Search results for "Helicoverpa"

showing 10 items of 20 documents

Characterization of the resistance to Vip3Aa in Helicoverpa armigera from Australia and the role of midgut processing and receptor binding.

2016

AbstractCrops expressing genes from Bacillus thuringiensis (Bt crops) are among the most successful technologies developed for the control of pests but the evolution of resistance to them remains a challenge. Insect resistant cotton and maize expressing the Bt Vip3Aa protein were recently commercialized, though not yet in Australia. We found that, although relatively high, the frequency of alleles for resistance to Vip3Aa in field populations of H. armigera in Australia did not increase over the past four seasons until 2014/15. Three new isofemale lines were determined to be allelic with previously isolated lines, suggesting that they belong to one common gene and this mechanism is relative…

0106 biological sciences0301 basic medicineCrops AgriculturalInsecticidesHelicoverpa armigeraPlant disease resistanceMothsmedicine.disease_cause01 natural sciencesArticleMicrobiology03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanymedicineAnimalsBinding siteGeneAllelesDisease ResistancePlant DiseasesMultidisciplinarybiologyToxinfungiAustraliaMidgutbiology.organism_classificationPlants Genetically Modified010602 entomology030104 developmental biologyCry1AcScientific reports
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Isolating, characterising and identifying a Cry1Ac resistance mutation in field populations of Helicoverpa punctigera

2018

AbstractTransgenic cotton expressing insecticidal proteins from Bacillus thuringiensis (Bt) has been grown in Australia for over 20 years and resistance remains the biggest threat. The native moth, Helicoverpa punctigera is a significant pest of cotton. A genotype causing resistance to Cry1Ac in H. punctigera was isolated from the field and a homozygous line established. The phenotype is recessive and homozygous individuals possess 113 fold resistance to Cry1Ac. Individuals that carry Cry1Ac resistance genes are rare in Australia with a frequency of 0.033 being detected in field populations. RNAseq, RT-PCR and DNA sequencing reveals a single nucleotide polymorphism at a splice site in the c…

0106 biological sciences0301 basic medicineHelicoverpa punctigeralcsh:MedicinePolymorphism Single Nucleotide01 natural sciencesArticleInsecticide ResistanceHemolysin Proteins03 medical and health sciencesBacterial ProteinsBacillus thuringiensisGenotypeAnimalsPest Control Biologicallcsh:ScienceGeneGeneticsGossypiumMultidisciplinaryBacillus thuringiensis ToxinsbiologyCadherinlcsh:RfungiAustraliaIntronCadherinsResistance mutationbiology.organism_classificationEndotoxinsLepidoptera010602 entomology030104 developmental biologyCry1Aclcsh:QScientific Reports
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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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RNA interference in Lepidoptera: an overview of successful and unsuccessful studies and implications for experimental design.

2011

International audience; Gene silencing through RNA interference (RNAi) has revolutionized the study of gene function, particularly in non-model insects. However, in Lepidoptera (moths and butterflies) RNAi has many times proven to be difficult to achieve. Most of the negative results have been anecdotal and the positive experiments have not been collected in such a way that they are possible to analyze. In this review, we have collected detailed data from more than 150 experiments including all to date published and many unpublished experiments. Despite a large variation in the data, trends that are found are that RNAi is particularly successful in the family Saturniidae and in genes involv…

0106 biological sciencesPhysiology[SDV]Life Sciences [q-bio]Tissue uptakeBioinformatics01 natural sciencesRNA interferenceRNA interferenceDatabases GeneticDelivery methodsCaenorhabditis elegansRegulation of gene expression0303 health sciencesIMMUNE-RESPONSESMANDUCA-SEXTALepidopteraRNA silencingSILKWORM BOMBYX-MORIResearch DesignInsect ProteinsRNA InterferenceMESSENGER-RNAHELICOVERPA-ARMIGERADOUBLE-STRANDED-RNAComputational biologyBiologyLepidoptera genitaliadsRNA properties03 medical and health sciencesBACILLUS-THURINGIENSISSMALL SILENCING RNASGene silencingAnimalsGene SilencingGene030304 developmental biologyRNA Double-StrandedMechanism (biology)fungiBiology and Life SciencesARMYWORM SPODOPTERA-FRUGIPERDAbiology.organism_classificationImmunity Innate010602 entomologyGene Expression RegulationInsect ScienceEpidermisCAENORHABDITIS-ELEGANSGene functionJournal of insect physiology
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Efficacy and Resistance Management Potential of a Modified Vip3C Protein for Control of Spodoptera frugiperda in Maize

