Search results for "Hemolysin Protein"

showing 10 items of 156 documents

Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (…

2004

AbstractBinding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis δ-endotoxins.In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry…

ProteasesBrush borderBacterial ToxinsBacillus thuringiensisBiophysicsmedicine.disease_causeBinding CompetitiveBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsProtoxin activationBinding siteProtein PrecursorsChymotrypsinBinding SitesbiologyBacillus thuringiensis ToxinsMicrovilliToxinColorado potato beetleCell MembranefungiCell Biologybiology.organism_classificationTrypsinColeopteraEndotoxinsBiochemistryMode of actionbiology.proteinmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Pore-forming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccharide.

1996

Cleavage of membrane-associated proteins with the release of biologically active macromolecules is an emerging theme in biology. However, little is known about the nature and regulation of the involved proteases or about the physiological inducers of the shedding process. We here report that rapid and massive shedding of the interleukin 6 receptor (IL-6R) and the lipopolysaccharide receptor (CD14) occurs from primary and transfected cells attacked by two prototypes of pore-forming bacterial toxins, streptolysin O and Escherichia coli hemolysin. Shedding is not induced by an streptolysin O toxin mutant which retains cell binding capacity but lacks pore-forming activity. The toxin-dependent c…

ProteasesCD14Lipopolysaccharide ReceptorsEnzyme-Linked Immunosorbent AssayBiologyTransfectionHemolysin ProteinsMonocytesCell LineHemolysin ProteinsBacterial ProteinsAntigens CDChlorocebus aethiopsEscherichia coliTumor Cells CulturedAnimalsHumansEnzyme InhibitorsReceptorCells CulturedMultidisciplinaryHaptoglobinsMacrophagesReceptors InterleukinTransfectionStaurosporineReceptors Interleukin-6Recombinant ProteinsKineticsBiochemistryStreptolysinsInterleukin-6 receptorTetradecanoylphorbol AcetateStreptolysinSignal transductionSignal TransductionResearch ArticleProceedings of the National Academy of Sciences
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A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border memb…

2007

AbstractInsect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin–receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprote…

ProteasesCell Membrane PermeabilityPore formationProteolysismedicine.medical_treatmentBacterial ToxinsBacillus thuringiensisBiophysicsInsecticidal toxinBiochemistryCry3Aa proteolysisHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineColorado potato beetleAnimalsMetalloprotease inhibitorMetalloproteinaseBinding SitesProteaseBacillus thuringiensis ToxinsMicrovillibiologymedicine.diagnostic_testSecretory VesiclesAcetohydroxamic acidColorado potato beetleCell Biologybiology.organism_classificationProteaseColeopteraEndotoxinsModels ChemicalBiochemistryPorosityProtein Bindingmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Functional significance of membrane associated proteolysis in the toxicity of Bacillus thuringiensis Cry3Aa toxin against Colorado potato beetle.

2012

Abstract Bacillus thuringiensis Cry toxins are widely used as biocontrol agents in bioinsecticides and transgenic plants. In the three domain-Cry toxins, domain II has been identified as an important determinant of their highly specific activity against insects. In this work, we assessed the role in membrane associated proteolysis and toxicity in Colorado potato beetle (CPB) of a previously reported ADAM recognition motif present in Cry3Aa toxin domain II. We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 344, 346, 347, 351 and 353 of the ADAM recognition motif in Cry3Aa toxin. Cry3Aa toxin mutants displayed decreased toxicity when comp…

ProteasesColoradoProteolysisMutantBacillus thuringiensisToxicologymedicine.disease_causeMicrobiologyHemolysin ProteinsRecognition sequenceBacterial ProteinsBacillus thuringiensismedicineAnimalsAmino Acid SequencePest Control BiologicalCells Culturedbiologymedicine.diagnostic_testBacillus thuringiensis ToxinsMicrovilliToxinfungiColorado potato beetleWild typeSequence Analysis DNAbiology.organism_classificationColeopteraEndotoxinsBiochemistryProteolysisMutagenesis Site-DirectedToxicon : official journal of the International Society on Toxinology
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Prohibitin, an essential protein for Colorado potato beetle larval viability, is relevant to Bacillus thuringiensis Cry3Aa toxicity

