Search results for "noctuidae"

showing 10 items of 28 documents

Shared Binding Sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A Toxins

2001

ABSTRACT Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth ( Plutella xylostella ) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that…

Bacterial ToxinsMolecular Sequence DataSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsAmino Acid SequenceBinding siteBinding SitesDiamondback mothBacillus thuringiensis ToxinsEcologybiologyHeliothis virescensfungibiology.organism_classificationEndotoxinsLepidopteraPlutellidaeCry1AcLarvaNoctuidaeFood ScienceBiotechnologyApplied and Environmental Microbiology
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Interaction of Bacillus thuringiensis Toxins with Larval Midgut Binding Sites of Helicoverpa armigera (Lepidoptera: Noctuidae)

2004

ABSTRACT In 1996, Bt-cotton (cotton expressing a Bacillus thuringiensis toxin gene) expressing the Cry1Ac protein was commercially introduced to control cotton pests. A threat to this first generation of transgenic cotton is the evolution of resistance by the insects. Second-generation Bt-cotton has been developed with either new B. thuringiensis genes or with a combination of cry genes. However, one requirement for the “stacked” gene strategy to work is that the stacked toxins bind to different binding sites. In the present study, the binding of 125 I-labeled Cry1Ab protein ( 125 I-Cry1Ab) and 125 I-Cry1Ac to brush border membrane vesicles (BBMV) of Helicoverpa armigera was analyzed in com…

Bacterial ToxinsPopulationBacillus thuringiensisCarbohydratesDrug ResistanceHelicoverpa armigeraModels BiologicalApplied Microbiology and BiotechnologyMicrobiologyHemolysin Proteinschemistry.chemical_compoundBacterial ProteinsLectinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsBinding siteSoybean agglutininPest Control BiologicaleducationGossypiumeducation.field_of_studyBinding SitesBacillus thuringiensis ToxinsEcologybiologyfungifood and beveragesPlants Genetically Modifiedbiology.organism_classificationSialic acidEndotoxinsLepidopteraKineticsCry1AcchemistryBiochemistryGenes BacterialLarvaNoctuidaeDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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Molecular and Insecticidal Characterization of a Cry1I Protein Toxic to Insects of the Families Noctuidae, Tortricidae, Plutellidae, and Chrysomelidae

2006

ABSTRACT The most notable characteristic of Bacillus thuringiensis is its ability to produce insecticidal proteins. More than 300 different proteins have been described with specific activity against insect species. We report the molecular and insecticidal characterization of a novel cry gene encoding a protein of the Cry1I group with toxic activity towards insects of the families Noctuidae, Tortricidae, Plutellidae, and Chrysomelidae. PCR analysis detected a DNA sequence with an open reading frame of 2.2 kb which encodes a protein with a molecular mass of 80.9 kDa. Trypsin digestion of this protein resulted in a fragment of ca. 60 kDa, typical of activated Cry1 proteins. The deduced sequen…

Earias insulanaBacterial ToxinsMolecular Sequence DataBacillus thuringiensisMothsLobesia botranaApplied Microbiology and BiotechnologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsAmino Acid SequencePest Control BiologicalBacillus thuringiensis ToxinsEcologybiologyfungiPlutellaSequence Analysis DNAbiology.organism_classificationColeopteraEndotoxinsOpen reading frameCry1AcBiochemistryPlutellidaeLarvaNoctuidaeFood ScienceBiotechnologyApplied and Environmental Microbiology
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Use of Bacillus thuringiensis toxins for control of the cotton pest earias insulana (Boisd.) (Lepidoptera: Noctuidae)

2006

ABSTRACT Thirteen of the most common lepidopteran-specific Cry proteins of Bacillus thuringiensis have been tested for their efficacy against newly hatched larvae of two populations of the spiny bollworm, Earias insulana . At a concentration of 100 μg of toxin per milliliter of artificial diet, six Cry toxins (Cry1Ca, Cry1Ea, Cry1Fa, Cry1Ja, Cry2Aa, and Cry2Ab) were not toxic at all. Cry1Aa, Cry1Ja, and Cry2Aa did not cause mortality but caused significant inhibition of growth. The other Cry toxins (Cry1Ab, Cry1Ac, Cry1Ba, Cry1Da, Cry1Ia, and Cry9Ca) were toxic to E. insulana larvae. The 50% lethal concentration values of these toxins ranged from 0.39 to 21.13 μg/ml (for Cry9Ca and Cry1Ia, …

Earias insulanaBacterial ToxinsPopulationBacillus thuringiensismedicine.disease_causeBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsControl of the cotton pest earias insulanaBacillus thuringiensisBotanyInvertebrate MicrobiologymedicineAnimalsToxinsPest Control BiologicaleducationGossypiumeducation.field_of_studyBinding SitesBacillus thuringiensis ToxinsMicrovilliEcologybiologyToxinfungiPlants Genetically Modifiedbiology.organism_classificationEndotoxinsLepidopteraBollwormCry1AcLarvaNoctuidaeBiological AssayFood ScienceBiotechnology
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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
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Extremely potent antifeedant neo-clerodane derivatives of scutecyprol A

2004

Two known neo-clerodane diterpenoids, scutecyprol A (1) and scutalbin C (2), have been isolated from the acetone extract of the aerial parts of Scutellaria sieberi. The antifeedant activity of scutecyprol A (1), of its 15-oxo derivative (3), and of several halohydrins (4-9), synthesized starting from compounds 1 and 3, against Spodoptera littoralis have been determined and structure-antifeedant relationships are discussed.

