Search results for " Toxins"

showing 10 items of 330 documents

A novel cytotoxin from Clostridium difficile serogroup F is a functional hybrid between two other large clostridial cytotoxins.

1999

Abstract The large clostridial cytotoxins (LCTs) constitute a group of high molecular weight clostridial cytotoxins that inactivate cellular small GTP-binding proteins. We demonstrate that a novel LCT (TcdB-1470) from Clostridium difficile strain 1470 is a functional hybrid between “reference” TcdB-10463 andClostridium sordellii TcsL-1522. It bound to the same specific receptor as TcdB-10463 but glucosylated the same GTP-binding proteins as TcsL-1522. All three toxins had equal enzymatic potencies but were equally cytotoxic only when microinjected. When applied extracellularly TcdB-1470 and TcdB-10463 were considerably more potent cytotoxins than TcsL-1522. The small GTP-binding protein R-R…

GlycosylationRecombinant Fusion ProteinsCellBacterial ToxinsGTPasemedicine.disease_causeBiochemistryMiceClostridiummedicineCell AdhesionCytotoxic T cellAnimalsReceptorCytotoxicityMolecular BiologyDNA Primerschemistry.chemical_classificationbiologyBase SequenceToxinClostridioides difficileCytotoxinsCell Biology3T3 Cellsbiology.organism_classificationmedicine.anatomical_structureEnzymeBiochemistrychemistryMicroscopy Electron ScanningThe Journal of biological chemistry
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Structural Domains of the Bacillus thuringiensis Vip3Af Protein Unraveled by Tryptic Digestion of Alanine Mutants

2019

Vip3 proteins are increasingly used in insect control in transgenic crops. To shed light on the structure of these proteins, we used the approach of the trypsin fragmentation of mutants altering the conformation of the Vip3Af protein. From an alanine scanning of Vip3Af, we selected mutants with an altered proteolytic pattern. Based on protease digestion patterns, their effect on oligomer formation, and theoretical cleavage sites, we generated a map of the Vip3Af protein with five domains which match some of the domains proposed independently by two in silico models. Domain I ranges amino acids (aa) 12&ndash

Health Toxicology and MutagenesisIn silicoMutantlcsh:MedicineToxicologyCleavage (embryo)03 medical and health sciencesagricultural_sciences_agronomytetrameric proteinsTetramerinsecticidal proteinsmedicineBt toxins030304 developmental biologychemistry.chemical_classificationAlanine0303 health sciences030306 microbiologyChemistrylcsh:RAlanine scanningtrypsin cleavageTrypsinAmino acidBiochemistrydomain mapmedicine.drugToxins
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Sequence of lethal events in HeLa cells exposed to the G2 blocking cytolethal distending toxin

2000

The bacterial cytolethal distending toxin (CDT) was previously shown to block the cell cycle of several cell lines at stage G2 through inactivation of the cyclin-dependent kinase Cdkl and without induction of DNA strand breaks. In the present study, we have analyzed, using various methods of analytical cytometry, the progressive transformation and delayed lethal events in the tumor-derived HeLa cell line temporarily exposed to CDT. The cell proliferation arrest induced by CDT was irreversible but, starting about two days after exposure, the G2 block released partially, concomitantly with a decline in the level of Cdkl phosphorylation. This partial release resulted in endoreduplication, lead…

HistologyTime FactorsCytolethal distending toxinCell divisionAntimetabolitesCell Survival[SDV]Life Sciences [q-bio]Bacterial ToxinsMitosisApoptosisKINASE CYCLIQUE DEPENDANTEBiologyCyclin BPathology and Forensic MedicineCDC2 Protein KinaseEndoreduplicationHumansCyclin B1PhosphorylationMitosisCentrosomeCell DeathCell growthCell BiologyGeneral MedicineCell cycleFlow CytometryVirologyMolecular biologyImmunohistochemistry[SDV] Life Sciences [q-bio]BromodeoxyuridineMicroscopy FluorescenceCell cultureApoptosisCell DivisionHeLa Cells
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Toxic and enzymatic activities of Vibrio vulnificus biotype 2 with respect to host specificity

