Search results for "spodoptera"

showing 10 items of 125 documents

Insecticidal activity of Vip3Aa, Vip3Ad, Vip3Ae, and Vip3Af from Bacillus thuringiensis against lepidopteran corn pests.

2012

Vip3Aa, Vip3Ad, Vip3Ae, and Vip3Af proteins from Bacillus thuringiensis were tested for their toxicity against Spodoptera frugiperda and Agrotis ipsilon. Vip3Ad was non-toxic to the two species. Vip3Ae and Vip3Af were significantly more toxic than Vip3Aa against S. frugiperda, both as protoxins and as toxins. Against A. ipsilon, Vip3Ae protoxin was more toxic than Vip3Aa and Vip3Af protoxins. Purification by metal-chelate affinity chromatography significantly affected Vip3Ae toxicity against the two insect species.

biologybusiness.industryvirusesfungiPest controlBacillus thuringiensisAgrotis ipsilonSpodopteraMothsbiology.organism_classificationMicrobiologyAffinity chromatographyBacterial ProteinsBacillus thuringiensisparasitic diseasesToxicityFall armywormAnimalsElectrophoresis Polyacrylamide GelbusinessPest Control BiologicalPolyacrylamide gel electrophoresisEcology Evolution Behavior and SystematicsJournal of invertebrate pathology
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A screening of five Bacillus thuringiensis Vip3A proteins for their activity against lepidopteran pests

2014

Five Bacillus thuringiensis Vip3A proteins (Vip3Aa, Vip3Ab, Vip3Ad, Vip3Ae and Vip3Af) and their corresponding trypsin-activated toxins were tested for their toxicity against eight lepidopteran pests: Agrotis ipsilon, Helicoverpa armigera, Mamestra brassicae, Spodoptera exigua, Spodoptera frugiperda, Spodoptera littoralis, Ostrinia nubilalis and Lobesia botrana. Toxicity was first tested at a high dose at 7 and 10. days. No major differences were found when comparing protoxins vs. trypsin-activated toxins. The proteins that were active against most of the insect species were Vip3Aa, Vip3Ae and Vip3Af, followed by Vip3Ab. Vip3Ad was non-toxic to any of the species tested. Considering the res…

biologyfungiMolecular Sequence DataAgrotis ipsilonSpodopteraHelicoverpa armigerabiology.organism_classificationLobesia botranaPlants Genetically ModifiedOstriniaMicrobiologyInsecticide ResistanceLepidopteraBacterial ProteinsBacillus thuringiensisBotanyExiguaAnimalsAmino Acid SequenceSpodoptera littoralisPest Control BiologicalEcology Evolution Behavior and Systematics
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Functional interactions between members of the REPAT family of insect pathogen-induced proteins

2012

Studies on the transcriptional response to pathogens in the insect larval gut have shown the regulation of several genes after the infection. Repat (REsponse to PAThogens) genes were first identified in Spodoptera exigua midgut as being up-regulated in response to the exposure to Bacillus thuringiensis toxins and baculovirus. Recently, new members of the REPAT family showed a constitutive up-regulation in a B. thuringiensis-resistant population. Based on a yeast two-hybrid screening, we have detected the interaction of REPAT1 with other members of the REPAT family, leading to the discovery of a new member: REPAT8. The functional role of this interaction was shown by following the changes of…

education.field_of_studybiologyPopulationMidgutSpodopteraSubcellular localizationbiology.organism_classificationmedicine.disease_causeMicrobiologyInsect ScienceBacillus thuringiensisGeneticsmedicineeducationMolecular BiologyGenePathogenEscherichia coliInsect Molecular Biology
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Herbivore-Induced Changes in Cotton Modulates Reproductive Behavior in the Moth Spodoptera littoralis

2017

Plants produce chemical defense compounds to resist herbivore attack either by repelling the herbivores or attracting natural enemies of the herbivores. We have previously shown that volatile compounds from cotton released in response to herbivory by conspecifics reduce oviposition in cotton leafworm moth Spodoptera littoralis. It remained, however, unclear whether herbivore-induced changes also affect moth pre-mating and mating behaviors. In this study we examined the effect of herbivore-induced changes in cotton on reproductive behaviors i.e., female calling, male attraction and investment, and mating behavior in S. littoralis. We found a reduction in the number of females calling i.e., f…

herbivoryreproductive behaviorpheromonal communicationrepellencylcsh:QH540-549.5fungilcsh:Evolutionlcsh:QH359-425lcsh:EcologySpodoptera littoralisplant resistanceFrontiers in Ecology and Evolution
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Hydrophobin (HFBI): a potential fusion partner for one-step purification of recombinant proteins from insect cells

