Search results for "Heliothis virescens"

showing 10 items of 11 documents

Bacillus thuringiensis Vip3Aa Toxin Resistance in Heliothis virescens (Lepidoptera: Noctuidae)

2017

ABSTRACT Laboratory selection with Vip3Aa of a field-derived population of Heliothis virescens produced >2,040-fold resistance in 12 generations of selection. The Vip3Aa-selected (Vip-Sel)-resistant population showed little cross-resistance to Cry1Ab and no cross-resistance to Cry1Ac. Resistance was unstable after 15 generations without exposure to the toxin. F 1 reciprocal crosses between Vip3Aa-unselected (Vip-Unsel) and Vip-Sel insects indicated a strong paternal influence on the inheritance of resistance. Resistance ranged from almost completely recessive (mean degree of dominance [ h ] = 0.04 if the resistant parent was female) to incompletely dominant (mean h = 0.53 if the resistan…

0106 biological sciences0301 basic medicineMultifactorial Inheritancemedia_common.quotation_subjectPopulationInsectBiology01 natural sciencesApplied Microbiology and BiotechnologyInsecticide ResistanceLepidoptera genitaliaHemolysin Proteins03 medical and health sciencesBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsSelection GeneticeducationCrosses Geneticmedia_commonGeneticseducation.field_of_studyBacillus thuringiensis ToxinsEcologyHeliothis virescensfungibiology.organism_classificationSurvival AnalysisEndotoxinsLepidoptera010602 entomology030104 developmental biologyCry1AcPaternal InheritanceNoctuidaeBiological AssayPEST analysisFood ScienceBiotechnologyApplied and Environmental Microbiology
researchProduct

Constitutive Activation of the Midgut Response to Bacillus thuringiensis in Bt-Resistant Spodoptera exigua

2010

Bacillus thuringiensis is the most effective microbial control agent for controlling numerous species from different insect orders. The main threat for the long term use of B. thuringiensis in pest control is the ability of insects to develop resistance. Thus, the identification of insect genes involved in conferring resistance is of paramount importance. A colony of Spodoptera exigua (Lepidoptera: Noctuidae) was selected for 15 years in the laboratory for resistance to Xentari (TM), a B. thuringiensis-based insecticide, reaching a final resistance level of greater than 1,000-fold. Around 600 midgut ESTs were analyzed by DNA-macroarray in order to find differences in midgut gene expression …

0106 biological sciencesDrug Resistancelcsh:MedicineGene ExpressionInsectaminopeptidase n01 natural sciencesAminopeptidasesHemolysin ProteinsEndotoxinmanduca-sextaBacillus thuringiensisInsect ProteinBiotechnology/Applied Microbiologylcsh:Scienceheliothis-virescensmedia_common0303 health sciencesLarvaMultidisciplinarybiologymediated insect resistanceGenetics and Genomics/Gene ExpressionEcology/Population Ecologybacterial-infectionNoctuidaeInsect ProteinsResearch Articlemedia_common.quotation_subjectAminopeptidaseMolecular Sequence DataBacillus thuringiensisBacterial ProteinSpodopteraSpodopterastem-cell proliferationMicrobiology03 medical and health sciencesMicrobiology/Applied MicrobiologyBacterial ProteinsExiguaBotanyBacillus thuringiensiAnimalscrystal proteinsBIOS Plant Development SystemsAmino Acid Sequencekinase pathways030304 developmental biologyposterior midgutHeliothis virescensBacillus thuringiensis ToxinsAnimaltrichoplusia-nilcsh:RfungiMidgutHemolysin Proteinbiology.organism_classificationEndotoxinsGastrointestinal Tract010602 entomologyPlant Biology/Agricultural Biotechnologylcsh:QSequence Alignment
researchProduct

Shared Binding Sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A Toxins

2001

ABSTRACT Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth ( Plutella xylostella ) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that…

Bacterial ToxinsMolecular Sequence DataSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsAmino Acid SequenceBinding siteBinding SitesDiamondback mothBacillus thuringiensis ToxinsEcologybiologyHeliothis virescensfungibiology.organism_classificationEndotoxinsLepidopteraPlutellidaeCry1AcLarvaNoctuidaeFood ScienceBiotechnologyApplied and Environmental Microbiology
researchProduct

