Search results for "binding"

showing 10 items of 3896 documents

Binding analyses of Cry1Ab and Cry1Ac with membrane vesicles from Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis.

2004

The binding properties of Bacillus thuringiensis toxins to brush border membrane vesicles of Dipel-resistant and -susceptible Ostrinia nubilalis larvae were compared using ligand-toxin immunoblot analysis, surface plasmon resonance (SPR), and radiolabeled toxin binding assays. In ligand-toxin immunoblot analysis, the number of Cry1Ab or Cry1Ac toxin binding proteins and the relative toxin binding intensity were similar in vesicles from resistant and susceptible larvae. Surface plasmon resonance with immobilized activated Cry1Ab toxin indicated that there were no significant differences in binding with fluid-phase vesicles from resistant and susceptible larvae. Homologous competition assays …

InsectaTime FactorsBrush borderBacterial ToxinsImmunoblottingBiophysicsBacillus thuringiensisReceptors Cell SurfacePlasma protein bindingBiologyMothsmedicine.disease_causeLigandsBiochemistryBinding CompetitiveCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding sitePest Control BiologicalMolecular BiologyBinding SitesBacillus thuringiensis ToxinsDose-Response Relationship DrugMicrovilliToxinVesiclefungiCell Membranefood and beveragesCell BiologySurface Plasmon Resonancebiology.organism_classificationMolecular biologyEndotoxinsKineticsmedicine.anatomical_structureCry1AcBiochemistryInsect ProteinsProtein BindingBiochemical and biophysical research communications
researchProduct

Lack of Detrimental Effects of Bacillus thuringiensis Cry Toxins on the Insect Predator Chrysoperla carnea : a Toxicological, Histopathological, and …

2006

ABSTRACT The effect of Cry proteins of Bacillus thuringiensis on the green lacewing ( Chrysoperla carnea ) was studied by using a holistic approach which consisted of independent, complementary experimental strategies. Tritrophic experiments were performed, in which lacewing larvae were fed Helicoverpa armigera larvae reared on Cry1Ac, Cry1Ab, or Cry2Ab toxins. In complementary experiments, a predetermined amount of purified Cry1Ac was directly fed to lacewing larvae. In both experiments no effects on prey utilization or fitness parameters were found. Since binding to the midgut is an indispensable step for toxicity of Cry proteins to known target insects, we hypothesized that specific bind…

InsectanoctuidaeBacterial ToxinsBacillus thuringiensisHelicoverpa armigeraApplied Microbiology and BiotechnologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyExiguaInvertebrate MicrobiologyAnimalsBioassaycrystal proteinsPest Control BiologicalChrysoperla carnealarval midgutBacillus thuringiensis ToxinsMicrovilliEcologybiologybinding-sitesfungitoxicityMidgutbiology.organism_classificationspodoptera-exiguaEndotoxinsPRI BioscienceBiochemistryCry1Acmaize expressing cry1abNoctuidaeDigestive Systemborder membrane-vesicleshelicoverpa-armigera lepidopteraFood ScienceBiotechnologyresistant transgenic plants
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

Different mechanisms of resistance to Bacillus thuringiensis toxins in the indianmeal moth.

2001

ABSTRACT Susceptibility to protoxin and toxin forms of Cry1Ab and the binding of 125 I-labeled Cry1Ab and Cry1Ac has been examined in three Plodia interpunctella colonies, one susceptible (688 s ) and two resistant (198 r and Dpl r ) to Bacillus thuringiensis . Toxicological studies showed that the 198 r colony was 11-fold more resistant to Cry1Ab protoxin than to Cry1Ab activated toxin, whereas the Dpl r colony was 4-fold more resistant to protoxin versus toxin. Binding results with 125 I-labeled toxins indicated the occurrence of two different binding sites for Cry1Ab in the susceptible insects, one of them shared with Cry1Ac. Cry1Ab binding was found to be altered in insects from both re…

