Search results for "crystal proteins"

showing 7 items of 7 documents

Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
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Effect of Cry Toxins on Xylotrechus arvicola (Coleoptera: Cerambycidae) Larvae

2022

Simple Summary Xylotrechus arvicola is a destructive pest in vineyards (Vitis vinifera) in the main wine-producing areas of the Iberian Peninsula. X. arvicola larvae bore into the grapevine wood-making galleries, thus damaging the plant both directly and indirectly. The susceptibility of X. arvicola larvae to five coleopteran toxic Cry proteins was evaluated under laboratory conditions in order to deepen the knowledge of the effect of these proteins on this insect throughout its biological development. The Cry proteins tested could be applied to control X. arvicola larvae since they were able to kill them and cause serious alterations in the larvae during the remaining months of development…

animal structuresSciencefungiQBacillus thuringiensisfood and beveragesCase ReportPlagues ControlvineyardsXylophagous polyphagousInsect Scienceparasitic diseases<i>Bacillus thuringiensis</i>crystal proteinsinsect pestInsects
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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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Constitutive Activation of the Midgut Response to Bacillus thuringiensis in Bt-Resistant Spodoptera exigua

2010

Bacillus thuringiensis is the most effective microbial control agent for controlling numerous species from different insect orders. The main threat for the long term use of B. thuringiensis in pest control is the ability of insects to develop resistance. Thus, the identification of insect genes involved in conferring resistance is of paramount importance. A colony of Spodoptera exigua (Lepidoptera: Noctuidae) was selected for 15 years in the laboratory for resistance to Xentari (TM), a B. thuringiensis-based insecticide, reaching a final resistance level of greater than 1,000-fold. Around 600 midgut ESTs were analyzed by DNA-macroarray in order to find differences in midgut gene expression …

0106 biological sciencesDrug Resistancelcsh:MedicineGene ExpressionInsectaminopeptidase n01 natural sciencesAminopeptidasesHemolysin ProteinsEndotoxinmanduca-sextaBacillus thuringiensisInsect ProteinBiotechnology/Applied Microbiologylcsh:Scienceheliothis-virescensmedia_common0303 health sciencesLarvaMultidisciplinarybiologymediated insect resistanceGenetics and Genomics/Gene ExpressionEcology/Population Ecologybacterial-infectionNoctuidaeInsect ProteinsResearch Articlemedia_common.quotation_subjectAminopeptidaseMolecular Sequence DataBacillus thuringiensisBacterial ProteinSpodopteraSpodopterastem-cell proliferationMicrobiology03 medical and health sciencesMicrobiology/Applied MicrobiologyBacterial ProteinsExiguaBotanyBacillus thuringiensiAnimalscrystal proteinsBIOS Plant Development SystemsAmino Acid Sequencekinase pathways030304 developmental biologyposterior midgutHeliothis virescensBacillus thuringiensis ToxinsAnimaltrichoplusia-nilcsh:RfungiMidgutHemolysin Proteinbiology.organism_classificationEndotoxinsGastrointestinal Tract010602 entomologyPlant Biology/Agricultural Biotechnologylcsh:QSequence Alignment
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Biochemistry and genetics of insect resistance to Bacillus thuringiensis.

2001

▪ Abstract  Bacillus thuringiensis (Bt) is a valuable source of insecticidal proteins for use in conventional sprayable formulations and in transgenic crops, and it is the most promising alternative to synthetic insecticides. However, evolution of resistance in insect populations is a serious threat to this technology. So far, only one insect species has evolved significant levels of resistance in the field, but laboratory selection experiments have shown the high potential of other species to evolve resistance against Bt. We have reviewed the current knowledge on the biochemical mechanisms and genetics of resistance to Bt products and insecticidal crystal proteins. The understanding of th…

Pesticide resistanceInsectamedia_common.quotation_subjectBacillus thuringiensisInsectGenetically modified cropsBiologyInsecticide ResistanceBacillus thuringiensisAnimalsInsecticidal crystal proteinsPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commonGeneticsResistance (ecology)business.industryDipterafungiPest controlbiology.organism_classificationBiotechnologyColeopteraLepidopteraCry1AcInsect SciencebusinessAnnual review of entomology
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Insect resistance to Bacillus thuringiensis insecticidal crystal proteins

2000

Several insect species have developed resistance to insecticidal crystal proteins from Bacillus thuringiensis, either through laboratory selection, or under field conditions. In this chapter we review the current knowledge on the biochemical and genetic mechanisms of resistance to B. thuringiensis. This knowledge will be important in the design of appropriate tactics to manage the development of resistance in insect populations.

GeneticsbiologyResistance (ecology)Bacillus thuringiensismedia_common.quotation_subjectfungiInsectInsecticidal crystal proteinsbiology.organism_classificationSelection (genetic algorithm)Field conditionsmedia_common
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Lack of cross‐resistance to otherBacillus thuringiensiscrystal proteins in a population ofPlutella xylostellahighly resistant to cryia(b)

1994

Competition experiments were performed with brush border membrane vesicles of diamondback moth larvae using 125I‐labelled CryIA(b) and unlabelled CryIA(a), CryIA(b) and CryIA(c). The results suggested a model with a single binding site for CryIA(b). Heterologous competition showed that CryIA(c) competed as effectively as CryIA(b) for the CryIA(b) binding site, whereas CryIA(a) competed less effectively. Toxicity tests were performed on third instar larvae with trypsin‐activated insecticidal crystal proteins (ICPs) and a commercial formulation of Bacillus thuringiensis (Bt) (Dipel). A laboratory colony was found to be susceptible to all four ICPs tested and to Dipel. CryIA(b), CryIA(c) and C…

education.field_of_studyDiamondback mothbiologyfungiPopulationPlutellabiology.organism_classificationMolecular biologyInsect ScienceBacillus thuringiensisBotanyInsecticidal crystal proteinseducationAgronomy and Crop ScienceCross-resistanceBiocontrol Science and Technology
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