Specific binding of radiolabeled Cry1Fa insecticidal protein from Bacillus thuringiensis to midgut sites in lepidopteran species

2012

ABSTRACT Cry1Fa insecticidal protein was successfully radiolabeled with 125 I-Na. Specific binding to brush border membrane vesicles was shown for the lepidopteran species Ostrinia nubilalis , Spodoptera frugiperda , Spodoptera exigua , Helicoverpa armigera , Heliothis virescens , and Plutella xylostella . Homologous competition assays were performed to obtain equilibrium binding parameters ( K d [dissociation constant] and R t [concentration of binding sites]) for these six insect species.

BioquímicavirusesBiotecnologia agrícolaBacillus thuringiensisHelicoverpa armigeraSpodopteraSpodopteraApplied Microbiology and BiotechnologyOstriniaIodine RadioisotopesHemolysin ProteinsPlagues ControlBacterial ProteinsSpecies SpecificityBacillus thuringiensisExiguaBotanyparasitic diseasesPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteTransport VesiclesBinding SitesEcologybiologyHeliothis virescensBacillus thuringiensis ToxinsMicrovillifungiPlutellabiology.organism_classificationEndotoxinsLepidopteraBiochemistryDigestive SystemProteïnesFood ScienceBiotechnology
researchProduct

Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)

2003

Abstract Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1…

Brush borderBacterial ToxinsBacillus thuringiensisGenetically modified cropsBinding CompetitiveBiochemistryMicrobiologyIodine RadioisotopesRadioligand AssayBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyBinding SitesMicrovillibiologyHeliothis virescensCytoplasmic Vesiclesfungifood and beveragesPlutellabiology.organism_classificationRecombinant ProteinsLepidopteraKineticsBt cottonCry1AcLarvaInsect ScienceProtein BindingPink bollwormInsect Biochemistry and Molecular Biology
researchProduct

Reduced levels of membrane-bound alkaline phosphatase in Vip3Aa-resistant Heliothis virescens

2020

ABSTRACTThe Vip3Aa insecticidal protein fromBacillus thuringiensis(Bt) is produced by specific transgenic corn and cotton varieties for efficient control of target lepidopteran pests. The main threat to this technology is the evolution of resistance in targeted insect pests, thus understanding the mechanistic basis of resistance is crucial to deploy the most appropriate strategies for resistance management. In this work, a laboratory-selected colony ofHeliothis virescens(Vip-Sel) highly resistant to the Vip3Aa protein was used to test whether an alteration of membrane receptors in the insect midgut might explain the resistance phenotype. Binding of125I-labeled Vip3Aa to brush border membran…

Genetically modified maizeHeliothis virescensbiologyBrush borderBiochemistryCell surface receptorBacillus thuringiensisfungiAlkaline phosphataseMidgutReceptorbiology.organism_classification
researchProduct

Reduced membrane-bound alkaline phosphatase does not affect binding of Vip3Aa in a Heliothis virescens resistant colony

2020

The Vip3Aa insecticidal protein from Bacillus thuringiensis (Bt) is produced by specific transgenic corn and cotton varieties for efficient control of target lepidopteran pests. The main threat to this technology is the evolution of resistance in targeted insect pests and understanding the mechanistic basis of resistance is crucial to deploy the most appropriate strategies for resistance management. In this work, we tested whether alteration of membrane receptors in the insect midgut might explain the &gt

HELIOTHIS-VIRESCENSInsecticidesHealth Toxicology and Mutagenesislcsh:MedicinePROTEIN0601 Biochemistry and Cell BiologyToxicologyBiotecnologiaInsecticide ResistanceBacillus thuringiensisSITES0303 health sciencesbiologyChemistryfood and beveragesPlants Genetically ModifiedLepidopteraBiochemistryFood Science & TechnologyInsect ProteinsAlkaline phosphatase1115 Pharmacology and Pharmaceutical Sciencestobacco budwormLife Sciences & BiomedicineSPODOPTERA-FRUGIPERDA MIDGUTProtein BindingEXPRESSIONBrush borderBacillus thuringiensisCRY1ACArticleVESICLES03 medical and health sciencesBACILLUS-THURINGIENSISBacterial ProteinsDownregulation and upregulationinsecticidal proteinsCell surface receptor<i>Bacillus thuringiensis</i>AnimalsCROPS030304 developmental biologyScience & TechnologyGenetically modified maizeHeliothis virescens030306 microbiologylcsh:RfungiMembrane ProteinsMidgutAlkaline Phosphatasebiology.organism_classificationTOXIN RESISTANCEinsect resistanceProteïnes
researchProduct