2018

AbstractA modified Vip3C protein has been developed that has a spectrum of activity that has the potential to be commercially useful for pest control, and shows good efficacy against Spodoptera frugiperda in insect bioassays and field trials. For the first time Vip3A and Vip3C proteins have been compared to Cry1 and Cry2 proteins in a complete set of experiments from insect bioassays to competition binding assays to field trials, and the results of these complementary experiments are in agreement with each other. Binding assays with radiolabelled toxins and brush border membrane vesicles from S. frugiperda and Helicoverpa armigera show that the modified Vip3C protein shares binding sites wi…

0301 basic medicineBrush bordermedia_common.quotation_subject030106 microbiologyBacillus thuringiensislcsh:MedicineInsectBiologyHelicoverpa armigeraSpodopteraSpodopteraZea maysArticleInsecticide Resistance03 medical and health sciencesBacillus thuringiensisBioassayAnimalsBinding sitePest Control Biologicallcsh:Sciencemedia_commonMultidisciplinaryBinding Sitesbusiness.industryfungilcsh:RPest controlbiology.organism_classificationPlants Genetically ModifiedEndotoxinsBiochemistryLarvalcsh:QbusinessScientific Reports
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Analysis of cross-resistance to Vip3 proteins in eight insect colonies, from four insect species, selected for resistance to Bacillus thuringiensis i…

2018

Abstract Bacillus thuringiensis Vip3 proteins are synthesized and secreted during the vegetative growth phase. They are activated by gut proteases, recognize and bind to midgut receptors, form pores and lyse cells. We tested the susceptibility to Vip3Aa and Vip3Ca of Cry1A-, Cry2A-, Dipel- and Vip3-resistant insect colonies from different species to determine whether resistance to other insecticidal proteins confers cross-resistance to Vip3 proteins. As expected, the colonies resistant to Cry1A proteins, Dipel (Helicoverpa armigera, Trichoplusia ni, Ostrinia furnacalis and Plodia interpunctella) or Cry2Ab (H. armigera and T. ni) were not cross-resistant to Vip3 proteins. In contrast, H. arm…

0301 basic medicineProteasesInsectabiologymedia_common.quotation_subjectfungi030106 microbiologyBacillus thuringiensisMidgutInsectHelicoverpa armigerabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsCross-resistancemedia_commonOstrinia furnacalisJournal of Invertebrate Pathology
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Characterization of Bacillus thuringiensis isolates by their insecticidal activity and their production of Cry and Vip3 proteins.

2018

WOS: 000449027600099 PubMed ID: 30383811 Bacillus thuringiensis (Bt) constitutes the active ingredient of many successful bioinsecticides used in agriculture. In the present study, the genetic diversity and toxicity of Bt isolates was investigated by characterization of native isolates originating from soil, fig leaves and fruits from a Turkish collection. Among a total of 80 Bt isolates, 18 of them were found carrying a vip3 gene (in 23% of total), which were further selected. Insecticidal activity of spore/crystal mixtures and their supernatants showed that some of the Bt isolates had significantly more toxicity against some lepidopteran species than the HD1 reference strain. Five isolate…

