Search results for "Cry1A"

showing 10 items of 53 documents

Scientific Opinion on application EFSA‐GMO‐BE‐2013‐117 for authorisation of genetically modified maize MON 87427 × MON 89034 × NK603 and subcombinati…

2017

Scientific opinionRequestor: Competent Authority of BelgiumQuestion number: EFSA-Q-2013-00765; In this opinion, the EFSA Panel on Genetically Modified Organisms (GMO Panel) assessed the three-event stack maize MON 87427 9 MON 89034 9 NK603 and its three subcombinations, independently of their origin. The GMO Panel has previously assessed the three single events combined to produce this three-event stack maize and did not identify safety concerns. No new data on the single events, leading to modification of the original conclusions on their safety, were identified. Based on the molecular, agronomic, phenotypic and compositional characteristics, the combination of the single maize events and …

0106 biological sciencesCry1Aherbicide tolerancemaïsVeterinary (miscellaneous)gmo[SDV]Life Sciences [q-bio]MON87427xMON89034xNK603ogmPlant Science010501 environmental sciencesmaizeCP4EPSPS01 natural sciencesMicrobiologyzea maysMON 87427 × MON 89034 × NK603Cry2Ab2CP4 EPSPS0105 earth and related environmental sciences2. Zero hungerCP4 EPSPSCry1A.105indian cornRegulation (EC) No 1829/2003105GMO;maize;herbicide tolerance;insect resistance;CP4 EPSPS;Cry1A.105;Cry2Ab2;Regulation (EC) No 1829/2003;MON 87427 x MON 89034 x NK603MON 87427 9 MON 89034 9 NK603Scientific OpinionRegulation (EC) No1829/2003Animal Science and ZoologyParasitologyinsect resistance010606 plant biology & botanyFood ScienceRegulation (EC) No 1829/2003
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Annual post-market environmental monitoring (PMEM) report on the cultivation of genetically modified maize MON 810 in 2014 from Monsanto Europe S.A.

2016

Requestor: European CommissionQuestion number: EFSA-Q-2015-00650; Following a request from the European Commission, the Panel on Genetically Modified Organisms of the European Food Safety Authority (GMO Panel) assessed the annual post-market environmental monitoring (PMEM) report for the 2014 growing season of maize MON 810 provided by Monsanto Europe S.A. The GMO Panel concludes that the insect resistance monitoring data do not indicate a decrease in susceptibility of field Iberian populations of corn borers to the Cry1Ab protein over the 2014 season. However, as the methodology for insect resistance monitoring remained unchanged compared to previous PMEM reports, the GMO Panel reiterates …

0106 biological sciencesSettore BIO/07 - EcologiaVeterinary (miscellaneous)[SDV]Life Sciences [q-bio]TP1-1185Plant Science010501 environmental sciencesZea mays01 natural sciencesMicrobiologycase‐specific monitoringCry1Ab case-specific monitoring farmer questionnaires general surveillance insect resistance management Zea maysTX341-641Cry1Ab0105 earth and related environmental sciences2. Zero hungerNutrition. Foods and food supplyChemical technologyfungigeneral surveillance10079 Institute of Veterinary Pharmacology and Toxicologyfarmer questionnairesinsect resistance managementSettore AGR/02 - Agronomia E Coltivazioni ErbaceeSettore AGR/11 - Entomologia Generale E Applicata570 Life sciences; biologyAnimal Science and ZoologyParasitology010606 plant biology & botanyFood Science
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Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua

2021

The ATP binding cassette (ABC) transporters are membrane proteins that can act as putative receptors for Cry proteins from Bacillus thuringiensis (Bt) in the midgut of different insects. For the beet armyworm, Spodoptera exigua, ABCC2 and ABCC3 have been found to interact with Cry1A proteins, the main insecticidal proteins used in Bt crops, as well as Bt-based pesticides. The ABCC2 has shown to have specific binding towards Cry1Ac and is involved in the toxic process of Cry1A proteins, but the role of this transporter and how it relates with the Cry1A proteins is still unknown. Here, we have characterized the interactions between the SeABCC2 and the main proteins that bind to the receptor. …

0301 basic medicineCell SurvivalBacillus thuringiensisATP-binding cassette transporterSpodopteraSpodopteraBiochemistryHemolysin Proteins03 medical and health sciences0302 clinical medicineBacterial ProteinsProtein DomainsBacillus thuringiensisSf9 CellsAnimalsBinding siteReceptorMolecular BiologyBinding SitesBacillus thuringiensis ToxinsbiologyChemistryfungifood and beveragesTransporterCell Biologybiology.organism_classificationMultidrug Resistance-Associated Protein 2Endotoxins030104 developmental biologyMembrane proteinCry1AcBiochemistryMutationInsect ProteinsMultidrug Resistance-Associated ProteinsProtein Multimerization030217 neurology & neurosurgeryProtein BindingBiochemical Journal
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Insecticidal Activity and Synergistic Combinations of Ten Different Bt Toxins against Mythimna separata (Walker)