Differences in the midgut proteolytic activity of twoHeliothis virescens strains, one susceptible and one resistant toBacillus thuringiensis toxins

1996

The development of resistance to Bacillus thuringiensis toxic proteins is a growing concern because it could threaten both conventional and gene transfer use of this environmentally safe biological insecticide. The most common mechanism of resistance involves changes in binding affinity of toxin receptors in the insect midgut membrane. This has not been the case in Heliothis virescens. We have investigated changes in midgut proteolytic activity as a possibility to explain the resistance observed in this insect species. We have developed an improvement of known methods to demonstrate proteolytic activity in crude extracts. Using this method we have found differences in the proteolytic activi…

Heliothis virescensbiologyStrain (chemistry)PhysiologyToxinmedia_common.quotation_subjectfungiMidgutGeneral MedicineInsectbiology.organism_classificationmedicine.disease_causeBiochemistryIn vitroMicrobiologyInsect ScienceBacillus thuringiensismedicineReceptormedia_commonArchives of Insect Biochemistry and Physiology
researchProduct

Synergism and Antagonism between Bacillus thuringiensis Vip3A and Cry1 Proteins in Heliothis virescens, Diatraea saccharalis and Spodoptera frugiperda

2014

Made available in DSpace on 2015-03-18T15:56:04Z (GMT). No. of bitstreams: 0 Previous issue date: 2014-10-02Bitstream added on 2015-03-18T16:28:28Z : No. of bitstreams: 1 WOS000342591500006.pdf: 270331 bytes, checksum: c280e3f5bc5e3bb0b92bf74d046135f0 (MD5) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Spanish Ministry of Economy and Competivity FEDER Second generation Bt crops (insect resistant crops carrying Bacillus thuringiensis genes) combine more than one gene that codes for insecticidal proteins in the same plant to provide better control of agricultural pests. Some of the new combinations involve co-expression of cry and vip genes. Because Cry and Vip proteins …

InsecticidesBacillus thuringiensislcsh:MedicineSpodopteraSpodopteraDiatraea saccharalisHemolysin ProteinsLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyGeneticsEscherichia coliAnimalslcsh:ScienceMolecular BiologyMultidisciplinarybiologyHeliothis virescensBacillus thuringiensis Toxinslcsh:RfungiBiology and Life SciencesAgriculturebiology.organism_classificationEndotoxinsLepidopteraBiochemistryCry1AcLarvalcsh:QElectrophoresis Polyacrylamide GelPest ControlAntagonismZoologyEntomologyResearch ArticleBiotechnologyProtein BindingPLoS ONE
researchProduct

Mannose phosphate isomerase isoenzymes in Plutella xylostella support common genetic bases of resistance to Bacillus thuringiensis toxins in Llpidopt…

2001

ABSTRACT A strong correlation between two mannose phosphate isomerase (MPI) isoenzymes and resistance to Cry1A toxins from Bacillus thuringiensis has been found in a Plutella xylostella population. MPI linkage to Cry1A resistance had previously been reported for a Heliothis virescens population. The fact that the two populations share similar biochemical, genetic, and cross-resistance profiles of resistance suggests the occurrence of homologous resistance loci in both species.

PopulationBacterial ToxinsBacillus thuringiensisDrug ResistanceIsomeraseApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalseducationPest Control BiologicalGeneticseducation.field_of_studyMannose-6-Phosphate IsomeraseEcologyHeliothis virescensbiologyBacillus thuringiensis ToxinsMannose phosphate isomeraseParasporal bodyfungiPlutellaMannose-6-Phosphate Isomerasebiology.organism_classificationEndotoxinsIsoenzymesLepidopteraElectrophoresis Polyacrylamide GelFood ScienceBiotechnologyApplied and environmental microbiology
researchProduct