Search results for "Bacillus thuringiensis"

showing 10 items of 211 documents

Assessment of genetically modified soybean MON 87751 for food and feed uses under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐NL‐2014‐121)

2018

Abstract Soybean MON 87751 was developed through Agrobacterium tumefaciens‐mediated transformation to provide protection certain specific lepidopteran pests by the expression of the Cry1A.105 and Cry2Ab2 proteins derived from Bacillus thuringiensis. The molecular characterisation data and bioinformatic analyses did not identify issues requiring assessment for food and feed safety. None of the compositional, agronomic and phenotypic differences identified between soybean MON 87751 and the conventional counterpart required further assessment. The GMO Panel did not identify safety concerns regarding the toxicity and allergenicity of the Cry1A.105 and Cry2Ab2 proteins as expressed in soybean MO…

0106 biological sciencesCry1AVeterinary (miscellaneous)Plant ScienceTP1-1185Biology01 natural sciencesMicrobiologyGenetically modified soybeansoybean (Glycinemax)MON877510404 agricultural biotechnologyEnvironmental safetyBacillus thuringiensisTX341-641Cry2Ab2Cry1A.105Animal healthbusiness.industryGMONutrition. Foods and food supplyChemical technologyfungiRegulation (EC) No 1829/2003food and beverages10504 agricultural and veterinary sciencesbiology.organism_classification040401 food scienceBiotechnologySettore AGR/02 - Agronomia E Coltivazioni ErbaceeSettore AGR/11 - Entomologia Generale E ApplicataScientific OpinionMON 87751insect resistantAnimal Science and ZoologyParasitologybusinesssoybean (Glycine max)010606 plant biology & botanyFood ScienceRegulation (EC) No 1829/2003EFSA Journal
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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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Effects of Bacillus thuringiensis δ-Endotoxins on the Pea Aphid ( Acyrthosiphon pisum )

2009

ABSTRACT Four Bacillus thuringiensis δ-endotoxins, Cry3A, Cry4Aa, Cry11Aa, and Cyt1Aa, were found to exhibit low to moderate toxicity on the pea aphid, Acyrthosiphon pisum , in terms both of mortality and growth rate. Cry1Ab was essentially nontoxic except at high rates. To demonstrate these effects, we had to use exhaustive buffer-based controls.

0106 biological sciencesHomopteraBacillus thuringiensismedicine.disease_cause01 natural sciencesApplied Microbiology and BiotechnologyHemolysin Proteins03 medical and health sciencesBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologymedicineAnimalsFood science030304 developmental biology0303 health sciencesAphidBacillaceaeBacillus thuringiensis ToxinsEcologybiologyToxinfungiPeasfood and beveragesAphididaebiology.organism_classificationSurvival AnalysisBacillales3. Good healthAcyrthosiphon pisumEndotoxins010602 entomologyAphids1-1-1 Article périodique à comité de lecture[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/SymbiosisFood ScienceBiotechnologyApplied and Environmental Microbiology
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Assessment of the Antimicrobial Activity and the Entomocidal Potential of Bacillus thuringiensis Isolates from Algeria.

2017

This work represents the first initiative to analyze the distribution of B. thuringiensis in Algeria and to evaluate the biological potential of the isolates. A total of 157 isolates were recovered, with at least one isolate in 94.4% of the samples. The highest Bt index was found in samples from rhizospheric soil (0.48) and from the Mediterranean area (0.44). Most isolates showed antifungal activity (98.5%), in contrast to the few that had antibacterial activity (29.9%). A high genetic diversity was made evident by the finding of many different crystal shapes and various combinations of shapes within a single isolate (in 58.4% of the isolates). Also, over 50% of the isolates harbored cry1, …

0301 basic medicineAntifungalStaphylococcus aureusmedicine.drug_classHealth Toxicology and Mutagenesis030106 microbiologyBacterial ToxinsBiological pest controlBacillus thuringiensisBiologyToxicologyArticleMicrobiology03 medical and health sciencesB. thuringiensisAnti-Infective AgentsBacterial ProteinsBacillus thuringiensismedicineEscherichia colibiocontrolGeneSoil MicrobiologyGenetic diversitycryChitinasesFungi<i>B. thuringiensis</i>; antibacterial; antifungal; <i>cry</i>; <i>vip3</i>; chitinase; biocontrolAntimicrobialbiology.organism_classificationCryptochromesantibacterialHexosaminidasesGenes BacterialAlgeriachitinaseChitinasePseudomonas aeruginosavip3biology.proteinMicroscopy Electron ScanningAntibacterial activityantifungalToxins
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2016

Bacillus thuringiensis Cry3Aa and Cry3Ca proteins have been reported to be toxic against the African sweetpotato pest Cylas puncticollis. In the present work, the binding sites of these proteins in C. puncticollis brush border vesicles suggest the occurrence of different binding sites, but only one of them is shared. Our results suggest that pest resistance mediated by alteration of the shared Cry-receptor binding site might not render both Cry proteins ineffective.

