Search results for "Spodoptera"

showing 10 items of 125 documents

A novel baculovirus-derived promoter with high activity in the baculovirus expression system

2016

The baculovirus expression vector system (BEVS) has been widely used to produce a large number of recombinant proteins, and is becoming one of the most powerful, robust, and cost-effective systems for the production of eukaryotic proteins. Nevertheless, as in any other protein expression system, it is important to improve the production capabilities of this vector. The orf46 viral gene was identified among the most highly abundant sequences in the transcriptome of Spodoptera exigua larvae infected with its native baculovirus, the S. exigua multiple nucleopolyhedrovirus (SeMNPV). Different sequences upstream of the orf46 gene were cloned, and their promoter activities were tested by the expr…

0301 basic medicineInsect virusviruseslcsh:MedicineSpodopteraGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesNucleopolyhedrovirusVirologyExiguaPolyhedrinInsect virusGeneMolecular BiologySf21biologyGeneral Neurosciencelcsh:RfungiPromoterGeneral Medicinebiology.organism_classificationMolecular biologyAutographa californica030104 developmental biologyProtein expressionGeneral Agricultural and Biological SciencesBiotechnologyPeerJ
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Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein.

2016

The Vip3Ca protein, discovered in a screening of Spanish collections of Bacillus thuringiensis, was known to be toxic to Chrysodeixis chalcites, Mamestra brassicae and Trichoplusia ni. In the present study, its activity has been tested with additional insect species and we found that Cydia pomonella is moderately susceptible to this protein. Vip3Ca (of approximately 90 kDa) was processed to an approximately 70 kDa protein when incubated with midgut juice in all tested species. The kinetics of proteolysis correlated with the susceptibility of the insect species to Vip3Ca. The activation was faster to slower in the following order: M. brassicae (susceptible), Spodoptera littoralis (moderately…

0301 basic medicineInsecticides030106 microbiologyInsect pest controlAgrotis ipsilonVegetative insecticidal proteinsMothsmedicine.disease_causeMicrobiologyCiencias BiológicasInsecticide Resistance03 medical and health sciencesBiología Celular MicrobiologíaBacterial ProteinsBacillus thuringiensisBotanyTrichoplusiamedicineAnimalsSpodoptera littoralisPest Control BiologicalEcology Evolution Behavior and SystematicsHistological localizationbiologyToxinfungiVEGETATIVE INSECTICIDAL PROTEINSMidgutBioinsecticidesApical membranebiology.organism_classificationCROP PROTECTIONChrysodeixis chalcitesBIOINSECTICIDES030104 developmental biologyCrop protectionINSECT PEST CONTROLHISTOLOGICAL LOCALIZATIONCIENCIAS NATURALES Y EXACTASJournal of invertebrate pathology
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Susceptibility, mechanisms of response and resistance to Bacillus thuringiensis toxins in Spodoptera spp.

2016

Bioinsecticides based on Bacillus thuringiensis have long been used as an alternative to synthetic insecticides to control insect pests. In this review, we focus on insects of the genus Spodoptera, including relevant polyphagous species that are primary and secondary pests of many crops, and how B. thuringiensis toxins can be used for Spodoptera spp. pest management. We summarize the main findings related to susceptibility, midgut binding specificity, mechanisms of response and resistance of this insect genus to B. thuringiensis toxins.

0301 basic medicineIntegrated pest managementResistance (ecology)media_common.quotation_subjectBacterial ToxinsfungiBacillus thuringiensisfood and beveragesMidgutInsectSpodopteraBiologySpodopterabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciences030104 developmental biologyInsect ScienceBacillus thuringiensisBotanyAnimalsEcology Evolution Behavior and Systematicsmedia_commonCurrent Opinion in Insect Science
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Critical amino acids for the insecticidal activity of Vip3Af from Bacillus thuringiensis: Inference on structural aspects

2018

AbstractVip3 vegetative insecticidal proteins from Bacillus thuringiensis are an important tool for crop protection against caterpillar pests in IPM strategies. While there is wide consensus on their general mode of action, the details of their mode of action are not completely elucidated and their structure remains unknown. In this work the alanine scanning technique was performed on 558 out of the total of 788 amino acids of the Vip3Af1 protein. From the 558 residue substitutions, 19 impaired protein expression and other 19 substitutions severely compromised the insecticidal activity against Spodoptera frugiperda. The latter 19 substitutions mainly clustered in two regions of the protein …

0301 basic medicineModels MolecularAmino Acid MotifsBacillus thuringiensislcsh:MedicineSpodopteraSpodopteraArticle03 medical and health sciencesProtein structureProtein sequencingBacterial ProteinsBacillus thuringiensisAnimalsMode of actionlcsh:Sciencechemistry.chemical_classificationMultidisciplinaryAlaninebiologyProtein Stabilitylcsh:RAlanine scanningbiology.organism_classificationProtein tertiary structureAmino acidProtein Structure TertiaryMolecular Docking Simulation030104 developmental biologychemistryBiochemistryAmino Acid Substitutionlcsh:QScientific Reports
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Artefactual band patterns by SDS-PAGE of the Vip3Af protein in the presence of proteases mask the extremely high stability of this protein.