InsecticidesBacterial ToxinsBacillus thuringiensisMothsmedicine.disease_causeApplied Microbiology and BiotechnologyBinding CompetitiveMicrobiologyToxicologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineInvertebrate MicrobiologyAnimalsBinding siteProtein PrecursorsLarvaBacillaceaeEcologybiologyBacillus thuringiensis ToxinsMicrovilliToxinParasporal bodyfungibiology.organism_classificationBacillalesEndotoxinsCry1AcLarvaFood ScienceBiotechnologyApplied and environmental microbiology
researchProduct

Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera: Yponomeutidae)

2009

The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larv…

InsecticidesBinding SitesBacillus thuringiensis Toxinsbiologymedia_common.quotation_subjectfungiBiological pest controlInsectMothsPrays oleaebiology.organism_classificationEndotoxinsLepidoptera genitaliaHemolysin ProteinsBiopesticideBacterial ProteinsCry1AcLarvaBacillus thuringiensisBotanyAnimalsPEST analysisPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commonJournal of Invertebrate Pathology
researchProduct

The Rapid Evolution of Resistance to Vip3Aa Insecticidal Protein in Mythimna separata (Walker) Is Not Related to Altered Binding to Midgut Receptors

2021

Laboratory selection for resistance of field populations is a well-known and useful tool to understand the potential of insect populations to evolve resistance to insecticides. It provides us with estimates of the frequency of resistance alleles and allows us to study the mechanisms by which insects developed resistance to shed light on the mode of action and optimize resistance management strategies. Here, a field population of Mythimna separata was subjected to laboratory selection with either Vip3Aa, Cry1Ab, or Cry1F insecticidal proteins from Bacillus thuringiensis. The population rapidly evolved resistance to Vip3Aa reaching, after eight generations, a level of >3061-fold resistance…

InsecticidesHealth Toxicology and Mutagenesismedia_common.quotation_subjectPopulationBacillus thuringiensisInsectMothsToxicologyInsecticide Resistance03 medical and health sciencesMythimna separataHemolysin ProteinsBacterial ProteinsBacillus thuringiensis<i>Bacillus thuringiensis</i>cross resistanceBt toxinsAnimalseducationCross-resistance030304 developmental biologymedia_commonGenetics0303 health sciencesLarvaeducation.field_of_studybiologyResistance (ecology)Bacillus thuringiensis Toxins030306 microbiologyCommunicationfungiRMidgutbiology.organism_classificationEndotoxinsLarvaoriental armywormMedicineProtein BindingToxins
researchProduct

Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors a…

1995

The promoter region and transcriptional regulation of the nuoA-N gene locus encoding the proton-translocating NADH:quinone oxidoreductase was analysed. A 560 bp intergenic region upstream of the nuo locus was followed by a gene (designated lrhA for LysR homologue A) coding for a gene regulator similar to those of the LysR family. Disruption of lrhA did not affect growth (respiratory or non-respiratory) or expression of nuo significantly. Transcriptional regulation of nuo by electron acceptors, electron donors and the transcriptional regulators ArcA, FNR, NarL and NarP, and by IHF (integration host factor) was studied with protein and operon fusions containing the promoter region up to base …

Integration Host FactorsIron-Sulfur ProteinsTranscription GeneticOperonMolecular Sequence DataRepressorLocus (genetics)medicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsOperonmedicineTranscriptional regulationEscherichia coliAmino Acid SequencePromoter Regions GeneticMolecular BiologyEscherichia coliGenebiologyBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsNADH dehydrogenasePromoterNADH DehydrogenaseGene Expression Regulation BacterialMolecular biologyAerobiosisDNA-Binding ProteinsRepressor ProteinsBiochemistrybiology.proteinbacteriaProtonsSequence AlignmentBacterial Outer Membrane ProteinsTranscription FactorsMolecular microbiology
researchProduct

The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix

2004

Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal tissues suggested that based on their distribution all four collagen receptor integrins, namely alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1, are possible receptors for collagen IX. Furthermore primary chondrocytes and chondrosarcoma cells express the four integrins simultaneously. Chondrosarcoma cells, as well as Chinese hamster ovary cells transfected to express alpha1beta1, alpha2beta1, or alpha10beta1 integrin as their only collage…

