Search results for "Bacillus"

showing 10 items of 774 documents

Toxicity of five Cry proteins against the insect pest Acanthoscelides obtectus (Coleoptera: Chrisomelidae: Bruchinae).

2019

Abstract The beetle Acanthoscelides obtectus (Say) causes severe post-harvest losses in the common bean (Phaseolus vulgaris). Under laboratory conditions, the susceptibility of A. obtectus to five coleopteran-specific Cry toxic proteins from Bacillus thuringiensis (Cry1Ba, Cry1Ia, Cry3Aa, Cry7Ab, and Cry23/37) was evaluated. After 30 days exposure, Cry proteins demonstrated high activity against A. obtectus adults (100% mortality). Proteins showed statistical differences in toxicity parameters compared to the control treatment, but the parameters were similar among them, and indicated that the final toxic effects can be observed after the 24th day. The toxic effects on A. obtectus larvae we…

0106 biological sciences0301 basic medicineved/biology.organism_classification_rank.speciesBacillus thuringiensisAcanthoscelides obtectus01 natural sciencesInsect ControlInsect pestToxicology03 medical and health sciencesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsLarvaControl treatmentbiologyBacillus thuringiensis Toxinsved/biologyfood and beveragesBean weevilbiology.organism_classificationColeopteraEndotoxins010602 entomology030104 developmental biologyBiological Control AgentsLarvaToxicityPhaseolusJournal of invertebrate pathology
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Response Mechanisms of Invertebrates to Bacillus thuringiensis and Its Pesticidal Proteins

2021

SUMMARY Extensive use of chemical insecticides adversely affects both environment and human health. One of the most popular biological pest control alternatives is bioinsecticides based on Bacillus thuringiensis. This entomopathogenic bacterium produces different protein types which are toxic to several insect, mite, and nematode species. Currently, insecticidal proteins belonging to the Cry and Vip3 groups are widely used to control insect pests both in formulated sprays and in transgenic crops. However, the benefits of B. thuringiensis-based products are threatened by insect resistance evolution. Numerous studies have highlighted that mutations in genes coding for surrogate receptors are …

0106 biological sciences0303 health sciencesbusiness.industrymedia_common.quotation_subjectfungiBiological pest controlInsectGenetically modified cropsBiologybiology.organism_classification01 natural sciencesMicrobiologyBiotechnology010602 entomology03 medical and health sciencesInfectious DiseasesNematodeBacillus thuringiensisbusinessMolecular BiologyGeneCaenorhabditis elegansBacteria030304 developmental biologymedia_commonMicrobiology and Molecular Biology Reviews
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Assessment of genetically modified maize 4114 for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐NL‐2014‐123)

2018

Abstract Maize 4114 was developed through Agrobacterium tumefaciens‐mediated transformation to provide protection against certain lepidopteran and coleopteran pests by expression of the Cry1F, Cry34Ab1 and Cry35Ab1 proteins derived from Bacillus thuringiensis, and tolerance to the herbicidal active ingredient glufosinate‐ammonium by expression of the PAT protein derived from Streptomyces viridochromogenes. The molecular characterisation data did not identify issues requiring assessment for food/feed safety. None of the compositional, agronomic and phenotypic differences identified between maize 4114 and the non‐genetically modified (GM) comparator(s) required further assessment. There were …

0106 biological sciences4114herbicide toleranceAgrobacteriumCry1F[SDV]Life Sciences [q-bio]Veterinary (miscellaneous)Cry34Ab1Context (language use)4114; Cry1F; Cry34Ab1; Cry35Ab1; GMO; herbicide tolerance; insect-resistant; maize (Zea mays); PAT; Regulation (EC) No 1829/2003TP1-1185Plant Science010501 environmental sciences01 natural sciencesMicrobiologyBacillus thuringiensisinsect‐resistantinsect-resistantTX341-641maize (Zea mays)0105 earth and related environmental sciences2. Zero hungerGenetically modified maizeAnimal healthbiologyNutrition. Foods and food supplyGMObusiness.industryChemical technologyCry35Ab1Regulation (EC) No 1829/2003maize (Zea mays)biology.organism_classificationGenetically modified organismBiotechnologyTransformation (genetics)Scientific Opinion13. Climate actionAnimal Science and ZoologyParasitologybusinessCry 1FPATRegulation (EC) No 1829/2003010606 plant biology & botanyFood SciencePotential toxicity
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Effect of hydrogen peroxide on the dehydrogenase and quinone-reductase activity of irradiated Lactobacillus plantarum cells

