Search results for "Helicoverpa"

showing 10 items of 20 documents

Downregulation of a Chitin Deacetylase-Like Protein in Response to Baculovirus Infection and Its Application for Improving Baculovirus Infectivity

2009

ABSTRACT Several expressed sequence tags (ESTs) with homology to chitin deacetylase-like protein (CDA) were selected from a group of Helicoverpa armigera genes whose expression changed after infection with H. armigera single nucleopolyhedrovirus (HearNPV). Some of these ESTs coded for a midgut protein containing a chitin deacetylase domain (CDAD). The expressed protein, HaCDA5a, did not show chitin deacetylase activity, but it showed a strong affinity for binding to chitin. Sequence analysis showed the lack of any chitin binding domain, described for all currently known peritrophic membrane (PM) proteins. HaCDA5a has previously been detected in the H. armigera PM. Such localization, togethe…

BaculoviridaeExpressed Sequence TagvirusesMolecular Sequence DataImmunologyDown-RegulationChitinMothMothsSpodopteraSpodopteraHelicoverpa armigeraMicrobiologyAmidohydrolasesMicrobiologychemistry.chemical_compoundChitinDownregulation and upregulationChitin bindingVirologyAnimalsAmino Acid SequenceCells CulturedPhylogenyOligonucleotide Array Sequence AnalysisExpressed Sequence TagsAmidohydrolaseInfectivitySequence Homology Amino AcidbiologyAnimalOligonucleotide Array Sequence AnalysiGene Expression ProfilingfungiSequence Analysis DNAbiology.organism_classificationVirologyIsoenzymeGenome Replication and Regulation of Viral Gene ExpressionChitin deacetylaseIsoenzymeschemistryInsect ScienceBaculoviridaeSequence AlignmentJournal of Virology
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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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Binding Site Alteration Is Responsible for Field-Isolated Resistance to Bacillus thuringiensis Cry2A Insecticidal Proteins in Two Helicoverpa Species

2010

Background Evolution of resistance by target pests is the main threat to the long-term efficacy of crops expressing Bacillus thuringiensis (Bt) insecticidal proteins. Cry2 proteins play a pivotal role in current Bt spray formulations and transgenic crops and they complement Cry1A proteins because of their different mode of action. Their presence is critical in the control of those lepidopteran species, such as Helicoverpa spp., which are not highly susceptible to Cry1A proteins. In Australia, a transgenic variety of cotton expressing Cry1Ac and Cry2Ab (Bollgard II) comprises at least 80% of the total cotton area. Prior to the widespread adoption of Bollgard II, the frequency of alleles conf…

0106 biological sciencesCrops AgriculturalInsecticidesHelicoverpa punctigeraScienceUNESCO::CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología generalBacillus thuringiensisBacterial ProteinGenetically modified cropsHelicoverpa armigera01 natural sciencesMicrobiologyLepidoptera genitaliaInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanyBacillus thuringiensiBiotechnology/Applied MicrobiologyAnimalsMode of actionBiotechnology/Plant BiotechnologyHelicoverpaInsecticide030304 developmental biology0303 health sciencesMultidisciplinaryBinding SitesbiologyAnimalQfungiBinding SiteRbiology.organism_classificationBinding site alterationHelicoverpa speciesLepidoptera010602 entomologyCry1AcBacillus thuringiensis; Binding site alteration; Helicoverpa speciesMedicine:CIENCIAS DE LA VIDA::Biología de insectos (Entomología)::Entomología general [UNESCO]Plant Biology/Agricultural BiotechnologyResearch ArticleProtein BindingPLoS ONE
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Toxicity of several d-endotoxins of Bacillus thuringiensis against Helicoverpa armigera (Lepidoptera: Noctuidae) from Spain

2005

Abstract Toxicity and larval growth inhibition of 11 insecticidal proteins of Bacillus thuringiensis were evaluated against neonate larvae of Helicoverpa armigera, a major pest of important crops in Spain and other countries, by a whole-diet contamination method. The most active toxins were Cry1Ac4 and Cry2Aa1, with LC50 values of 3.5 and 6.3 μg/ml, respectively. At the concentrations tested, Cry1Ac4, Cry2Aa1, Cry9Ca, Cry1Fa1, Cry1Ab3, Cry2Ab2, Cry1Da, and Cry1Ja1, produced a significant growth inhibition, whereas Cry1Aa3, Cry1Ca2, and Cry1Ea had no effect.