2013

Bacillus thuringienesis (Bt) Cry toxins constitute the most extensively used environmentally safe biopesticide and their mode of action relies on the interaction of the toxins with membrane proteins in the midgut of susceptible insects that mediate toxicity and insect specificity. Therefore, identification of Bt Cry toxin interacting proteins in the midgut of target insects and understanding their role in toxicity is of great interest to exploit their insecticidal action. Using ligand blot, we demonstrated that Bt Cry3Aa toxin bound to a 30kDa protein in Colorado potato beetle (CPB) larval midgut membrane, identified by sequence homology as prohibitin-1 protein. Prohibitins comprise a highl…

ProteasesHealth Toxicology and MutagenesisBiologymedicine.disease_causeHemolysin ProteinsBacterial ProteinsRNA interferenceBacillus thuringiensisProhibitinsmedicineAnimalsProhibitinBinding siteMode of actionSolanum tuberosumBacillus thuringiensis ToxinsToxinfungiGeneral Medicinebiology.organism_classificationMolecular biologyColeopteraEndotoxinsRepressor ProteinsMembrane proteinBiochemistryLarvaAgronomy and Crop SciencePesticide Biochemistry and Physiology
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Unraveling the Composition of Insecticidal Crystal Proteins in Bacillus thuringiensis: a Proteomics Approach.

2020

ABSTRACT Bacillus thuringiensis (Bt) is the most widely used active ingredient for biological insecticides. The composition of δ-endotoxins (Cry and Cyt proteins) in the parasporal crystal determines the toxicity profile of each Bt strain. However, a reliable method for their identification and quantification has not been available, due to the high sequence identity of the genes that encode the δ-endotoxins and the toxins themselves. Here, we have developed an accurate and reproducible mass spectrometry-based method (liquid chromatography-tandem mass spectrometry-multiple reaction monitoring [LC-MS/MS-MRM]) using isotopically labeled proteotypic peptides for each protein in a particular mix…

ProteomicsInsecticidesProteomeQuantitative proteomicsBacillus thuringiensisProteomics01 natural sciencesApplied Microbiology and Biotechnology03 medical and health sciencesBiosafetyHemolysin ProteinsBacterial ProteinsTandem Mass SpectrometryBacillus thuringiensisInvertebrate Microbiology030304 developmental biologyPhytosanitary certificationActive ingredient0303 health sciencesChromatographyEcologybiologyBacillus thuringiensis ToxinsChemistry010401 analytical chemistrybiology.organism_classification0104 chemical sciencesEndotoxinsComposition (visual arts)FermentationFood ScienceBiotechnologyChromatography LiquidApplied and environmental microbiology
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Characterization ofBacillus thuringiensisserovarbolivia(serotype H63), a novel serovar isolated from the Bolivian high valleys

1999

The type strain Bacillus thuringiensis var. bolivia (serotype H63), isolated from the Bolivian high valleys, has been characterized at different levels. Its parasporal crystal has an unusual shape and it is composed of a protein of 155 kDa which shows two bands of 75 and 80 kDa after activation. Analysis by PCR shows the presence of cry1 genes, and amplification with specific primers gave products for cry1 E, cry1 D, cry4 A and cry4 B with sizes different to those expected. Immunoblotting tests showed positive reaction for Cry1 E, Cry3 A, Cry4 A and Cry11 A crystal proteins. The plasmid pattern revealed two large and two small plasmids. Toxicity tests were performed against 14 insects and a…

SerotypeBoliviaBacterial ToxinsBlotting WesternBacillus thuringiensisApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsPlasmidBacterial ProteinsBacillus thuringiensisTrichoplusiaAnimalsBacillaceaeBacillus thuringiensis ToxinsbiologyStrain (chemistry)fungiParasporal bodybiology.organism_classificationBacillalesColeopteraEndotoxinsLarvaMicroscopy Electron ScanningElectrophoresis Polyacrylamide GelPlasmidsLetters in Applied Microbiology
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Surface and virulence properties of environmental Vibrio cholerae non-O1 from Albufera Lake (Valencia, Spain).

