens

showing 2 related works from this author

Binding Site Alteration Is Responsible for Field-Isolated Resistance to Bacillus thuringiensis Cry2A Insecticidal Proteins in Two Helicoverpa Species

2010

Background Evolution of resistance by target pests is the main threat to the long-term efficacy of crops expressing Bacillus thuringiensis (Bt) insecticidal proteins. Cry2 proteins play a pivotal role in current Bt spray formulations and transgenic crops and they complement Cry1A proteins because of their different mode of action. Their presence is critical in the control of those lepidopteran species, such as Helicoverpa spp., which are not highly susceptible to Cry1A proteins. In Australia, a transgenic variety of cotton expressing Cry1Ac and Cry2Ab (Bollgard II) comprises at least 80% of the total cotton area. Prior to the widespread adoption of Bollgard II, the frequency of alleles conf…

0106 biological sciencesCrops AgriculturalInsecticidesHelicoverpa punctigeraScienceUNESCO::CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología generalBacillus thuringiensisBacterial ProteinGenetically modified cropsHelicoverpa armigera01 natural sciencesMicrobiologyLepidoptera genitaliaInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanyBacillus thuringiensiBiotechnology/Applied MicrobiologyAnimalsMode of actionBiotechnology/Plant BiotechnologyHelicoverpaInsecticide030304 developmental biology0303 health sciencesMultidisciplinaryBinding SitesbiologyAnimalQfungiBinding SiteRbiology.organism_classificationBinding site alterationHelicoverpa speciesLepidoptera010602 entomologyCry1AcBacillus thuringiensis; Binding site alteration; Helicoverpa speciesMedicine:CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología general [UNESCO]Plant Biology/Agricultural BiotechnologyResearch ArticleProtein BindingPLoS ONE
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Specific binding  of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species

2008

ABSTRACT For a long time, it has been assumed that the mode of action of Cry2A toxins was unique and different from that of other three-domain Cry toxins due to their apparent nonspecific and unsaturable binding to an unlimited number of receptors. However, based on the homology of the tertiary structure among three-domain Cry toxins, similar modes of action for all of them are expected. To confirm this hypothesis, binding assays were carried out with 125 I-labeled Cry2Ab. Saturation assays showed that Cry2Ab binds in a specific and saturable manner to brush border membrane vesicles (BBMVs) of Helicoverpa armigera . Homologous-competition assays with 125 I-Cry2Ab demonstrated that this toxi…

BioquímicaBrush borderBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaPlasma protein bindingHelicoverpa armigeraApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteHelicoverpaBacillus thuringiensis ToxinsStaining and LabelingEcologybiologyfungiMidgutbiology.organism_classificationEndotoxinsGastrointestinal TractLepidopteraKineticsBiochemistryHelicoverpa zeaProteïnesProtein BindingFood ScienceBiotechnology
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