Veterinary medicineBiological pest controlBacillus thuringiensisHelicoverpa armigeraLepidoptera genitaliachemistry.chemical_compoundHelicoverpa armigeraBacillus thuringiensisBotanyAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsbiologyfungiICPbiology.organism_classificationEndotoxinsLepidopteraBiopesticideMicrobial insect controlchemistrySpainGrowth inhibitionLarvaNoctuidaeCotton pestsCry toxinsPEST analysisGrowth inhibition
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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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Domain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pests

2020

The bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested…

InsecticidesAsiaInsectaHealth Toxicology and Mutagenesismedicine.medical_treatmentBacillus thuringiensislcsh:MedicineSpodopteraToxicologyArticleLethal Dose 5003 medical and health sciencesHelicoverpa armigeraBacterial ProteinsProtein DomainsBacillus thuringiensismedicineAnimalsSpodoptera littoralisPest Control Biological030304 developmental biologychemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyProtein Stabilitylcsh:RfungiSpodoptera spp.Ostrinia furnacalisSouth Americabiology.organism_classificationFusion proteinAnticarsia gemmatalisAmino acidEuropeAnticarsia gemmatalisspodoptera spp. helicoverpa armigeraBiochemistrychemistryAfricaNorth AmericaMamestra brassicaeOstrinia furnacalis
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RNA interference in Lepidoptera: an overview of successful and unsuccessful studies and implications for experimental design.

2011

International audience; Gene silencing through RNA interference (RNAi) has revolutionized the study of gene function, particularly in non-model insects. However, in Lepidoptera (moths and butterflies) RNAi has many times proven to be difficult to achieve. Most of the negative results have been anecdotal and the positive experiments have not been collected in such a way that they are possible to analyze. In this review, we have collected detailed data from more than 150 experiments including all to date published and many unpublished experiments. Despite a large variation in the data, trends that are found are that RNAi is particularly successful in the family Saturniidae and in genes involv…

0106 biological sciencesPhysiology[SDV]Life Sciences [q-bio]Tissue uptakeBioinformatics01 natural sciencesRNA interferenceRNA interferenceDatabases GeneticDelivery methodsCaenorhabditis elegansRegulation of gene expression0303 health sciencesIMMUNE-RESPONSESMANDUCA-SEXTALepidopteraRNA silencingSILKWORM BOMBYX-MORIResearch DesignInsect ProteinsRNA InterferenceMESSENGER-RNAHELICOVERPA-ARMIGERADOUBLE-STRANDED-RNAComputational biologyBiologyLepidoptera genitaliadsRNA properties03 medical and health sciencesBACILLUS-THURINGIENSISSMALL SILENCING RNASGene silencingAnimalsGene SilencingGene030304 developmental biologyRNA Double-StrandedMechanism (biology)fungiBiology and Life SciencesARMYWORM SPODOPTERA-FRUGIPERDAbiology.organism_classificationImmunity Innate010602 entomologyGene Expression RegulationInsect ScienceEpidermisCAENORHABDITIS-ELEGANSGene functionJournal of insect physiology
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Common receptor for Bacillus thuringiensis toxins Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera, Helicoverpa zea and Spodoptera exigua

2005

ABSTRACT Binding studies using 125 I-Cry1Ac and biotinylated Cry1Fa toxins indicate the occurrence of a common receptor for Cry1Ac, Cry1Fa, and Cry1Ja in Helicoverpa armigera , Helicoverpa zea , and Spodoptera exigua . Our results, along with previous binding data and the observed cases of cross-resistance, suggest that this pattern seems to be widespread among lepidopteran species.

Bacterial ToxinsBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaReceptors Cell SurfaceSpodopteraHelicoverpa armigeraSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaBotanyInvertebrate MicrobiologyAnimalsBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungibiology.organism_classificationEndotoxinsLepidopteraCry1AcInsect ProteinsNoctuidaeHelicoverpa zeaFood ScienceBiotechnology
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Characterization of the resistance to Vip3Aa in Helicoverpa armigera from Australia and the role of midgut processing and receptor binding.

2016

AbstractCrops expressing genes from Bacillus thuringiensis (Bt crops) are among the most successful technologies developed for the control of pests but the evolution of resistance to them remains a challenge. Insect resistant cotton and maize expressing the Bt Vip3Aa protein were recently commercialized, though not yet in Australia. We found that, although relatively high, the frequency of alleles for resistance to Vip3Aa in field populations of H. armigera in Australia did not increase over the past four seasons until 2014/15. Three new isofemale lines were determined to be allelic with previously isolated lines, suggesting that they belong to one common gene and this mechanism is relative…

0106 biological sciences0301 basic medicineCrops AgriculturalInsecticidesHelicoverpa armigeraPlant disease resistanceMothsmedicine.disease_cause01 natural sciencesArticleMicrobiology03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanymedicineAnimalsBinding siteGeneAllelesDisease ResistancePlant DiseasesMultidisciplinarybiologyToxinfungiAustraliaMidgutbiology.organism_classificationPlants Genetically Modified010602 entomology030104 developmental biologyCry1AcScientific reports
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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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