Integrin alpha1Integrin alpha2LigandsPolymerase Chain ReactionBiochemistryCollagen receptorMiceCricetinaeReceptorbiologyReverse Transcriptase Polymerase Chain ReactionChemistryChinese hamster ovary cellRecombinant ProteinsCell biologyBiochemistryCollagenIntegrin alpha ChainsProtein BindingMolecular Sequence DataIntegrinChondrosarcomaCHO CellsFibrilCollagen Type IXCell LineChondrocytesMicroscopy Electron TransmissionCell Line TumorCell AdhesionEscherichia coliAnimalsHumansImmunoprecipitationAmino Acid SequenceRNA MessengerBinding siteCell adhesionMolecular BiologyBinding SitesSequence Homology Amino AcidCell BiologyProtein Structure TertiaryRatsMicroscopy ElectronCollagen type I alpha 1CartilageMutationMutagenesis Site-Directedbiology.proteinRNAPeptidesJournal of Biological Chemistry
researchProduct

MMGBSA As a Tool To Understand the Binding Affinities of Filamin–Peptide Interactions

2013

Filamins (FLN) are large dimeric proteins that cross-link actin and work as important scaffolds in human cells. FLNs consist of an N-terminal actin-binding domain followed by 24 immunoglobulin-like domains (FLN1-24). FLN domains are divided into four subgroups based on their amino acid sequences. One of these subgroups, including domains 4, 9, 12, 17, 19, 21, and 23, shares a similar ligand-binding site between the β strands C and D. Several proteins, such as integrins β2 and β7, glycoprotein Ibα (GPIbα), and migfilin, have been shown to bind to this site. Here, we computationally estimated the binding free energies of filamin A (FLNa) subunits with bound peptides using the molecular mechan…

Integrin beta ChainsFilaminsGeneral Chemical EngineeringIntegrinPeptidePlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesBiologyLigandsFilaminta3111Protein Structure SecondaryProtein structureProtein Interaction MappingHumansFLNAProtein Interaction Domains and MotifsBinding siteta116chemistry.chemical_classificationBinding Sitesta1182General ChemistryComputer Science ApplicationsAmino acidCytoskeletal ProteinsCrystallographyPlatelet Glycoprotein GPIb-IX ComplexchemistryCD18 AntigensBiophysicsbiology.proteinThermodynamicsPeptidesCell Adhesion MoleculesAlgorithmsProtein BindingJournal of Chemical Information and Modeling
researchProduct

Pro-prion Binds Filamin A, Facilitating Its Interaction with Integrin β1, and Contributes to Melanomagenesis

2010

Filamin A (FLNA) is an integrator of cell mechanics and signaling. The spreading and migration observed in FLNA sufficient A7 melanoma cells but not in the parental FLNA deficient M2 cells have been attributed to FLNA. In A7 and M2 cells, the normal prion (PrP) exists as pro-PrP, retaining its glycosylphosphatidyl-inositol (GPI) anchor peptide signal sequence (GPI-PSS). The GPI-PSS of PrP has a FLNA binding motif and binds FLNA. Reducing PrP expression in A7 cells alters the spatial distribution of FLNA and organization of actin and diminishes cell spreading and migration. Integrin β1 also binds FLNA. In A7 cells, FLNA, PrP, and integrin β1 exist as two independent, yet functionally linked,…

Integrin beta ChainsGlycosylphosphatidylinositolsPrionsFilaminsanimal diseasesAmino Acid MotifsIntegrinPlasma protein bindingBiologyFilaminBiochemistryCell membraneContractile ProteinsCell MovementCell Line TumormedicineHumansFLNACytoskeletonMelanomaMolecular BiologyActinMicrofilament ProteinsCell Biologynervous system diseasesCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurebiology.proteinCancer researchSignal transductionProtein BindingJournal of Biological Chemistry
researchProduct