1996

In this work, the enzymatic activities of selected strains of biotypes 1 and 2 of Vabrio vulnificus were analyzed by using conventional methods and the API ZYM system. The toxic activities of extracellular products (ECPs) were further evaluated by in vitro and in vivo experiments. The ECPs of both biotypes (i) showed high-level hydrolytic activities, (ii) displayed cytotoxicity for fish cell lines, and (iii) were lethal for eels. Exotoxins seem to be proteinaceous since heat treatment of ECP samples destroyed their toxicity. Only biotype 2 strains were virulent for cels, suggesting that host specificity must be related to differences in cell surface properties. Infectivity trials with other…

Hot TemperatureBacterial ToxinsExotoxinsVirulenceVibrio vulnificusBiologyApplied Microbiology and BiotechnologyCell LineMicrobiologyfluids and secretionsSpecies SpecificityVibrionaceaeExtracellularAnimalsCytotoxicityVibrioInfectivityEelsCell DeathVirulenceEcologyHydrolysisFishesbiology.organism_classificationVibrioBacterial Typing TechniquesBacteriaResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum*

2013

Understanding how Bacillus thuringiensis (Bt) toxins interact with proteins in the midgut of susceptible coleopteran insects is crucial to fully explain the molecular bases of Bt specificity and insecticidal action. In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sodium solute symporter (TcSSS) have been identified by ligand blot as putative Cry3Ba toxin-binding proteins in Tribolium castaneum (Tc) larvae. RNA interference knockdown of TcCad1 or TcSSS proteins resulted in decreased susceptibility to Cry3Ba toxin, demonstrating the Cry toxin receptor functionality for these proteins. In contrast, TcAPN-I silencing had no effect on Cry3Ba larval toxicity, suggesting that th…

ImmunoblottingMolecular Sequence DataReceptors Cell SurfacePlasma protein bindingBiologyCD13 Antigensmedicine.disease_causeBiochemistrySodium-solute symporterdigestive systemMicrobiologyEpitopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisparasitic diseasesmedicineAnimalsAmino Acid SequenceReceptorMolecular BiologyPeptide sequenceTriboliumBinding SitesBacillus thuringiensis ToxinsSequence Homology Amino AcidSymportersCadherinToxinfungiSodiumCell Biologybiology.organism_classificationCadherinsEndotoxinsBiochemistrySymporterbacteriaInsect ProteinsRNA InterferenceProtein Binding
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Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation.

1994

Chemical modification of histidine residues in staphylococcal alpha-toxin leads to loss of functional activity. Site-directed mutants of the toxin in which each of the four histidine residues was replaced by several amino acids were therefore produced. The mutant proteins were purified and characterized. Exchange of H-259 or H-144 was sometimes tolerated without reduction in hemolytic activity. These histidine residues are thus not essential for toxin function. Exchange of H-35 and H-48, however, had marked effects. H-35 mutant toxins bound with high affinity to rabbit erythrocytes but displayed faulty oligomerization and were unable to form pores. H-48 mutant toxins also had severely impai…

ImmunologyMutantBacterial ToxinsBiologyHemolysin Proteinsmedicine.disease_causeMicrobiologyHemolysisHemolysin ProteinsStructure-Activity RelationshipmedicineStructure–activity relationshipAnimalsHistidineHistidinechemistry.chemical_classificationToxinErythrocyte Membranebiology.organism_classificationAmino acidN-terminusInfectious DiseaseschemistryBiochemistryMutagenesis Site-DirectedParasitologyRabbitsBacteriaResearch Article
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Binding analyses of Cry1Ab and Cry1Ac with membrane vesicles from Bacillus thuringiensis-resistant and -susceptible Ostrinia nubilalis.