1990

A total of 140 environmental Vibrio cholerae non-O1 isolates, together with several culture collection strains from both environmental and clinical sources, were studied in relation to hemagglutination, surface hydrophobicity, and the enzymatic, hemolytic, cytotoxic, and enterotoxic activities of their extracellular products. A total of 78 and 62% of the strains produced hemagglutinins and exohemagglutinins, respectively. Four different hemagglutinating and two exohemagglutinating activities were found by using eight sugars in the inhibition assays. Cell-bound mannose-sensitive hemagglutination was detected mainly in chicken blood, whereas fucose-sensitive hemagglutination was recorded only…

SerotypeHemagglutinationVirulenceFresh WaterEnterotoxinBiologymedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsVibrio cholerae non-O1VibrionaceaemedicineVibrio choleraeAntigens BacterialEcologyVirulenceCytotoxinsO AntigensHemagglutininbiology.organism_classificationEnzymesHemagglutininsVibrio choleraeSpainWater MicrobiologyFood ScienceBiotechnologyPlasmidsResearch ArticleApplied and environmental microbiology
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Characterization of Bacillus thuringiensis ser. balearica (Serotype H48) and ser. navarrensis (serotype H50): two novel serovars isolated in Spain.

2000

The novel strains of Bacillus thuringiensis PM9 and NA69, isolated from soil samples in Spain, were classified and characterized in terms of their crystal proteins, plasmid profile, cry genes content, and their toxicological properties against several species of Lepidoptera, Coleoptera, and Diptera. Both strains share morphological and biochemical characteristics with previously described B. thuringiensis strains, although their unique H antigens identify them as two new serotypes. Two new serovar names, B. thuringiensis serovar balearica (H serotype 48) and B. thuringiensis serovar navarrensis (H serotype 50) are proposed for the type strains PM9 and NA69, respectively.

SerotypeInsectaBacterial ToxinsImmunoblottingBacillus thuringiensisH antigenApplied Microbiology and BiotechnologyMicrobiologyPolymerase Chain ReactionMicrobiologyLepidoptera genitaliaHemolysin ProteinsPlasmidBacterial ProteinsBacillus thuringiensisAnimalsTypingSerotypingPest Control BiologicalSoil MicrobiologyInclusion BodiesAntigens BacterialBacillaceaebiologyBacillus thuringiensis ToxinsfungiGeneral Medicinebiology.organism_classificationBacillalesBacterial Typing TechniquesEndotoxinsElectrophoresis Polyacrylamide GelPlasmidsCurrent microbiology
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Polynucleotide differentiation using hybrid solid-state nanopore functionalizing with α-hemolysin

2019

We report results from full atomistic molecular dynamics simulations on the properties of biomimetic nanopores. This latter result was obtained through the direct insertion of an α-hemolysin protein inside a hydrophobic solid-state nanopore. Upon translocation of different DNA strands, we demonstrate here that the theoretical system presents the same discrimination properties as the experimental one obtained previously. This opens an interesting way to promote the stability of a specific protein inside a solid nanopore to develop further biomimetic applications for DNA or protein sequencing.

Specific proteinPolynucleotidesSolid-state02 engineering and technologyMolecular Dynamics Simulation010402 general chemistry01 natural sciencesHemolysin ProteinsNanoporesMolecular dynamicschemistry.chemical_compoundProtein sequencingBiomimeticsAmino Acid SequenceChemistryHemolysinDNAGeneral Chemistry021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesNanoporePolynucleotideBiophysics0210 nano-technologyHydrophobic and Hydrophilic InteractionsDNASoft Matter
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