Search results for "Hemolysin Protein"

showing 10 items of 156 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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Chromosome-Encoded Hemolysin, Phospholipase, and Collagenase in Plasmidless Isolates of Photobacterium damselae subsp. damselae Contribute to Virulen…

2017

ABSTRACT Photobacterium damselae subsp. damselae is a pathogen of marine animals, including fish of importance in aquaculture. The virulence plasmid pPHDD1, characteristic of highly hemolytic isolates, encodes the hemolysins damselysin (Dly) and phobalysin (PhlyP). Strains lacking pPHDD1 constitute the vast majority of the isolates from fish outbreaks, but genetic studies to identify virulence factors in plasmidless strains are scarce. Here, we show that the chromosome I-encoded hemolysin PhlyC plays roles in virulence and cell toxicity in pPHDD1-negative isolates of this pathogen. By combining the analyses of whole genomes and of gene deletion mutants, we identified two hitherto uncharacte…

0301 basic medicine030106 microbiologyVirulenceGenetics and Molecular BiologyBiologyHemolysin ProteinsApplied Microbiology and BiotechnologyMicrobiology03 medical and health sciencesFish DiseasesHemolysin ProteinsPlasmidAnimalsCollagenasesPathogenEcologyVirulencePhotobacteriumHemolysinChromosomes BacterialPhotobacteriumbiology.organism_classification030104 developmental biologyPhotobacterium damselaePhospholipasesBassGram-Negative Bacterial InfectionsLecithinaseFood ScienceBiotechnologyPlasmidsApplied and environmental microbiology
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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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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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Editorial for Special Issue: The Insecticidal Bacterial Toxins in Modern Agriculture.

2017

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0301 basic medicineMicrobial toxinsBacillus thuringiensis Toxinsbusiness.industryHealth Toxicology and Mutagenesislcsh:RBacillus thuringiensislcsh:MedicineBiologyToxicologyPlants Genetically ModifiedBiotechnologyEndotoxins03 medical and health sciencesHemolysin Proteins030104 developmental biologyn/aEditorialBacterial ProteinsAgriculturebusinessPest Control BiologicalEcosystemToxins
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Whole-genome characterization of Shewanella algae strain SYT3 isolated from seawater reveals insight into hemolysis.

2018

Aim: To describe the genomic characteristics of seawater-borne hemolytic Shewanella algae and its resistance genes. Materials &amp; methods: Whole genome sequence of S. algae SYT3 was determined using llumina MiSeq platform. Multiple-database-based analysis was performed to identify the genetic background of its hemolytic activity and the antibiotic resistance genes. Results: S. algae SYT3 possesses a homolog of the hly operon involved in the synthesis of hemolysin. We also identified candidate genes associated with resistance to β-lactam antibiotics (bla OXA-55) and fluoroquinolone (qnrA3). Conclusion: The study provides an insight into the hemolytic activity of S. algae. Our findings als…

0301 basic medicineMicrobiology (medical)DNA BacterialShewanellaOperon030106 microbiologyTaiwanShewanella algaeMicrobial Sensitivity TestsMicrobiologyGenomeHemolysisbeta-LactamasesMicrobiology03 medical and health sciencesHemolysin ProteinsAntibiotic resistanceAlgaeBacterial ProteinsRNA Ribosomal 16SDrug Resistance BacterialmedicineHumansSeawaterGenePhylogenyWhole genome sequencingbiologyWhole Genome SequencingChromosome Mappingbiology.organism_classificationmedicine.diseaseHemolysisAnti-Bacterial AgentsBacterial Typing TechniquesGenome BacterialFuture microbiology
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Ephestia kuehniella tolerance to Bacillus thuringiensis Cry1Aa is associated with reduced oligomer formation

2016

The basis of the different susceptibility of Ephestia kuehniella to the Cry1Aa and Cry1Ac δ-endotoxins from Bacillus thuringiensis kurstaki BNS3 was studied. Both toxins bound specifically to the BBMV of E. kuehniella. The result of the ligand blot showed that Cry1Ac bound to three putative receptors of about 100, 65 and 80 kDa and Cry1Aa interacted only with a 100 kDa protein. Pronase digestion of the BBMV-bound toxins was used to analyze the toxin insertion. Both toxins inserted into the BBMV as monomers however, a 14 kDa peptide of α4-α5 which correspond to the oligomeric form of this peptide was detected in case of Cry1Ac only. Analysis of the in vitro oligomerisation of these toxins in…

0301 basic medicineProtein ConformationBacillus thuringiensisBiophysicsPeptidemedicine.disease_causeBiochemistryOligomerHemolysin Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsBacillus thuringiensismedicineAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis Toxins030102 biochemistry & molecular biologybiologyToxinfungiCell BiologyLigand (biochemistry)biology.organism_classificationEndotoxinsLepidopteraBlot030104 developmental biologyBiochemistryCry1AcchemistryProtein MultimerizationBiochemical and Biophysical Research Communications
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