2004

The binding properties of Bacillus thuringiensis toxins to brush border membrane vesicles of Dipel-resistant and -susceptible Ostrinia nubilalis larvae were compared using ligand-toxin immunoblot analysis, surface plasmon resonance (SPR), and radiolabeled toxin binding assays. In ligand-toxin immunoblot analysis, the number of Cry1Ab or Cry1Ac toxin binding proteins and the relative toxin binding intensity were similar in vesicles from resistant and susceptible larvae. Surface plasmon resonance with immobilized activated Cry1Ab toxin indicated that there were no significant differences in binding with fluid-phase vesicles from resistant and susceptible larvae. Homologous competition assays …

InsectaTime FactorsBrush borderBacterial ToxinsImmunoblottingBiophysicsBacillus thuringiensisReceptors Cell SurfacePlasma protein bindingBiologyMothsmedicine.disease_causeLigandsBiochemistryBinding CompetitiveCell membraneHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding sitePest Control BiologicalMolecular BiologyBinding SitesBacillus thuringiensis ToxinsDose-Response Relationship DrugMicrovilliToxinVesiclefungiCell Membranefood and beveragesCell BiologySurface Plasmon Resonancebiology.organism_classificationMolecular biologyEndotoxinsKineticsmedicine.anatomical_structureCry1AcBiochemistryInsect ProteinsProtein BindingBiochemical and biophysical research communications
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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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Screening for Bacillus thuringiensis Crystal Proteins Active against the Cabbage Looper, Trichoplusia ni

2000

Abstract Toxicity tests were performed to find among Cry1 and Cry2 Bacillus thuringiensis crystal proteins those with high activity against the cabbage looper. Tests were performed with neonate larvae on surface-contaminated artificial diet. The crystal proteins found to be toxic were, from higher to lower toxicity: Cry1Ac, Cry1Ab, Cry1C, Cry2Aa, Cry1J, and Cry1F (LC50 of 1.1–4.1, 3.4–4.4, 12, 34, 87, and 250 ng/cm2, respectively). Cry1B, Cry1D, and Cry1E can be considered nontoxic (LC50 higher than 2500 ng/cm2). Cry1Aa was moderately toxic to nontoxic, depending on the source (LC50 of 420 ng/cm2 from PGS and 8100 ng/cm2 from Ecogen). In vitro binding assays with trypsin-activated 125I-labe…

InsecticidesBacillus thuringiensis ToxinsBrush borderBacterial ToxinsfungiBacillus thuringiensisMidgutMothsBiologybiology.organism_classificationBacillalesEndotoxinsIodine RadioisotopesHemolysin ProteinsBacterial ProteinsCry1AcBiochemistryCabbage looperBacillus thuringiensisBotanyToxicityTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsJournal of Invertebrate Pathology
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Synergism and Antagonism between Bacillus thuringiensis Vip3A and Cry1 Proteins in Heliothis virescens, Diatraea saccharalis and Spodoptera frugiperda

2014

Made available in DSpace on 2015-03-18T15:56:04Z (GMT). No. of bitstreams: 0 Previous issue date: 2014-10-02Bitstream added on 2015-03-18T16:28:28Z : No. of bitstreams: 1 WOS000342591500006.pdf: 270331 bytes, checksum: c280e3f5bc5e3bb0b92bf74d046135f0 (MD5) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Spanish Ministry of Economy and Competivity FEDER Second generation Bt crops (insect resistant crops carrying Bacillus thuringiensis genes) combine more than one gene that codes for insecticidal proteins in the same plant to provide better control of agricultural pests. Some of the new combinations involve co-expression of cry and vip genes. Because Cry and Vip proteins …

InsecticidesBacillus thuringiensislcsh:MedicineSpodopteraSpodopteraDiatraea saccharalisHemolysin ProteinsLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyGeneticsEscherichia coliAnimalslcsh:ScienceMolecular BiologyMultidisciplinarybiologyHeliothis virescensBacillus thuringiensis Toxinslcsh:RfungiBiology and Life SciencesAgriculturebiology.organism_classificationEndotoxinsLepidopteraBiochemistryCry1AcLarvalcsh:QElectrophoresis Polyacrylamide GelPest ControlAntagonismZoologyEntomologyResearch ArticleBiotechnologyProtein BindingPLoS ONE
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