InsecticidesbiologyScutellaria sieberiScutalbin CStereochemistryScutellariaGeneral ChemistryhalohydrinSpodoptera littoralisSpodopterabiology.organism_classificationantifeedant activityDiterpenes ClerodaneLepidoptera genitaliachemistry.chemical_compoundchemistryAcetoneNoctuidaeAnimalsscutecyprol ASettore BIO/15 - Biologia FarmaceuticaScutellaria sieberiGeneral Agricultural and Biological SciencesSpodoptera littoralis
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Broad-spectrum cross-resistance in Spodoptera exigua from selection with a marginally toxic Cry protein.

2009

BACKGROUND:Spodoptera exigua (Hubner) has developed resistance to a wide range of chemical insecticides. Products based on Bacillus thuringiensis Cry toxins are used in integrated pest management as an ecologically friendly alternative for pest control. Since there are few B. thuringiensis Cry proteins highly active against S. exigua, it is desirable to apply appropriate resistance management strategies to prevent the evolution of resistance to these proteins. RESULTS:Spodoptera exigua larvae were selected with Cry1Ab, a protein with low activity against this pest. Selected larvae developed > 30-fold resistance to Cry1Ab in 13 generations, relative to an unselected strain. The estimated rea…

Integrated pest managementInsecticidesBacillus thuringiensisSpodopteraSpodopteraToxicologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaAnimalsCross-resistancebiologyBacillus thuringiensis Toxinsbusiness.industryfungiPest controlGeneral Medicinebiology.organism_classificationBiotechnologyEndotoxinsInsect ScienceLarvaNoctuidaePEST analysisbusinessAgronomy and Crop SciencePest management science
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High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from <em>Spodoptera exigua</em> (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…

Lepidoptera genitaliaAgglutination (biology)biologyBiochemistryC-type lectinlawExiguaRecombinant DNANoctuidaeSpodopterabiology.organism_classificationProtein concentrationlaw.invention
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Effects of ajugarins and related neoclerodane diterpenoids on feeding behaviour of Leptinotarsa decemlineata and Spodoptera exigua larvae

2001

Three naturally occurring ajugarins and seven semisynthetic derivatives of them, possessing different functionalities in the decalin part, together with two natural furoneoclerodane diterpenes, have been assessed as feeding behavior modifying agents of larvae of the generalist Spodoptera exigua and a specialist like Leptinotarsa decemlineata. Ajugarin I and some of its derivatives exhibited a significant antifeedant activity against larvae of S. exigua in both choice and no-choice assays. Conversely, the furoneoclerodane diterpenes only presented antifeedant activity against larvae of L. decemlineata. These results indicate that the biological action of the tested substances is strongly mod…

Magnetic Resonance SpectroscopyPlant ScienceSpodopteraHorticultureSpodopteraBiochemistryLepidoptera genitaliachemistry.chemical_compoundExiguaBotanyAnimalsMolecular BiologyLeptinotarsaLarvabiologyfungiFeeding BehaviorGeneral Medicinebiology.organism_classificationTerpenoidColeopterachemistryBiochemistryLarvaNoctuidaeDiterpenesDiterpenePhytochemistry
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Baculovirus infection affects caterpillar chemoperception

2021

International audience; Baculoviruses are double-stranded DNA entomopathogenic viruses that infect predominantly insects of the order Lepidoptera. Research in the last decade has started to disentangle the mechanisms underlying the insect-virus interaction, particularly focusing on the effects of the baculovirus infection in the host's physiology. Among crucial physiological functions, olfaction has a key role in reproductive tasks, food source detection and enemy avoidance. In this work, we describe that Spodoptera exigua multiple nucleopolyhedrovirus (SeMNPV) induces expression changes in some odorant receptors (ORs)-the centrepiece of insect's olfaction-when infecting larvae from its nat…

OlfactionSpodopteraSpodopteraReceptors OdorantBiochemistryLepidoptera genitalia03 medical and health sciences0302 clinical medicineExiguaAnimalsBehaviour[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBaculovirusMolecular Biology030304 developmental biologyNeuronsGenetics0303 health sciencesbiologyOdorant receptorsHost (biology)fungibiology.organism_classificationOlfactionNucleopolyhedrovirusesBeet armywormDrosophila melanogasterLarvaInsect ScienceInsect ProteinsNoctuidaeCaterpillarHeterologous expressionDrosophila melanogaster030217 neurology & neurosurgeryInsect Biochemistry and Molecular Biology
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