2020

Abstract The resistance of lactobacilli to oxidative stress is of great importance for their applicability as probiotics. This study aimed to evaluate the response of Lactobacillus plantarum strain ATCC® 14917™, grown in either de Man, Rogosa, and Sharpe agar (MRS medium) or tryptic soy broth (TSB medium), to 1–2 mM H2O2 after the exposure to different doses of ionising radiation. Two bacterial extracellular enzyme groups, dehydrogenases (DHAs) and quinone reductases (QRs), served as the criteria of viability and antioxidant activity, respectively. The irradiated L. plantarum culture grown in TSB showed increased QR activity at irradiation doses of 2–50 Gy, with the maximum activity at 10 G…

0106 biological sciencesAntioxidantfood.ingredientmedicine.medical_treatmentDehydrogenase01 natural sciencesTryptic soy brothchemistry.chemical_compound0404 agricultural biotechnologyfoodQuinone Reductases010608 biotechnologymedicineAgarFood scienceHydrogen peroxidechemistry.chemical_classificationbiologyfood and beverages04 agricultural and veterinary sciencesbiology.organism_classification040401 food scienceEnzymechemistryLactobacillus plantarumFood ScienceLWT
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Fermented sweet lemon juice (Citrus limetta) using Lactobacillus plantarum LS5: Chemical composition, antioxidant and antibacterial activities

2017

Sweet lemon juice was fermented with Lactobacillus plantarum LS5 to produce a probiotic juice. The cell counts of the L. plantarum LS5 increased from 7.0 ± 0.1 to 8.63 ± 0.38 log CFU/mL during fermentation (37 °C for 48 h) (p < 0.05) and decreased from 8.63 ± 0.38 to 7.14 ± 0.21 log CFU/mL after storage (4 °C for 28 d). Antibacterial activity against S. Typhimurium and E. coli O157:H7 was observed in fermented sweet lemon juice. Immediately after fermentation, pH, lactic acid and antioxidant capacity of the samples increased, while glucose and fructose, total acidity, citric acid and phenolic decreased. During storage, phenolics, and antioxidant decreased in both fermented and non-fermented…

0106 biological sciencesAntioxidantmedicine.medical_treatmentMedicine (miscellaneous)medicine.disease_cause01 natural scienceslaw.inventionE. coli O157:H7Probiotic0404 agricultural biotechnologylawCitrus limetta010608 biotechnologymedicineTX341-641Food scienceChemical compositionEscherichia coliNutrition and DieteticsbiologyChemistryNutrition. Foods and food supplyfood and beverages04 agricultural and veterinary sciencesCitrus limettabiology.organism_classification040401 food sciencecarbohydrates (lipids)Lemon juiceFermentationS. TyphimuriumLactobacillus plantarumFood ScienceLactobacillus plantarumSweet lemon juiceJournal of Functional Foods
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The Spodoptera exigua ABCC2 Acts as a Cry1A Receptor Independently of its Nucleotide Binding Domain II

2019

ABC proteins are primary-active transporters that require the binding and hydrolysis of ATP to transport substrates across the membrane. Since the first report of an ABCC2 transporter as receptor of Cry1A toxins, the number of ABC transporters known to be involved in the mode of action of Cry toxins has increased. In Spodoptera exigua, a mutation in the SeABCC2 gene is described as genetically linked to resistance to the Bt-product XentariTM. This mutation affects an intracellular domain involved in ATP binding, but not the extracellular loops. We analyzed whether this mutation affects the role of the SeABCC2 as a functional receptor to Cry1A toxins. The results show that Sf21 cells express…

