Search results for "Hemolysin"

showing 10 items of 169 documents

Purification and characterization of a pore-forming protein from the marine sponge Tethya lyncurium

1992

A pore-forming protein was detected and purified for the first time from a marine sponge (Tethya lyncurium). The purified protein has a polypeptide molecular mass of 21 kDa and a pI of 6.4. Tethya pore-forming protein (also called Tethya hemolysin) rapidly lysed erythrocytes from a variety of organisms. After binding to target membranes, the hemolysin resisted elution with EDTA, salt or solutions of low ionic strength and hence resembled an integral membrane protein. Erythrocytes could be protected from hemolysis induced by Tethya hemolysin by addition of 30 mM dextran 4 (4-6 kDa; equivalent hydrodynamic diffusion radius, 1.75-2.3 nm) to the extracellular medium, but not by addition of unch…

Cell Membrane PermeabilityLysisChemical PhenomenaCarbohydratesHemolysisBiochemistryPore forming proteinHemolysin ProteinsAdenosine TriphosphateOsmotic PressureAnimalsHumansColloidsIntegral membrane proteinSheepbiologyMolecular massChemistry PhysicalErythrocyte MembraneDextransHemolysinMembrane transportbiology.organism_classificationPoriferaMolecular WeightMicroscopy ElectronMembraneBiochemistryChromatography GelPotassiumTethyaRabbits
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Toxicity and mode of action of Bacillus thuringiensis Cry proteins in the Mediterranean corn borer, Sesamia nonagrioides (Lefebvre)

2006

ABSTRACT Sesamia nonagrioides is one of the most damaging pests of corn in Spain and other Mediterranean countries. Bt corn expressing the Bacillus thuringiensis Cry1Ab toxin is being grown on about 58,000 ha in Spain. Here we studied the mode of action of this Cry protein on S. nonagrioides (binding to specific receptors, stability of binding, and pore formation) and the modes of action of other Cry proteins that were found to be active in this work (Cry1Ac, Cry1Ca, and Cry1Fa). Binding assays were performed with 125 I- or biotin-labeled toxins and larval brush border membrane vesicles (BBMV). Competition experiments indicated that these toxins bind specifically and that Cry1Aa, Cry1Ab, an…

Cell Membrane PermeabilityMembrane permeabilityBacterial ToxinsBacillus thuringiensisSesamia nonagrioidesBacterial ToxinBacterial ProteinZea maysApplied Microbiology and BiotechnologyOstriniaHemolysin ProteinsZea mayBacterial ProteinsEndotoxinBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBacillus thuringiensiBinding siteMode of actionPest Control BiologicalGenetically modified maizeBacillus thuringiensis ToxinsEcologybiologyMicrovilliAnimalfungifood and beveragesHemolysin Proteinbiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraCry1AcBiochemistryLarvaFood ScienceBiotechnology
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Superoxide generation by human neutrophils induced by low doses of Escherichia coli hemolysin.

1991

Escherichia coli hemolysin (Hly) was isolated from bacterial culture supernatants by polyethylene glycol precipitation and centrifugation in glycerol density gradients. The toxin preparations contained less than 1 mol of lipopolysaccharide per 10 mol of protein, and they had no fatty acids. The capacity of purified hemolysin to stimulate superoxide anion production in polymorphonuclear leukocytes was monitored kinetically in a lumimeter by using the lucigenin assay and was correlated with the kinetics of transmembrane pore formation. When applied to leukocytes suspended in protein-free buffer, very low concentrations (0.02 to 0.1 HU/ml) of the toxin strongly stimulated the production of sup…

Cell Membrane PermeabilityNeutrophilsImmunologyBacterial ToxinsBiologymedicine.disease_causeHemolysin ProteinsMicrobiologychemistry.chemical_compoundHemolysin ProteinsBacterial ProteinsSuperoxidesmedicineEscherichia coliHumansCentrifugationLucigeninEscherichia coliSuperoxideToxinEscherichia coli ProteinsHemolysinFlow CytometryRespiratory burstKineticsInfectious DiseaseschemistryBiochemistryTetradecanoylphorbol AcetateParasitologyPropidiumResearch ArticleInfection and immunity
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The cytotoxin-hemolysin genes of human and eel pathogenic Vibrio vulnificus strains: comparison of nucleotide sequences and application to the geneti…

