Search results for "toxin"

showing 10 items of 1434 documents

Major histocompatibility complex class II binding site for streptococcal pyrogenic (erythrogenic) toxin A.

1994

Streptococcal pyrogenic exotoxin A (SPEA) is an important pathogenicity factor of group A streptococci. It is a member of the family of „superantigens” produced by Staphylococcus aureus and Streptococcus pyogenes and its T lymphocyte stimulating activity is involved into the pathogenesis of certain diseases caused by pyogenic streptococci. In this study we have produced and characterized recombinant SPEA molecules in Escherichia coli. These molecules are indistinguishable from natural SPEA in both T cell stimulatory and HLA class II binding activities. Human class II molecules are more efficient than mouse class II molecules in presenting SPEA to T cells. In binding tests to major histocomp…

Microbiology (medical)Recombinant Fusion ProteinsT-LymphocytesImmunologyAntigen presentationErythrogenic toxinBacterial ToxinsMolecular Sequence DataExotoxinsEnterotoxinmedicine.disease_causeMajor histocompatibility complexLymphocyte ActivationMicrobiologyCell LineMajor Histocompatibility ComplexEnterotoxinsMicestomatognathic systemBacterial ProteinsmedicineEscherichia coliImmunology and AllergyAnimalsHumansCells CulturedMice Inbred BALB CBinding SitesSuperantigensbiologyBase SequencePyrogensToxic shock syndromeMembrane ProteinsStreptococcusGeneral MedicineGene Expression Regulation BacterialHLA-DR Antigensmedicine.diseasebiology.organism_classificationSpeaStreptococcus pyogenesbiology.proteinExotoxinMedical microbiology and immunology
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Identification of group A porcine rotavirus strains bearing a novel VP4 (P) genotype in Italian swine herds.

2007

ABSTRACT The VP4 gene of a G5 Italian porcine rotavirus strain, 344/04-1, was nontypeable by PCR genotyping. The amino acid sequence of the full-length VP4 protein had low identity (≤76.6%) with the homologous sequences of representative strains of the remaining P genotypes, providing evidence for a novel P genotype.

Microbiology (medical)RotavirusGenotypeSwinevirusesMolecular Sequence DataReoviridaeViral Nonstructural Proteinsmedicine.disease_causeGroup AVirusRotavirus Infectionsfluids and secretionsRotavirusVirologyGenotypemedicineAnimalsPeptide sequenceGenotypingAntigens ViralGlycoproteinsToxins BiologicalSwine DiseasesbiologyStrain (biology)virus diseasesSequence Analysis DNAbiology.organism_classificationVirologyItalyCapsid Proteins
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Characterization of Shiga toxin-producing Escherichia coli O157:H7 isolated in Italy and in France

2002

ABSTRACT Twenty-one Escherichia coli O157:H7 strains isolated in northern Italy from sporadic cases of hemolytic-uremic syndrome and from cattle and food were characterized by virulence gene analysis, pulsed-field gel electrophoresis (PFGE) of Xba I-digested DNA, enterobacterial repetitive intergenic consensus (ERIC) sequence-based PCR (ERIC-PCR), and antibiotic resistance patterns and compared to 18 strains isolated in France from human cases of diarrhea, cattle, and the environment. Strains isolated in Sicily (southern Italy) from a local farm (one strain) and from calves just imported from France (11 strains) and Spain (six strains) were also typed. Whereas the eae and hlyA genes were al…

Microbiology (medical)Settore MED/07 - Microbiologia E Microbiologia ClinicaMeatEpidemiologyCattle DiseasesVirulenceMicrobial Sensitivity TestsEscherichia coli O157Shiga Toxin 1medicine.disease_causePolymerase Chain ReactionShiga Toxin 2law.inventionMicrobiologychemistry.chemical_compoundIntergenic regionShiga-like toxinlawGenotypePulsed-field gel electrophoresismedicineAnimalsHumansChildEscherichia coliEscherichia coli InfectionsPhylogenyPolymerase chain reactionVirulencebiologyShiga toxinShiga Toxin Escherichia coli O157:H7Anti-Bacterial AgentsBacterial Typing TechniquesElectrophoresis Gel Pulsed-FieldItalychemistryHemolytic-Uremic Syndromebiology.proteinCattleFrance
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Recombinant epidermolytic (exfoliative) toxin A of Staphylococcus aureus is not a superantigen

1992

The epidermolytic (exfoliative) toxins produced by Staphylococcus aureus cause epidermolysis and skin blistering. In addition, they have been implicated to belong to the group of T lymphocyte stimulating molecules known as "superantigens". Here we show that recombinant epidermolytic toxin A produced in S. aureus is not mitogenic for human and murine T lymphocytes. We discuss the possibility that minute contaminations of highly mitogenic exoproteins may cause the mitogenicity in several proteins that are reported to be superantigens.