0301 basic medicineBrentidaeGeneticsendocrine systemPesticide resistancebiologyBrush borderbusiness.industryWeevilfungi030106 microbiologyPest controlToxicologybiology.organism_classification03 medical and health sciencesBacillus thuringiensisBotanyPEST analysisBinding sitebusinessToxicon
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Efficacy and Resistance Management Potential of a Modified Vip3C Protein for Control of Spodoptera frugiperda in Maize

2018

AbstractA modified Vip3C protein has been developed that has a spectrum of activity that has the potential to be commercially useful for pest control, and shows good efficacy against Spodoptera frugiperda in insect bioassays and field trials. For the first time Vip3A and Vip3C proteins have been compared to Cry1 and Cry2 proteins in a complete set of experiments from insect bioassays to competition binding assays to field trials, and the results of these complementary experiments are in agreement with each other. Binding assays with radiolabelled toxins and brush border membrane vesicles from S. frugiperda and Helicoverpa armigera show that the modified Vip3C protein shares binding sites wi…

0301 basic medicineBrush bordermedia_common.quotation_subject030106 microbiologyBacillus thuringiensislcsh:MedicineInsectBiologyHelicoverpa armigeraSpodopteraSpodopteraZea maysArticleInsecticide Resistance03 medical and health sciencesBacillus thuringiensisBioassayAnimalsBinding sitePest Control Biologicallcsh:Sciencemedia_commonMultidisciplinaryBinding Sitesbusiness.industryfungilcsh:RPest controlbiology.organism_classificationPlants Genetically ModifiedEndotoxinsBiochemistryLarvalcsh:QbusinessScientific Reports
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Validation of ADAM10 metalloprotease as aBacillus thuringiensisCry3Aa toxin functional receptor in Colorado potato beetle (Leptinotarsa decemlineata)

2016

Bacillus thuringiensis parasporal crystal proteins (Cry proteins) are insecticidal pore-forming toxins that bind to specific receptor molecules on the brush border membrane of susceptible insect midgut cells to exert their toxic action. In the Colorado potato beetle (CPB), a coleopteran pest, we previously proposed that interaction of Cry3Aa toxin with a CPB ADAM10 metalloprotease is an essential part of the mode of action of this toxin. Here, we annotated the gene sequence encoding an ADAM10 metalloprotease protein (CPB-ADAM10) in the CPB genome sequencing project, and using RNA interference gene silencing we demonstrated that CPB-ADAM10 is a Cry3Aa toxin functional receptor in CPB. Cry3Aa…

0301 basic medicineBrush bordermedicine.diagnostic_testbiologyToxinProteolysis030106 microbiologyColorado potato beetleMidgutmedicine.disease_causebiology.organism_classificationMicrobiology03 medical and health sciencessurgical procedures operative030104 developmental biologyBiochemistryRNA interferenceInsect ScienceBacillus thuringiensisGeneticsmedicineReceptorMolecular Biologycirculatory and respiratory physiologyInsect Molecular Biology
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Hetero-oligomerization of Bacillus thuringiensis Cry1A proteins enhance binding to the ABCC2 transporter of Spodoptera exigua

2021

The ATP binding cassette (ABC) transporters are membrane proteins that can act as putative receptors for Cry proteins from Bacillus thuringiensis (Bt) in the midgut of different insects. For the beet armyworm, Spodoptera exigua, ABCC2 and ABCC3 have been found to interact with Cry1A proteins, the main insecticidal proteins used in Bt crops, as well as Bt-based pesticides. The ABCC2 has shown to have specific binding towards Cry1Ac and is involved in the toxic process of Cry1A proteins, but the role of this transporter and how it relates with the Cry1A proteins is still unknown. Here, we have characterized the interactions between the SeABCC2 and the main proteins that bind to the receptor. …

0301 basic medicineCell SurvivalBacillus thuringiensisATP-binding cassette transporterSpodopteraSpodopteraBiochemistryHemolysin Proteins03 medical and health sciences0302 clinical medicineBacterial ProteinsProtein DomainsBacillus thuringiensisSf9 CellsAnimalsBinding siteReceptorMolecular BiologyBinding SitesBacillus thuringiensis ToxinsbiologyChemistryfungifood and beveragesTransporterCell Biologybiology.organism_classificationMultidrug Resistance-Associated Protein 2Endotoxins030104 developmental biologyMembrane proteinCry1AcBiochemistryMutationInsect ProteinsMultidrug Resistance-Associated ProteinsProtein Multimerization030217 neurology & neurosurgeryProtein BindingBiochemical Journal
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Assessment of genetically modified maize MON 87411 for food and feed uses, import and processing, under Regulation (EC) No 1829/2003 (application EFS…

2018

Maize MON 87411 was developed to confer resistance to corn rootworms (Diabrotica spp.) by the expression of a modified version of the Bacillus thuringiensis cry3Bb1 gene and a DvSnf7 dsRNA expression cassette, and tolerance to glyphosate-containing herbicides by the expression of a CP4 5-enolpyruvylshikimate-3-phosphate synthase (cp4 epsps) gene. The molecular characterisation data and bioinformatics analyses did not identify issues requiring assessment for food and feed safety. No statistically significant differences in the agronomic and phenotypic characteristics tested between maize MON 87411 and its conventional counterpart were identified. The compositional analysis of maize MON 87411…

0301 basic medicineCry3Bb1DvSnf7Cry3Bb1Veterinary (miscellaneous)[SDV]Life Sciences [q-bio]TP1-1185Plant Science010501 environmental sciences01 natural sciencesMicrobiology03 medical and health sciencesPlant scienceEnvironmental safetyBacillus thuringiensisTX341-641Diabroticamaize (Zea mays)0105 earth and related environmental sciences2. Zero hungerGenetically modified maizeCP4 EPSPSbiologyAnimal healthNutrition. Foods and food supplybusiness.industryGMOChemical technologyRegulation (EC) No 1829/2003biology.organism_classificationFood safetyMON 87411BiotechnologyScientific Opinion030104 developmental biologyAnimal Science and ZoologyParasitologybusinessRegulation (EC) No 1829/2003Food Science
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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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