2005

Vibrio vulnificus can be divided into two groups on the basis of pathogenesis. Group 1 is pathogenic only to humans, whereas group 2 is pathogenic to eels and occasionally to humans. Although both groups produce a 50-kDa cytotoxin-hemolysin (V. vulnificus hemolysin; VVH), the toxins are different. In the present study, the nucleotide sequence of the toxin gene (vvhA ) of strain CDC B3547 (a group 2 strain) was determined, and the deduced amino acid sequence was compared to that of strain L-180 (a group 1 strain). The nucleotide sequence of vvhA of strain CDC B3547 was about 96% identical with that of strain L-180, which results in a difference of 3 amino acid residues in the C-terminal lect…

Cholera ToxinSequence analysisImmunologyMolecular Sequence DataVirulenceVibrio vulnificusBiologyMicrobiologyPolymerase Chain ReactionMicrobiologyHemolysin ProteinsVirologyAnimalsHumansGenePeptide sequenceVibrio vulnificusEelsStrain (chemistry)Base SequenceNucleic acid sequenceHemolysinSequence Analysis DNAbiology.organism_classificationGenes BacterialVibrio InfectionsMicrobiology and immunology
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Cholesterol reporter molecules.

2007

Cholesterol is a major constituent of the membranes in most eukaryotic cells where it fulfills multiple functions. Cholesterol regulates the physical state of the phospholipid bilayer, affects the activity of several membrane proteins, and is the precursor for steroid hormones and bile acids. Cholesterol plays a crucial role in the formation of membrane microdomains such as “lipid rafts” and caveolae. However, our current understanding on the membrane organization, intracellular distribution and trafficking of cholesterol is rather poor. This is mainly due to inherent difficulties to label and track this small lipid. In this review, we describe different approaches to detect cholesterol in …

Cholesterol oxidaseBacterial ToxinsBiophysicsBiologyBiochemistryFilipinchemistry.chemical_compoundHemolysin ProteinsMembrane MicrodomainsCaveolaeAnimalsHumansFilipinLipid bilayerMolecular BiologyLipid raftFluorescent DyesCholesterolCholesterol OxidaseCholesterol bindingCell BiologyCholesterolEukaryotic CellschemistryMembrane proteinBiochemistryMolecular Probeslipids (amino acids peptides and proteins)Bioscience reports
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Interaction ofEscherichia colihemolysin with biological membranes

2001

Escherichia coli hemolysin (HlyA) is a membrane-permeabilizing protein belonging to the family of RTX-toxins. Lytic activity depends on binding of Ca2(+) to the C-terminus of the molecule. The N-terminus of HlyA harbors hydrophobic sequences that are believed to constitute the membrane-inserting domain. In this study, 13 HlyA cysteine-replacement mutants were constructed and labeled with the polarity-sensitive fluorescent probe 6-bromoacetyl-2-dimethylaminonaphthalene (badan). The fluorescence emission of the label was examined in soluble and membrane-bound toxin. Binding effected a major blue shift in the emission of six residues within the N-terminal hydrophobic domain, indicating inserti…

Conformational changeProtein ConformationPlasma protein bindingBiologymedicine.disease_causeHemolysisBiochemistryHemolysin ProteinsProtein structureBacterial Proteins2-NaphthylamineEscherichia colimedicineCysteineCloning MolecularLipid bilayerEscherichia coliFluorescent DyesEscherichia coli ProteinsCell MembraneErythrocyte MembraneBiological membraneProtein Structure TertiarySpectrometry FluorescenceMembraneBiochemistryMutagenesisLiposomesChromatography GelCalciumElectrophoresis Polyacrylamide GelProtein BindingBinding domainEuropean Journal of Biochemistry
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Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.

1996

Staphylococcus aureus alpha-toxin is a hydrophilic polypeptide of 293 amino acids that produces heptameric transmembrane pores. During assembly, the formation of a pre-pore precedes membrane permeabilization; the latter is linked to a conformational change in the oligomer. Here, 41 single-cysteine replacement toxin mutants were thiol-specifically labelled with the polarity-sensitive fluorescent probe acrylodan. After oligomerization on membranes, only the mutants with acrylodan attached to residues in the sequence 118-140 exhibited a marked blue shift in the fluorescence emission maximum, indicative of movement of the fluorophore to a hydrophobic environment. Within this region, two functio…