2018

The oriental armyworm (OAW), Mythimna separata (Walker), is a destructive pest of agricultural crops in Asia and Australia. Commercialized Bt crops have performed very well against their target pests

0301 basic medicineInsecticidesHealth Toxicology and MutagenesisBacterial ToxinsBacillus thuringiensislcsh:MedicineVip3 proteinMothsToxicologymedicine.disease_causeArticleMicrobiology03 medical and health sciencesMythimna separataBacillus thuringiensis<i>Bacillus thuringiensis</i>medicineAnimalsBioassayPotencyCry proteinbiologyToxinlcsh:Rfungifood and beveragesDrug Synergismbiology.organism_classification030104 developmental biologyCry1AcLarvaoriental armywormPEST analysisBacteriaToxins
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Ephestia kuehniella tolerance to Bacillus thuringiensis Cry1Aa is associated with reduced oligomer formation

2016

The basis of the different susceptibility of Ephestia kuehniella to the Cry1Aa and Cry1Ac δ-endotoxins from Bacillus thuringiensis kurstaki BNS3 was studied. Both toxins bound specifically to the BBMV of E. kuehniella. The result of the ligand blot showed that Cry1Ac bound to three putative receptors of about 100, 65 and 80 kDa and Cry1Aa interacted only with a 100 kDa protein. Pronase digestion of the BBMV-bound toxins was used to analyze the toxin insertion. Both toxins inserted into the BBMV as monomers however, a 14 kDa peptide of α4-α5 which correspond to the oligomeric form of this peptide was detected in case of Cry1Ac only. Analysis of the in vitro oligomerisation of these toxins in…

0301 basic medicineProtein ConformationBacillus thuringiensisBiophysicsPeptidemedicine.disease_causeBiochemistryOligomerHemolysin Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsBacillus thuringiensismedicineAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis Toxins030102 biochemistry & molecular biologybiologyToxinfungiCell BiologyLigand (biochemistry)biology.organism_classificationEndotoxinsLepidopteraBlot030104 developmental biologyBiochemistryCry1AcchemistryProtein MultimerizationBiochemical and Biophysical Research Communications
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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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A mathematical model of exposure of nontarget Lepidoptera to Bt-maize pollen expressing Cry1Ab within Europe

2010

Genetically modified (GM) maize MON810 expresses a Cry1Ab insecticidal protein, derived from Bacillus thuringiensis ( Bt ), toxic to lepidopteran target pests such as Ostrinia nubilalis . An environmental risk to non-target Lepidoptera from this GM crop is exposure to harmful amounts of Bt -containing pollen deposited on host plants in or near MON810 fields. An 11-parameter mathematical model analysed exposure of larvae of three non-target species: the butterflies Inachis io (L.), Vanessa atalanta (L.) and moth Plutella xylostella (L.), in 11 representative maize cultivation regions in four European countries. A mortality–dose relationship was integrated with a dose–distance relationship t…

1001genetically modified maize Cry1Ab non-target Lepidoptera mathematical model exposure risk assessment60Bacillus thuringiensismedicine.disease_causeZea maysModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyOstriniaExposureCropLepidoptera genitaliaHemolysin ProteinsMathematical modelBacterial ProteinsResearch articlesPollenBacillus thuringiensismedicineAnimalsPest Control BiologicalGeneral Environmental ScienceRisk assessmentGenetically modified maize31General Immunology and MicrobiologybiologyBacillus thuringiensis Toxinsbusiness.industryfungiPest controlPlutellafood and beveragesGeneral MedicineNon-target lepidopterabiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraAgronomyGenetically modified maizePollenCry1abGeneral Agricultural and Biological SciencesbusinessButterflies
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Integrative Model for Binding of Bacillus thuringiensis Toxins in Susceptible and Resistant Larvae of the Diamondback Moth (Plutella xylostella)

1999

ABSTRACT Insecticidal crystal proteins from Bacillus thuringiensis in sprays and transgenic crops are extremely useful for environmentally sound pest management, but their long-term efficacy is threatened by evolution of resistance by target pests. The diamondback moth ( Plutella xylostella ) is the first insect to evolve resistance to B. thuringiensis in open-field populations. The only known mechanism of resistance to B. thuringiensis in the diamondback moth is reduced binding of toxin to midgut binding sites. In the present work we analyzed competitive binding of B. thuringiensis toxins Cry1Aa, Cry1Ab, Cry1Ac, and Cry1F to brush border membrane vesicles from larval midguts in a susceptib…

Bacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsApplied Microbiology and BiotechnologyBinding CompetitiveModels BiologicalHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalGeneticsBacillaceaeDiamondback mothBinding SitesEcologybiologyBacillus thuringiensis ToxinsParasporal bodyfungiPlutellafood and beveragesbiology.organism_classificationEndotoxinsCry1AcLarvaFood ScienceBiotechnology
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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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