2008

Hydrophobins play an important role in binding and assembly of fungal surface structures as well as in medium-air interactions. These, hydrophobic properties provide interesting possibilities when purification of macromolecules is concerned. In aqueous micellar two-phase systems, based on surfactants, the water soluble hydrophobins are concentrated inside micellar structures and, thus, distributed to defined aqueous phases. This, one-step purification is attractive particularly when large-scale production of recombinant proteins is concerned. In the present study the hydrophobin HFBI of Trichoderma reesei was expressed as an N-terminal fusion with chicken avidin in baculovirus infected inse…

hydrophobinaqueous micellar two-phase system (AMTPS)HydrophobinRecombinant Fusion ProteinsBlotting Westernfluorescence scanning microscopy (FSM)SpodopteraMicellesurfactantslaw.inventionFungal ProteinsPulmonary surfactantlawprotein purificationProtein purificationAnimalsMicellesTrichoderma reeseiTrichodermaMicroscopy Confocalbiologytechnology industry and agricultureAvidinbiology.organism_classificationBiochemistryCytoplasmRecombinant DNAbiology.proteinBaculoviridaeBiotechnologyAvidinProtein Expression and Purification
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Recurrent domestication by Lepidoptera of genes from their parasites mediated by Bracoviruses

2015

Bracoviruses are symbiotic viruses associated with tens of thousands of species of parasitic wasps that develop within the body of lepidopteran hosts and that collectively parasitize caterpillars of virtually every lepidopteran species. Viral particles are produced in the wasp ovaries and injected into host larvae with the wasp eggs. Once in the host body, the viral DNA circles enclosed in the particles integrate into lepidopteran host cell DNA. Here we show that bracovirus DNA sequences have been inserted repeatedly into lepidopteran genomes, indicating this viral DNA can also enter germline cells. The original mode of Horizontal Gene Transfer (HGT) unveiled here is based on the integrativ…

hôteanimal structuresBase Sequenceadn virallcsh:QH426-470Biodiversité et EcologieMolecular Sequence DataWaspsinsecte parasitefungiGenes InsectvirusSpodopterabracovirusBiodiversity and Ecologylcsh:GeneticsPolydnaviridaeDNA ViralAnimalsguêpelepidoptera[SDE.BE]Environmental Sciences/Biodiversity and Ecologygénomique des populationsResearch Article
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Dissimilar Regulation of Antimicrobial Proteins in the Midgut of Spodoptera exigua Larvae Challenged with Bacillus thuringiensis Toxins or Baculoviru…

2015

Antimicrobial peptides (AMPs) and lysozymes are the main effectors of the insect immune system, and they are involved in both local and systemic responses. Among local responses, midgut immune reaction plays an important role in fighting pathogens that reach the insect body through the oral route, as do many microorganisms used in pest control. Under this point of view, understanding how insects defend themselves locally during the first phases of infections caused by food-borne pathogens is important to further improve microbial control strategies. In the present study, we analyzed the transcriptional response of AMPs and lysozymes in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae…

media_common.quotation_subjectAntimicrobial peptidesMolecular Sequence DataBacillus thuringiensislcsh:MedicineInsectSpodopteraSpodopteraMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaHemolymphAnimalsAmino Acid SequencePest Control Biologicallcsh:SciencePhylogenymedia_commonMultidisciplinarybiologyBacillus thuringiensis ToxinsSequence Homology Amino AcidMonophenol Monooxygenasefungilcsh:RMidgutbiology.organism_classificationEndotoxinsSettore AGR/11 - ENTOMOLOGIA GENERALE E APPLICATALarvaNoctuidaeInsect ProteinsMuramidaselcsh:QBaculoviridaeDigestive SystemAntimicrobial Cationic PeptidesResearch ArticlePLoS ONE
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Domains of the E1 Protein of Human Papillomavirus Type 33 Involved in Binding to the E2 Protein