0106 biological sciencesCell SurvivalHealth Toxicology and Mutagenesislcsh:MedicineReceptors Cell SurfaceATP-binding cassette transporterSpodopteraSpodopteraToxicologymedicine.disease_causeBt resistance01 natural sciencesArticleCell LineHemolysin Proteins03 medical and health sciencesBacterial Proteinsmode of actionGTP-Binding ProteinsATP hydrolysismedicineAnimalsReceptor030304 developmental biology0303 health sciencesMutationBacillus thuringiensis ToxinsbiologyChemistryfungilcsh:Rheterologous expressionTransporterbiology.organism_classificationMultidrug Resistance-Associated Protein 2Cell biologyEndotoxins010602 entomologyCyclic nucleotide-binding domainSf21 cellstruncated transporterInsect ProteinsHeterologous expressionMultidrug Resistance-Associated ProteinsToxins
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Stimulation of Defense Reactions in Medicago truncatula by Antagonistic Lipopeptides from Paenibacillus sp. Strain B2

2010

ABSTRACT With the aim of obtaining new strategies to control plant diseases, we investigated the ability of antagonistic lipopolypeptides (paenimyxin) from Paenibacillus sp. strain B2 to elicit hydrogen peroxide (H 2 O 2 ) production and several defense-related genes in the model legume Medicago truncatula . For this purpose, M. truncatula cell suspensions were used and a pathosystem between M. truncatula and Fusarium acuminatum was established. In M. truncatula cell cultures, the induction of H 2 O 2 reached a maximum 20 min after elicitation with paenimyxin, whereas concentrations higher than 20 μM inhibited H 2 O 2 induction and this was correlated with a lethal effect. In plant roots in…

0106 biological sciencesChalcone synthaseCell Culture TechniquesPhenylalanine ammonia-lyase01 natural sciencesApplied Microbiology and BiotechnologyPlant RootsMicrobiologyCell wall03 medical and health sciencesPathosystemPaenibacillusLipopeptidesPlant MicrobiologyFusariumGene Expression Regulation Plant030304 developmental biology[SDV.EE]Life Sciences [q-bio]/Ecology environment0303 health sciencesEcologybiologyfungiPANIBACILLUS SP. STRAIN B2food and beveragesHydrogen Peroxidebiology.organism_classificationMedicago truncatulaCoculture TechniquesInvertaseChitinasebiology.proteinMEDICAGO TRUNCATULAPaenibacillus010606 plant biology & botanyFood ScienceBiotechnology
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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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Insecticidal Activity of Bacillus thuringiensis Proteins against Coleopteran Pests

2020

Bacillus thuringiensis is the most successful microbial insecticide agent and its proteins have been studied for many years due to its toxicity against insects mainly belonging to the orders Lepidoptera, Diptera and Coleoptera, which are pests of agro-forestry and medical-veterinary interest. However, studies on the interactions between this bacterium and the insect species classified in the order Coleoptera are more limited when compared to other insect orders. To date, 45 Cry proteins, 2 Cyt proteins, 11 Vip proteins, and 2 Sip proteins have been reported with activity against coleopteran species. A number of these proteins have been successfully used in some insecticidal formulations and…

0106 biological sciencesCrops AgriculturalOrder ColeopteraHealth Toxicology and Mutagenesismedia_common.quotation_subjectBacillus thuringiensis proteinsBacillus thuringiensislcsh:MedicineInsectGenetically modified cropsReviewToxicologyInsecticidal activity01 natural sciencesinsecticidal activityLepidoptera genitalia03 medical and health sciencesHemolysin Proteinsmode of actionBacillus thuringiensisBotanyAnimalsstructureMode of actionPest Control Biologicalcoleopteran pests030304 developmental biologymedia_common0303 health sciencesbiologyBacillus thuringiensis Toxinslcsh:RfungiStructurebiology.organism_classificationPlants Genetically ModifiedColeopteraEndotoxins010602 entomologyBiological Control AgentsMode of actionColeopteran pests<i>Bacillus thuringiensis</i> proteinsBacteriaToxins
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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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