Microbiology (medical)Staphylococcus aureusT-LymphocytesBlotting WesternImmunologyClostridium difficile toxin ABiologyLymphocyte Activationmedicine.disease_causeMonocytesMicrobiologylaw.inventionMicelawSuperantigenmedicineAnimalsHumansImmunology and AllergyCloning MolecularStaphylococcus aureus delta toxinCells CulturedAntigens BacterialMice Inbred BALB CToxinGeneral MedicineT lymphocyteRecombinant ProteinsExfoliatinsCytolysisStaphylococcus aureusRecombinant DNAInterleukin-2SpleenMedical Microbiology and Immunology
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Staphylococcus aureus α-Toxin’s Close Contacts Ensure the Kill

2018

The membrane pore-forming α-toxin is an important virulence factor of Staphylococcus aureus. Target cells can remove pores from their surface, but recent work shows that α-toxin may undermine this self-defense by clinging to epithelial cell junctions. The findings could lead to the development of novel remedies against S. aureus infections.

Microbiology (medical)Staphylococcus aureusVirulence FactorsBacterial ToxinsBiologymedicine.disease_causeMicrobiologyVirulence factorCell LineMicrobiologyAdherens junctionADAM10 ProteinHemolysin Proteins03 medical and health sciencesVirologymedicineAnimalsHumans030304 developmental biology0303 health sciencesPore-forming toxin030306 microbiologyMembrane ProteinsEpithelial CellsAdherens JunctionsStaphylococcal InfectionsEpitheliumInfectious Diseasesmedicine.anatomical_structureStaphylococcus aureusPinocytosisCarrier ProteinsTrends in Microbiology
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A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes

1993

Depending on the size of the pores one wishes to produce in plasma membranes, the choice will probably fall on one of the three toxins discussed above. S. aureus alpha-toxin should be tried first when pores of 1-1.5 nm diameter are required. This is generally the case when Ca2+ and nucleotide dependence of a given process is being studied. If alpha-toxin does not work, this is probably due to the fact that the toxin either does not produce pores, or that the pores are too small. In this case, high concentrations of alpha-toxin should be tried. If this still does not work, we recommend the use of HlyA. When very large pores are to be created, e.g. for introduction of antibodies into the cell…

Microbiology (medical)TetanolysinPore-forming toxinCell Membrane PermeabilityEscherichia coli ProteinsEscherichia coli ProteinsBacterial ToxinsCell MembraneImmunologyGeneral MedicineMembrane transportBiologyHemolysin Proteinschemistry.chemical_compoundMembraneBacterial ProteinschemistryBiochemistryStreptolysinsBiophysicsImmunology and AllergyCell permeabilityMedical Microbiology and Immunology
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Biosensing of microcystins in water samples; recent advances

2020

Safety and quality of water are significant matters for agriculture, animals and human health. Microcystins, as secondary metabolite of cyanobacteria (blue-green algae) and cyclic heptapeptide cyanotoxin, are one of the main marine toxins in continental aquatic ecosystems. More than 100 microcystins have been identified, of which MC-LR is the most important type due to its high toxicity and common detection in the environment. Climate change is an impressive factor with effects on cyanobacterial blooms as source of microcystins. The presence of this cyanotoxin in freshwater, drinking water, water reservoir supplies and food (vegetable, fish and shellfish) has created a common phenomenon in …

MicrocystinsBiomedical EngineeringBiophysicsBiosensing Techniques02 engineering and technologyMicrocystin01 natural sciencesFreshwater ecosystemHuman healthWater reservoirpolycyclic compoundsElectrochemistryAnimalsHumansEcosystemchemistry.chemical_classificationAquatic ecosystem010401 analytical chemistryReproducibility of ResultsWaterGeneral MedicineCyanotoxin021001 nanoscience & nanotechnology0104 chemical scienceschemistryEnvironmental chemistryEnvironmental science0210 nano-technologyEutrophicationMarine toxinBiotechnologyBiosensors and Bioelectronics
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Cyanobacteria and their metabolites in mono- and polidominant shallow eutrophic temperate lakes