0301 basic medicineTurkeyProtein ExpressionBacillus Thuringiensislcsh:MedicineArtificial Gene Amplification and ExtensionBacillusProtein SequencingMothsToxicologyPathology and Laboratory MedicinePolymerase Chain ReactionDatabase and Informatics MethodsBacillus thuringiensisMedicine and Health SciencesToxinslcsh:ScienceMaterialsSoil MicrobiologyMultidisciplinaryBacterial PathogensMedical MicrobiologyPhysical SciencesPathogensSequence AnalysisResearch ArticleSequence analysisBioinformatics030106 microbiologyBacterial ToxinsMaterials ScienceToxic AgentsSequence DatabasesBiologySpodopteraHelicoverpa armigeraResearch and Analysis MethodsCrystalsMicrobiologyMicrobiology03 medical and health sciencesBacterial ProteinsGene Expression and Vector TechniquesAnimalsPest Control BiologicalMolecular Biology TechniquesSequencing TechniquesGeneMolecular BiologyMicrobial PathogensPlant DiseasesGenetic diversityMolecular Biology Assays and Analysis TechniquesToxicityBacterialcsh:RfungiOrganismsBiology and Life Sciencesbiology.organism_classificationFicusSporePlant Leaves030104 developmental biologyBiological DatabasesCry1AcSusceptibilityFruitlcsh:QPloS one
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Production and characterization of Bacillus thuringiensis Cry1Ac-resistant cotton bollworm Helicoverpa zea (Boddie).

2007

ABSTRACT Laboratory-selected Bacillus thuringiensis -resistant colonies are important tools for elucidating B. thuringiensis resistance mechanisms. However, cotton bollworm, Helicoverpa zea , a target pest of transgenic corn and cotton expressing B. thuringiensis Cry1Ac (Bt corn and cotton), has proven difficult to select for stable resistance. Two populations of H. zea (AR and MR), resistant to the B. thuringiensis protein found in all commercial Bt cotton varieties (Cry1Ac), were established by selection with Cry1Ac activated toxin (AR) or MVP II (MR). Cry1Ac toxin reflects the form ingested by H. zea when feeding on Bt cotton, whereas MVP II is a Cry1Ac formulation used for resistance se…

Bacterial ToxinsBacillus thuringiensisMothsGossypiumApplied Microbiology and BiotechnologyCypermethrinInsecticide Resistancechemistry.chemical_compoundHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsPest Control BiologicalGossypiumGenetically modified maizeEcologybiologyBacillus thuringiensis Toxinsfungifood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticulturechemistryAgronomyCry1AcBt cottonHelicoverpa zeaPEST analysisFood ScienceBiotechnologyProtein BindingApplied and environmental microbiology
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Common receptor for Bacillus thuringiensis toxins Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea and Spodoptera exigua

2005

ABSTRACT Binding studies using 125 I-Cry1Ac and biotinylated Cry1Fa toxins indicate the occurrence of a common receptor for Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera , Helicoverpa zea , and Spodoptera exigua . Our results, along with previous binding data and the observed cases of cross-resistance, suggest that this pattern seems to be widespread among lepidopteran species.

Bacterial ToxinsBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaReceptors Cell SurfaceSpodopteraHelicoverpa armigeraSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyInvertebrate MicrobiologyAnimalsBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungibiology.organism_classificationEndotoxinsLepidopteraCry1AcInsect ProteinsNoctuidaeHelicoverpa zeaFood ScienceBiotechnology
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Interaction of Bacillus thuringiensis Toxins with Larval Midgut Binding Sites of Helicoverpa armigera (Lepidoptera: Noctuidae)

2004

ABSTRACT In 1996, Bt-cotton (cotton expressing a Bacillus thuringiensis toxin gene) expressing the Cry1Ac protein was commercially introduced to control cotton pests. A threat to this first generation of transgenic cotton is the evolution of resistance by the insects. Second-generation Bt-cotton has been developed with either new B. thuringiensis genes or with a combination of cry genes. However, one requirement for the “stacked” gene strategy to work is that the stacked toxins bind to different binding sites. In the present study, the binding of 125 I-labeled Cry1Ab protein ( 125 I-Cry1Ab) and 125 I-Cry1Ac to brush border membrane vesicles (BBMV) of Helicoverpa armigera was analyzed in com…

Bacterial ToxinsPopulationBacillus thuringiensisCarbohydratesDrug ResistanceHelicoverpa armigeraModels BiologicalApplied Microbiology and BiotechnologyMicrobiologyHemolysin Proteinschemistry.chemical_compoundBacterial ProteinsLectinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsBinding siteSoybean agglutininPest Control BiologicaleducationGossypiumeducation.field_of_studyBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungifood and beveragesPlants Genetically Modifiedbiology.organism_classificationSialic acidEndotoxinsLepidopteraKineticsCry1AcchemistryBiochemistryGenes BacterialLarvaNoctuidaeDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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