1996

Papillomavirus E1 and E2 proteins are essential for the initiation of viral DNA replication. We have now analyzed the interaction of E1 and E2 of human papillomavirus type 33, which is associated with cervical carcinoma. When synthesized in insect cells using the baculovirus expression system, the E1 and E2 proteins interacted efficiently at 4 degree. A monoclonal antibody recognizing E1 amino acids 584--600 inhibited the binding of E2 and vice versa, indicating that these amino acids are involved in E2 binding. To confirm this result, a mutational analysis of E1 was performed. The E2 binding activity of E1 deletion and point mutant proteins was assayed using glutathione S-transferase E1 fu…

medicine.drug_classRecombinant Fusion ProteinsMolecular Sequence DataContext (language use)BiologySpodopteraMonoclonal antibodyAntibodies ViralCell Linechemistry.chemical_compoundMiceVirologymedicineTumor Cells CulturedAnimalsHumansPoint MutationPapillomaviridaeDNA PrimersGlutathione TransferaseSequence Deletionchemistry.chemical_classificationMice Inbred BALB CBase SequencePoint mutationTemperatureAntibodies MonoclonalGlutathioneOncogene Proteins ViralFusion proteinMolecular biologyIn vitroAmino acidchemistryEpitope MappingBinding domainProtein BindingVirology
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Regulation of the human bradykinin B2 receptor expressed in sf21 insect cells: A possible role for tyrosine kinases

2000

The functional regulation of the human bradykinin B2 receptor expressed in sf21 cells was studied. Human bradykinin B2 receptors were immunodetected as a band of 75–80 kDa in membranes from recombinant baculovirus-infected cells and visualized at the plasma membrane, by confocal microscopy, using an antibody against an epitope from its second extracellular loop. B2 receptors, detected in membranes by [3H-bradykinin] binding, showed a Kd of 0.66 nmol/L and an expression level of 2.57 pmol/mg of protein at 54 h postinfection. In these cells, bradykinin induced a transient increase of intracellular calcium ([Ca2+]i) in fura 2-AM loaded sf21 cells, and promoted [35S]-GTPγS binding to membranes.…

medicine.medical_specialtyReceptor Bradykinin B2G proteinGene Expressionchemistry.chemical_elementBradykininReceptors Cell SurfaceSpodopteraCalciumBiologyBradykininBiochemistryCalcium in biologychemistry.chemical_compoundGTP-Binding ProteinsInternal medicineHomologous desensitizationmedicineAnimalsHumansPhosphorylationBradykinin receptorPhosphoamino AcidsReceptorOctopamineMolecular BiologyBradykinin Receptor AntagonistsCells CulturedMicroscopy ConfocalReceptors BradykininCell MembraneCell BiologyProtein-Tyrosine KinasesTyrphostinsGenisteinMolecular biologyRecombinant ProteinsEndocrinologychemistryGuanosine 5'-O-(3-Thiotriphosphate)ThapsigarginCalciumBaculoviridaeTyrosine kinaseProtein BindingJournal of Cellular Biochemistry
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The Mighty Bt: Interactions between pests and pesticidal proteins from Bacillus thuringiensis

2022

Bacillus thuringiensis, también conocida como “Bt”, es una bacteria gram positiva que forma endosporas. Se trata de un organismo ubicuo, aunque se encuentra principalmente en el suelo o en ambientes con alta presencia de insectos. Fue aislada por primera vez en 1901 por el bacteriólogo Shigetane Ishiwata en muestras de intestino de gusanos de seda (Bombyx mori) infectados y fue apodada como “Sottokin- Bacillus” (“Bacilo de muerte súbita”) por la muerte que causaba cuando era ingerida por larvas de gusanos de seda. Pocos años después, el biólogo Ernst Berliner aisló B. thuringiensis de crisálidas de polilla mediterránea de la harina (Ephestia kuehniella) infectadas con esta bacteria en la pr…

ostriniathuringiensisUNESCO::CIENCIAS DE LA VIDAspodopteratoxinas btheliothis:CIENCIAS DE LA VIDA [UNESCO]
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