2022

Monodominant (one species dominates) or polidominant (multiple species dominate) cyanobacterial blooms are pronounced in productive freshwater ecosystems and pose a potential threat to the biota due to the synthesis of toxins. Seasonal changes in cyanobacteria species and cyanometabolites composition were studied in two shallow temperate eutrophic lakes. Data on cyanobacteria biomass and diversity of dominant species in the lakes were combined with chemical and molecular analyses of fifteen potentially toxin-producing cyanobacteria species (248 isolates from the lakes). Anatoxin-a, saxitoxin, microcystins and other non-ribosomal peptides formed the diverse profiles in monodominant (Planktot…

MicrocystistoksiinitrehevöityminenHealth Toxicology and MutagenesisPublic Health Environmental and Occupational HealthAphanizomenon gracilemicrocystinssaxitoxinCyanobacteriavedenlaatuBiotajärvetLakespeptiditanatoxin-anon-ribosomal peptidesBiomassanatoksiini-asyanobakteeritmicrocystins; saxitoxin; anatoxin-a; non-ribosomal peptides; oligopeptides; <i>Aphanizomenon gracile</i>; <i>Microcystis</i>; <i>Planktothrix agardhii</i>oligopeptidesPlanktothrix agardhiiEcosystem
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Stimulation of hippocampal acetylcholine release by hyperforin, a constituent of St. John’s Wort

2004

Abstract Extracts of the medicinal plant St. John’s Wort ( Hypericum perforatum ) are widely used in the therapy of affective disorders and have been reported to exert antidepressant, anxiolytic, and cognitive effects in experimental and clinical studies. We here report that hyperforin, the major active constituent of the extract, increases the release of acetylcholine from rat hippocampus in vivo as determined by microdialysis. Hippocampal acetylcholine levels were increased by 50–100% following the systemic administration of pure hyperforin at doses of 1 and 10 mg/kg. The effect was almost completely suppressed by local perfusion with calcium-free buffer or with tetrodotoxin (1 μM). We co…

Microdialysismedicine.drug_classMicrodialysisTetrodotoxinPhloroglucinolPharmacologyHippocampusAnxiolyticRats Sprague-DawleyBridged Bicyclo Compoundschemistry.chemical_compoundmedicineAnimalsAnesthetics LocalNeurotransmitterPlant ExtractsTerpenesGeneral NeuroscienceHypericum perforatumAcetylcholineAnti-Bacterial AgentsRatsHyperforinchemistryAntidepressantCholinergicHypericumAcetylcholinemedicine.drugNeuroscience Letters
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Pharmacological activity of C10-substituted analogs of the high-affinity kainate receptor agonist dysiherbaine

2009

Kainate receptor antagonists have potential as therapeutic agents in a number of neuropathologies. Synthetic modification of the convulsant marine toxin neodysiherbaine A (NDH) previously yielded molecules with a diverse set of pharmacological actions on kainate receptors. Here we characterize three new synthetic analogs of NDH that contain substituents at the C10 position in the pyran ring of the marine toxin. The analogs exhibited high-affinity binding to the GluK1 (GluR5) subunit and lower affinity binding to GluK2 (GluR6) and GluK3 (GluR7) subunits in radioligand displacement assays with recombinant kainate and AMPA receptors. As well, the natural toxin NDH exhibited approximately 100-f…

Models MolecularAgonistKainic acidPatch-Clamp TechniquesTime FactorsStereochemistrymedicine.drug_classProtein subunitGreen Fluorescent ProteinsGlutamic AcidKainate receptorAMPA receptorMolecular Dynamics SimulationLigandsTransfectionTritiumBinding CompetitiveArticleMembrane PotentialsRadioligand AssayStructure-Activity RelationshipCellular and Molecular Neurosciencechemistry.chemical_compoundReceptors Kainic AcidExcitatory Amino Acid AgonistsmedicineRadioligandHumansReceptoralpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidCell Line TransformedPharmacologyAlanineKainic AcidDose-Response Relationship DrugMolecular StructureChemistryBridged Bicyclo Compounds HeterocyclicProtein SubunitsBiochemistryMutagenesis Site-DirectedMarine toxinNeuropharmacology
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