Search results for "Spodoptera"

showing 10 items of 125 documents

Interaction of Bacillus thuringiensis Cry1 and Vip3A Proteins with Spodoptera frugiperda Midgut Binding Sites

2009

ABSTRACT Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa competed for those of Vip3Af.

Bioquímicaanimal structuresBiotecnologia agrícolaBacillus thuringiensisPlasma protein bindingSpodopteraSpodopteraHemolysin ProteinsApplied Microbiology and BiotechnologyProtein–protein interactionMicrobiologyLethal Dose 50Hemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteBacillus thuringiensis ToxinsEcologybiologyfungifood and beveragesMidgutbiology.organism_classificationBacillalesEndotoxinsGastrointestinal TractBiochemistryLarvasense organsProteïnesProtein BindingFood ScienceBiotechnologyApplied and Environmental Microbiology
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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
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Lyophilization of lepidopteran midguts: a preserving method for Bacillus thuringiensis toxin binding studies

2004

Binding assays with brush border membrane vesicles (BBMV) from insect midguts are commonly used in the study of the interactions between Bacillus thuringiensis Cry toxins and their receptors. Collaboration between laboratories often require that frozen insect samples are sent in dry ice. Because of customs restrictions and delays, sample thawing is always a risk and often the biological material becomes ruined during shipping. We have tested lyophilization as an alternative method for preserving insect midguts for binding studies with B. thuringiensis Cry toxins. For this purpose, BBMV were prepared from both frozen and lyophilized midguts from three lepidopteran species: Spodoptera exigua,…

Brush borderBacillus thuringiensisReceptors Cell SurfaceHelicoverpa armigeraSpodopteramedicine.disease_causeHost-Parasite InteractionsMicrobiologyBacterial ProteinsBacillus thuringiensisExiguamedicineAnimalsBinding sitePest Control BiologicalEcology Evolution Behavior and SystematicsCryopreservationMicrovillibiologyToxinfungibiology.organism_classificationLepidopteraFreeze DryingBiochemistryManduca sextaInsect ProteinsDigestive SystemJournal of Invertebrate Pathology
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In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by 125 I Radiolabeling

2014

ABSTRACT Bacillus thuringiensis vegetative insecticidal proteins (Vip3A) have been recently introduced in important crops as a strategy to delay the emerging resistance to the existing Cry toxins. The mode of action of Vip3A proteins has been studied in Spodoptera frugiperda with the aim of characterizing their binding to the insect midgut. Immunofluorescence histological localization of Vip3Aa in the midgut of intoxicated larvae showed that Vip3Aa bound to the brush border membrane along the entire apical surface. The presence of fluorescence in the cytoplasm of epithelial cells seems to suggest internalization of Vip3Aa or a fragment of it. Successful radiolabeling and optimization of the…

Brush bordermedia_common.quotation_subjectSpodopteraSpodopteraHemolysin ProteinsBinding CompetitiveApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsTrypsinBinding siteInternalizationmedia_commonBinding SitesBacillus thuringiensis ToxinsMicrovilliEcologybiologyfungiEpithelial CellsMidgutHydrogen-Ion Concentrationbiology.organism_classificationEndotoxinsBiochemistryCytoplasmIsotope LabelingLarvaDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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Midgut microbiota and host immunocompetence underlie Bacillus thuringiensis killing mechanism

2016

Bacillus thuringiensis is a widely used bacterial entomopathogen producing insecticidal toxins, some of which are expressed in insect-resistant transgenic crops. Surprisingly, the killing mechanism of B. thuringiensis remains controversial. In particular, the importance of the septicemia induced by the host midgut microbiota is still debated as a result of the lack of experimental evidence obtained without drastic manipulation of the midgut and its content. Here this key issue is addressed by RNAi-mediated silencing of an immune gene in a lepidopteran host Spodoptera littoralis, leaving the midgut microbiota unaltered. The resulting cellular immunosuppression was characterized by a reduced …

Crops Agricultural0301 basic medicineHemocytesSerratiaBacillus thuringiensisSpodopteraSerratiaMicrobiologyHemolysin Proteins03 medical and health sciencesBacterial ProteinsInsect-pathogen interactionImmunityBacillus thuringiensisAnimalsPest Control Biologicalbioinsecticide | insect-pathogen interactions | insect biocontrol | pore-forming toxins | immunitySpodoptera littoralisRNA Double-StrandedClostridiumImmunosuppression TherapyPore-forming toxinMultidisciplinaryBacillus thuringiensis ToxinsInsect biocontrolbiologyHost (biology)MicrobiotafungiImmunityMidgutBiological Sciencesbiology.organism_classificationImmunity InnateBioinsecticideEndotoxinsIntestines030104 developmental biologyGene Expression RegulationLarvaPore-forming toxinInsect ProteinsRNA InterferenceImmunocompetenceProceedings of the National Academy of Sciences
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Two genomes of highly polyphagous lepidopteran pests (Spodoptera frugiperda, Noctuidae) with different host-plant ranges

