Search results for " Toxins"

showing 10 items of 330 documents

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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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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Repair of a Bacterial Small β-Barrel Toxin Pore Depends on Channel Width

2017

ABSTRACT Membrane repair emerges as an innate defense protecting target cells against bacterial pore-forming toxins. Here, we report the first paradigm of Ca2+-dependent repair following attack by a small β-pore-forming toxin, namely, plasmid-encoded phobalysin of Photobacterium damselae subsp. damselae. In striking contrast, Vibrio cholerae cytolysin, the closest ortholog of phobalysin, subverted repair. Mutational analysis uncovered a role of channel width in toxicity and repair. Thus, the replacement of serine at phobalysin´s presumed channel narrow point with the bulkier tryptophan, the corresponding residue in Vibrio cholerae cytolysin (W318), modulated Ca2+ influx, lysosomal exocytosi…

0301 basic medicineBacterial ToxinsAerolysinmedicine.disease_causeMicrobiologySerine03 medical and health sciencesNanoporesVirologyExtracellularmedicineHumansVibrio choleraeChemistryToxinPerforinCell MembraneQR1-502Transmembrane proteinCell biology030104 developmental biologyPhotobacterium damselaeVibrio choleraeCalciumCytolysinResearch ArticlemBio
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The mycotoxin zearalenone enhances cell proliferation, colony formation and promotes cell migration in the human colon carcinoma cell line HCT116.

2016

IF 3.522; International audience; Zearalenone (ZEN) and Aflatoxin B1 (AFB1) are fungal secondary metabolites produced by Fusarium and Aspergillus genera, respectively. These mycotoxins are found world-wide as corn and wheat contaminants. AFB1 is probably the most toxic and carcinogenic mycotoxin. It has been demonstrated to be mutagenic, genotoxic, and hepatocarcinogenic. ZEN is a non-steroidal estrogenic mycotoxin that displays hepatotoxicity, immunotoxicity and genotoxicity. Its mutagenic and carcinogenic properties have so far remained controversial and questionable. Using the colon carcinoma cell line HCT116, we will show here that ZEN, at low concentrations, enhances cell proliferation…

0301 basic medicineBone-Marrow-CellsAflatoxinAflatoxin B1Time Factors[ SDV.TOX ] Life Sciences [q-bio]/ToxicologyToxicologymedicine.disease_causeInductionchemistry.chemical_compound0302 clinical medicineProliferation assayCell MovementZearalenonebiologyfood and beveragesCell migrationGeneral MedicineMigration assayDna-Damage030220 oncology & carcinogenesis[SDV.TOX]Life Sciences [q-bio]/ToxicologyColonic NeoplasmsZearalenoneChromosome-AberrationsBalb/C MiceFusariumendocrine systemPreventive Role03 medical and health sciencesBotanymedicineHumansNeoplasm InvasivenessMycotoxinCarcinogenCell ProliferationWound HealingDose-Response Relationship DrugCell growthfungiClonogenic assaybiology.organism_classificationHCT116 CellsMolecular biology030104 developmental biologychemistryMcf-7 CellsFusarium ToxinsIn-VitroVitamin-ECarcinogensGenotoxicityToxicology letters
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Staphylococcus aureus α-toxin: small pore, large consequences

2018

Abstract The small β-pore-forming α-toxin, also termed α-hemolysin or Hla is considered to be an important virulence factor of Staphylococcus aureus. Perforation of the plasma membrane (PM) by Hla leads to uncontrolled flux of ions and water. Already a small number of toxin pores seems to be sufficient to induce complex cellular responses, many of which depend on the efflux of potassium. In this article, we discuss the implications of secondary membrane lesions, for example, by endogenous channels, for Hla-mediated toxicity, for calcium-influx and membrane repair. Activation of purinergic receptors has been proposed to be a major contributor to the lytic effects of various pore forming prot…

0301 basic medicineCell Membrane PermeabilityStaphylococcal ToxoidBacterial ToxinsClinical BiochemistryPerforation (oil well)Endocytosismedicine.disease_causeBiochemistryVirulence factorHemolysin Proteins03 medical and health sciencesCytosol0302 clinical medicinemedicineHumansMolecular BiologyPore-forming toxinIon TransportChemistryToxinCell MembranePurinergic receptorCell biologyCytosol030104 developmental biologyCalciumEffluxProtein Kinases030217 neurology & neurosurgeryBiological Chemistry
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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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Grey Matter Microstructural Integrity Alterations in Blepharospasm Are Partially Reversed by Botulinum Neurotoxin Therapy.