2018

Abstract Vip3 proteins are secretable proteins from Bacillus thuringiensis with important characteristics for the microbiological control of agricultural pests. The exact details of their mode of action are yet to be disclosed and the crystallographic structure is still unknown. Vip3 proteins are expressed as protoxins that have to be activated by the insect gut proteases. A previous study on the peptidase processing of Vip3Aa revealed that the protoxin produced artefactual band patterns by SDS-PAGE due to the differential stability of this protein and the peptidases to SDS and heating (Bel et al., 2017 Toxins 9:131). To determine whether this phenomenon also applies to other Vip3A proteins…

0301 basic medicineProteases030106 microbiologyBacillus thuringiensisSpodopteraSpodopteraCleavage (embryo)Biochemistry03 medical and health sciencesBacterial ProteinsStructural BiologyBacillus thuringiensismedicineAnimalsMode of actionMolecular BiologyPolyacrylamide gel electrophoresisbiologyChemistryProtein StabilityfungiMidgutGeneral Medicinebiology.organism_classificationTrypsin030104 developmental biologyBiochemistryInsect ProteinsElectrophoresis Polyacrylamide Gelmedicine.drugPeptide HydrolasesInternational journal of biological macromolecules
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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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High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae)

2017

Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensors for capturing and identifying bacterial species. In this work, three C-type lectins from the Lepidoptera Spodoptera exigua were produced as recombinant proteins and their bacterial agglutination properties were characterized. The lowest protein concentration producing bacterial agglutination against a panel of different Gram+ an…

0301 basic medicineagglutinationlcsh:BiotechnologyClinical BiochemistryMicrobial Sensitivity TestsSpodopteraSpodopteraC-type lectin; agglutination; CRD; bacterial detection; <i>E. coli</i>ArticleMicrobiologylaw.inventionbacterial detectionLepidoptera genitalia03 medical and health sciences0302 clinical medicinelawC-type lectinlcsh:TP248.13-248.65Agglutination TestsExiguaEscherichia coliAnimalsLectins C-TypeAmino Acid SequenceConserved SequencePhylogenybiologyE. coliCRDGeneral Medicinebiology.organism_classificationImmunity InnateC-type lectinAgglutination (biology)030104 developmental biologyRecombinant DNANoctuidaeInsect ProteinsProtein concentration030215 immunologybiotechnology
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MultiBacTAG-Genetic Code Expansion Using the Baculovirus Expression System in Sf21 Cells

2018

The combination of genetic code expansion (GCE) and baculovirus-based protein expression in Spodoptera frugiperda cells is a powerful tool to express multiprotein complexes with site-specifically introduced noncanonical amino acids. This protocol describes the integration of synthetase and tRNA gene indispensable for GCE into the backbone of the Bacmid, the Tn7-mediated transposition of various genes of interest, as well as the final expression of protein using the MultiBacTAG system with different noncanonical amino acids.

0301 basic medicinechemistry.chemical_classificationbiologyChemistryvirusesBaculovirus expressionComputational biologySpodopteraGenetic codebiology.organism_classificationAmino acidTransposition (music)03 medical and health sciences030104 developmental biologyTransfer RNAGeneSf21
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Extracellular Domains of the Bradykinin B2 Receptor Involved in Ligand Binding and Agonist Sensing Defined by Anti-peptide Antibodies

1996

Many of the physiological functions of bradykinin are mediated via the B2 receptor. Little is known about binding sites for bradykinin on the receptor. Therefore, antisera against peptides derived from the putative extracellular domains of the B2 receptor were raised. The antibodies strongly reacted with their corresponding antigens and cross-reacted both with the denatured and the native B2 receptor. Affinity-purified antibodies to the various extracellular domains were used to probe the contact sites between the receptor and its agonist, bradykinin or its antagonist HOE140. Antibodies to extracellular domain 3 (second loop) efficiently interfered, in a concentration-dependent manner, with…

AgonistReceptor Bradykinin B2medicine.drug_classMolecular Sequence DataFluorescent Antibody TechniqueCHO CellsSpodopteraBradykininTransfectionBiochemistryAntibodiesProtein Structure SecondaryCell LineCricetinaeExtracellularmedicineAnimalsHumansAmino Acid SequenceBradykinin receptorBinding siteReceptorMolecular BiologyChemistryReceptors BradykininCell MembraneCell BiologyMolecular biologyPeptide FragmentsRecombinant ProteinsRatsCell biologyModels StructuralEctodomainCompetitive antagonistIntracellularJournal of Biological Chemistry
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Subtype-Specific Desensitization of Human Endothelin ETA and ETB Receptors Reflects Differential Receptor Phosphorylation

1997

Endothelins regulate blood pressure in mammals through G protein-coupled receptors. Two receptor subtypes, ETA and ETB, exist which differ by their agonist profiles. Here we show subtype-specific differences in the inactivation of these endothelin receptors. Using a modified inositol phosphate accumulation assay, we found that stimulation of ETA by endothelin-1 results in sustained activation of the subtype, retaining >30% of its initial activity even 20 min after agonist administration, whereas the ETB rapidly deactivated after agonist stimulation, losing >80% of its initial activity within 5 min after endothelin application. The discrepancy in receptor inactivation is reflected by subtype…

Agonistmedicine.hormonemedicine.medical_specialtyEndothelin receptor type Amedicine.drug_classmedia_common.quotation_subjectStimulationCHO CellsPalmitic AcidsSpodopteraLigandsBiochemistryEndothelinsCricetinaeInternal medicinemedicineAnimalsHumansPhosphorylationInternalizationReceptorProtein Kinase Cmedia_commonReceptors EndothelinChemistryImmune Serarespiratory systemReceptor Endothelin AReceptor Endothelin BKineticsEndocrinologycardiovascular systemPhosphorylationEndothelin receptorcirculatory and respiratory physiologyBiochemistry
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