2017

International audience; Emergence of polyphagous herbivorous insects entails significant adaptation to recognize, detoxify and digest a variety of host-plants. Despite of its biological and practical importance - since insects eat 20% of crops - no exhaustive analysis of gene repertoires required for adaptations in generalist insect herbivores has previously been performed. The noctuid moth Spodoptera frugiperda ranks as one of the world’s worst agricultural pests. This insect is polyphagous while the majority of other lepidopteran herbivores are specialist. It consists of two morphologically indistinguishable strains (“C” and “R”) that have different host plant ranges. To describe the evol…

Crops AgriculturalGenome Insectlcsh:Rfungilcsh:MedicineSpodopteraAdaptation PhysiologicalArticleSpecies SpecificityLarvaAnimalslcsh:QHerbivory[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]lcsh:Science[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]
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Improvement of baculovirus as protein expression vector and as biopesticide by CRISPR/Cas9 editing

2019

The clustered regularly interspaced short palindromic repeats (CRISPR) system?associated Cas9 endonuclease is a molecular tool that enables specific sequence editing with high efficiency. In this study, we have explored the use of CRISPR/Cas9 system for the engineering of baculovirus. We have shown that the delivering of Cas9-single guide RNA ribonucleoprotein (RNP) complex with or without DNA repair template into Sf21 insect cells through lipofection might be efficient to produce knockouts as well as knock-ins into the baculovirus. To evaluate potential application of our CRISPR/Cas9 method to improve baculovirus as protein expression vector and as biopesticide, we attempted to knockout se…

DNA repairvirusesBACULOVIRUSGenetic VectorsBioengineeringComputational biologyGenome ViralINGENIERÍAS Y TECNOLOGÍASBiologySpodopteraApplied Microbiology and BiotechnologyGenomelaw.inventionBiotecnología Industrial03 medical and health sciencesGenome editingGENOME EDITINGlawKNOCK-INSf9 CellsCRISPRAnimalsVector (molecular biology)Guide RNANUCLEOPOLYHEDROVIRUSPest Control BiologicalGeneCRISPR/CAS9030304 developmental biologyRibonucleoproteinGene Editing0303 health sciencesExpression vector030306 microbiologyCas93. Good healthKNOCKOUTRecombinant DNACRISPR-Cas SystemsBaculoviridaeBiotechnology
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Overexpression and functional characterization of kinin receptors reveal subtype-specific phosphorylation.

1999

G protein-coupled receptors such as the receptors for bradykinin are present in low copy numbers in most natural cells. To overcome the problems associated with the analysis of these receptors at the protein level, we used highly efficient expression systems such as the baculovirus/insect cell system. However, the structural and functional statuses of recombinant receptors have often remained elusive. We have expressed the two types of human kinin receptors, B1 and B2, in Sf9 cells. Both receptors are found on the surface of infected cells where they display the same pharmacological profiles as their cognate receptors of native cells. The functional analysis of kinin receptors coupled to th…

DNA ComplementaryReceptor Bradykinin B2ImmunoprecipitationSf9SpodopteraBradykininReceptor Bradykinin B1TransfectionBiochemistryAnimalsHumansBinding siteCloning MolecularPhosphorylationReceptorMicroscopy ConfocalKinaseChemistryReceptors BradykininCell MembraneKininMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphorylationCalciumIntracellularBiochemistry
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Critical Domains in the Specific Binding of Radiolabeled Vip3Af Insecticidal Protein to Brush Border Membrane Vesicles from Spodoptera spp. and Cultu…

2021

Vegetative insecticidal proteins (Vip3) from Bacillus thuringiensis have been used, in combination with Cry proteins, to better control insect pests and as a strategy to delay the evolution of resistance to Cry proteins in Bt crops (crops protected from insect attack by the expression of proteins from B. thuringiensis). In this study, we have set up the conditions to analyze the specific binding of 125I-Vip3Af to Spodoptera frugiperda and Spodoptera exigua brush border membrane vesicles (BBMV). Heterologous competition binding experiments revealed that Vip3Aa shares the same binding sites with Vip3Af, but Vip3Ca does not recognize all of them. As expected, Cry1Ac and Cry1F did not compete f…

EcologyBrush borderbiologyChemistryfungiSpodopterabiology.organism_classificationApplied Microbiology and BiotechnologyEpitopeProtein structureCry1AcBiochemistryBacillus thuringiensisBinding siteFood ScienceBiotechnologySf21Applied and Environmental Microbiology
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Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis

2022

12 p.-4 fig.-2 tab.

EndotoxinsInsecticidesBacterial ProteinsBacillus thuringiensisAnimalsTrypsinBioengineeringSpodopteraProteïnesBiotecnologiaApplied Microbiology and BiotechnologyBiochemistryBiotechnology
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