Conformational changeStaphylococcus aureusProtein ConformationMembrane lipidsBacterial ToxinsMolecular Sequence DataBiologyGeneral Biochemistry Genetics and Molecular BiologyCell membraneHemolysin ProteinsProtein structure2-NaphthylaminemedicinePoint MutationAmino Acid SequenceCysteineMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesGeneral Immunology and MicrobiologyMolecular StructureGeneral NeuroscienceCell MembraneTransmembrane proteinAmino acidmedicine.anatomical_structureMembraneSpectrometry FluorescenceBiochemistrychemistryLiposomesBiophysicsMutagenesis Site-DirectedResearch ArticleThe EMBO journal
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Midgut microbiota and host immunocompetence underlie Bacillus thuringiensis killing mechanism

2016

Bacillus thuringiensis is a widely used bacterial entomopathogen producing insecticidal toxins, some of which are expressed in insect-resistant transgenic crops. Surprisingly, the killing mechanism of B. thuringiensis remains controversial. In particular, the importance of the septicemia induced by the host midgut microbiota is still debated as a result of the lack of experimental evidence obtained without drastic manipulation of the midgut and its content. Here this key issue is addressed by RNAi-mediated silencing of an immune gene in a lepidopteran host Spodoptera littoralis, leaving the midgut microbiota unaltered. The resulting cellular immunosuppression was characterized by a reduced …

Crops Agricultural0301 basic medicineHemocytesSerratiaBacillus thuringiensisSpodopteraSerratiaMicrobiologyHemolysin Proteins03 medical and health sciencesBacterial ProteinsInsect-pathogen interactionImmunityBacillus thuringiensisAnimalsPest Control Biologicalbioinsecticide | insect-pathogen interactions | insect biocontrol | pore-forming toxins | immunitySpodoptera littoralisRNA Double-StrandedClostridiumImmunosuppression TherapyPore-forming toxinMultidisciplinaryBacillus thuringiensis ToxinsInsect biocontrolbiologyHost (biology)MicrobiotafungiImmunityMidgutBiological Sciencesbiology.organism_classificationImmunity InnateBioinsecticideEndotoxinsIntestines030104 developmental biologyGene Expression RegulationLarvaPore-forming toxinInsect ProteinsRNA InterferenceImmunocompetenceProceedings of the National Academy of Sciences
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The hemolysin-producer coelomocytes in Holothuria polii

1988

Using sodium metrizoate discontinuous gradients, two hemolysin-producer amebocyte populations have been separated from total circulating Holothuria polii coelomocytes. The amebocytes of population 1 are responsible for the production of the calcium-dependent and temperature-labile hemolysin, whereas those of population 2 produce the calcium-independent and temperature-stable one. The intracytoplasmic hemolysins were evidenced also by immunofluorescence. Petaloid and filipodial amebocytes were the only positive cell types.

Cytotoxicity ImmunologicAmebocyteeducation.field_of_studymedicine.diagnostic_testbiologyImmunologyPopulationTemperatureFluorescent Antibody TechniqueHemolysinImmunofluorescencebiology.organism_classificationMicrobiologyHemolysin ProteinsmedicineAnimalsHolothuriaeducationCoelomocyteEchinodermataDevelopmental BiologyDevelopmental & Comparative Immunology
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Cytotoxic activity of Ciona intestinalis (Tunicata) hemocytes: Properties of the in vitro reaction against erythrocyte targets

1993

Hemocytes (effectors) of Ciona intestinalis showed a natural cytotoxic capacity (HCA) when assayed in vitro against erythrocytes (targets). Cytotoxic cells lysed, to a variable extent, rabbit (RE), human (A, B, O), guinea pig, and sheep (SE) erythrocytes. Hemocyte cytotoxic activity (HCA) assayed against SE is a calcium-dependent reaction, occurs rapidly (15-30 min), at 25-37 degrees C over a wide range of pH (5.4-8.0). Assays were carried out using: 1) the medium in which hemocytes were maintained, 2) the soluble portion of hemocyte lysates, and 3) debris prepared from hemocyte lysates. Results suggest that HCA is a cell-mediated process that requires effector-target cell contacts. Anti-SE…

Cytotoxicity ImmunologicErythrocytesHemocytesLysisCiona intestinaliCytotoxicityHemolysinImmunologyCellHemocyteTunicateHemolymphmedicineAnimalsCytotoxic T cellCiona intestinalisInvertebrateCytotoxicitySheepbiologyHemolysinHemagglutination Testsbiology.organism_classificationMolecular biologyIn vitroCiona intestinalisRed blood cellmedicine.anatomical_structureImmunologySheep erythrocyteDevelopmental BiologyDevelopmental & Comparative Immunology
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