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
researchProduct

Specific binding  of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species

2008

ABSTRACT For a long time, it has been assumed that the mode of action of Cry2A toxins was unique and different from that of other three-domain Cry toxins due to their apparent nonspecific and unsaturable binding to an unlimited number of receptors. However, based on the homology of the tertiary structure among three-domain Cry toxins, similar modes of action for all of them are expected. To confirm this hypothesis, binding assays were carried out with 125 I-labeled Cry2Ab. Saturation assays showed that Cry2Ab binds in a specific and saturable manner to brush border membrane vesicles (BBMVs) of Helicoverpa armigera . Homologous-competition assays with 125 I-Cry2Ab demonstrated that this toxi…

BioquímicaBrush borderBiotecnologia agrícolaBacillus thuringiensisMicrobiologiaPlasma protein bindingHelicoverpa armigeraApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteHelicoverpaBacillus thuringiensis ToxinsStaining and LabelingEcologybiologyfungiMidgutbiology.organism_classificationEndotoxinsGastrointestinal TractLepidopteraKineticsBiochemistryHelicoverpa zeaProteïnesProtein BindingFood ScienceBiotechnology
researchProduct

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
researchProduct

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
researchProduct

Association of Cry1Ac toxin resistance in Helicoverpa zea (Boddie) with increased alkaline phosphatase levels in the midgut lumen.

2012

ABSTRACT Resistance to Bacillus thuringiensis Cry1Ac toxin was characterized in a population of Helicoverpa zea larvae previously shown not to have an alteration in toxin binding as the primary resistance mechanism to this toxin. Cry1Ac-selected larvae (AR1) were resistant to protoxins and toxins of Cry1Ab, Cry1Ac, and the corresponding modified proteins lacking helix α-1 (Cry1AbMod and Cry1AcMod). When comparing brush border membrane vesicles (BBMVs) prepared from susceptible (LC) and AR1 larval midguts, there were only negligible differences in overall Cry1Ac toxin binding, though AR1 had 18% reversible binding, in contrast to LC, in which all binding was irreversible. However, no differe…

Brush borderPopulationBacterial Proteinmedicine.disease_causeApplied Microbiology and BiotechnologyHemolysin ProteinsEndotoxinBacterial ProteinsBacillus thuringiensismedicineInvertebrate MicrobiologyAnimalseducationeducation.field_of_studybiologyEcologyBacillus thuringiensis ToxinsToxinAnimalfungiMidgutHemolysin ProteinLigand (biochemistry)biology.organism_classificationAlkaline PhosphataseEndotoxinsGastrointestinal TractLepidopteraBiochemistryLarvaAlkaline phosphataseHelicoverpa zeaFood ScienceBiotechnologyProtein BindingApplied and environmental microbiology
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

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
researchProduct

Western European Populations of the Ichneumonid Wasp Hyposoter didymator Belong to a Single Taxon

2019

Hyposoter didymator (Hymenoptera, Ichneumonidae) is a generalist solitary endoparasitoid of noctuid larvae. In the present work, we tested whether populations of H. didymator were divided in several genetically distinct taxa as described for many other generalist parasitoid species, and whether differences in H. didymator parasitism rates were explained by the insect host species and/or by the plant on which these hosts were feeding on. The genetic analysis of natural populations collected in different regions in France and Spain on seven different insect hosts and seven different host plants (775 individuals) showed that H. didymator populations belong to a unique single taxon. However, H.…

Settore AGR/11 - Entomologia Generale E ApplicataHost preferenceHyposoter didymatorHelicoverpa amigeraPopulation genetic structureWestern European populations
researchProduct

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
researchProduct

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
researchProduct