2016

OBJECTIVE Benign Essential Blepharospasm (BEB) and hemifacial spasm (HFS) are the most common hyperkinetic movement disorders of facial muscles. Although similar in clinical presentation different pathophysiological mechanisms are assumed. Botulinum Neurotoxin (BoNT) is a standard evidence-based treatment for both conditions. In this study we aimed to assess grey matter microstructural differences between these two groups of patients and compared them with healthy controls. In patients we furthermore tracked the longitudinal morphometric changes associated with BoNT therapy. We hypothesized microstructural differences between the groups at the time point of maximum symptoms representation a…

0301 basic medicineCentral Nervous SystemMaleMovement disordersBotulinum ToxinsBlepharospasmlcsh:MedicineToxicologyPathology and Laboratory MedicineNervous SystemDiagnostic Radiology0302 clinical medicineMaterials PhysicsMedicine and Health SciencesToxinsLongitudinal StudiesGray Matterlcsh:ScienceMicrostructureMultidisciplinaryMovement DisordersRadiology and ImagingPhysicsMotor CortexBrainNeurodegenerative DiseasesAnatomyMiddle AgedMagnetic Resonance ImagingPathophysiologyBotulinum neurotoxinFacial musclesDystoniamedicine.anatomical_structureTreatment OutcomeNeurologyPhysical SciencesFemalePrimary motor cortexmedicine.symptomAnatomyResearch ArticleAdultmedicine.medical_specialtyImaging TechniquesBlepharospasmToxic AgentsBacterial ToxinsMaterials ScienceBotulinum ToxinGrey matterResearch and Analysis Methods03 medical and health sciencesDiagnostic MedicineOphthalmologymedicineHumansHemifacial SpasmDemographyAgedbusiness.industrylcsh:RBiology and Life SciencesCorrectionmedicine.disease030104 developmental biologyCross-Sectional StudiesFacePeople and Placeslcsh:QbusinessHead030217 neurology & neurosurgeryHemifacial spasmPloS one
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Enterocyte Purge and Rapid Recovery Is a Resilience Reaction of the Gut Epithelium to Pore-Forming Toxin Attack.

2016

International audience; Besides digesting nutrients, the gut protects the host against invasion by pathogens. Enterocytes may be subjected to damage by both microbial and host defensive responses, causing their death. Here, we report a rapid epithelial response that alleviates infection stress and protects the enterocytes from the action of microbial virulence factors. Intestinal epithelia exposed to hemolysin, a pore-forming toxin secreted by Serratia marcescens, undergo an evolutionarily conserved process of thinning followed by the recovery of their initial thickness within a few hours. In response to hemolysin attack, Drosophila melanogaster enterocytes extrude most of their apical cyto…

0301 basic medicineCytoplasmDisease toleranceSurvivalApoptosismedicine.disease_causeOral infectionHemolysin ProteinsLipid droplet[SDV.IDA]Life Sciences [q-bio]/Food engineeringMitochondrial extrusionIntestinal MucosaSerratia marcescensBacterial-infectionPore-forming toxinbiologyCell DeathMicrovilliPlasma-membrane[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringGut EpitheliumMitochondriamedicine.anatomical_structureDrosophila melanogasterEnterocyteVirulence FactorsVarroidaeSerratia-marcescensBacterial ToxinsVirulenceMicrobiologyMicrobiologySerratia Infections03 medical and health sciencesVirologymedicineAnimalsApical cytoplasmDefense strategyDrosophila cyclin jToxinbiology.organism_classificationLipid dropletsDisease Models AnimalIntestinal Diseases030104 developmental biologyEnterocytesSerratia marcescensParasitologyDigestive SystemCell hostmicrobe
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