Search results for "toxins"

showing 10 items of 799 documents

Staphylococcal food poisoning case and molecular analysis of toxin genes in Staphylococcus aureus strains isolated from food in Sicily, Italy.

2014

A case of staphylococcal food poisoning was observed in two individuals of the same family after consumption of primosale, a semiripened sheep cheese produced in Sicily. Staphylococcus aureus isolated from the cheese produced enterotoxin C (SEC) and carried both the enterotoxin C (sec) and the toxic shock syndrome toxin (tsst-1) gene. Following this case, an extensive survey was conducted on 971 food samples (raw milk, cheese, meat, and food preparations). S. aureus was detected in 102 of 971 food samples, from all types of food with the exception of ricotta cheese. The tsst-1 gene was present in 42% of the strains, either alone or in combination with other toxin genes. The enterotoxin C ge…

DNA BacterialStaphylococcus aureusMeatBacterial ToxinsEnterotoxinBiologySettore BIO/19 - Microbiologia Generalemedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyPolymerase Chain ReactionMicrobiologyEnterotoxinsmedicineAnimalsFood scienceGeneSicilyfood safety.SuperantigensToxinToxic shock syndrome toxinRaw milktoxin geneMolecular analysisStaphylococcal Food PoisoningStaphylococcus aureusConsumer Product Safetytypical dairy productStaphylococcus aureuFood Microbiologyfood poisoningAnimal Science and ZoologyDairy ProductsStaphylococcal Food PoisoningFood ScienceFoodborne pathogens and disease
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Identification and typing of food-borne Staphylococcus aureus by PCR-based techniques.

2005

Abstract The possibility of using PCR for rapid identification of food-borne Staphylococcus aureus isolates was evaluated as an alternative to the API-Staph system. A total of 158 strains, 15 S. aureus , 12 other staphylococcal species, and 131 isolates recovered from 164 food samples were studied. They were phenotypically characterized by API-Staph profiles and tested for PCR amplification with specific primers directed to thermonuclease ( nuc ) and enterotoxin ( sea to see ) genes. Disagreement between the PCR results and API-Staph identification was further assessed by the analysis of randomly amplified polymorphic DNA (RAPD) profiles obtained with three universal primers (M13, T3, and T…

DNA BacterialStaphylococcus aureusMicrococcaceaeEnterotoxinBiologymedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyDNA RibosomalPolymerase Chain Reactionlaw.inventionMicrobiologyEnterotoxinsfluids and secretionsBacterial ProteinslawRNA Ribosomal 16SGenotypemedicineCluster AnalysisMicrococcal NucleaseTypingEcology Evolution Behavior and SystematicsPolymerase chain reactionGenes rRNASequence Analysis DNAbiology.organism_classification16S ribosomal RNAEndonucleasesMolecular biologyDNA FingerprintingRAPDBacterial Typing TechniquesRandom Amplified Polymorphic DNA TechniqueStaphylococcus aureusFood MicrobiologyNucleic Acid Amplification TechniquesSystematic and applied microbiology
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Concomitant loss of conformation and superantigenic activity of staphylococcal enterotoxin B deletion mutant proteins.

1993

The T-cell-stimulating activity of staphylococcal enterotoxin B (SEB) is an important factor in the pathogenesis of certain staphylococcal diseases. To investigate the immunologically active domains of the SEB molecule, we have produced truncated fragments of recombinant SEB by C-terminal and N-terminal deletions. The fragments were expressed as fusion proteins with protein A, including a cleavage site to remove the protein A part. Mutant proteins were tested for the ability to stimulate human resting T cells and SEB-reactive T-cell clones. Deletion of only 9 amino acids from the C terminus leads to complete loss of T-cell-stimulating activity. Removing further amino acids from the SEB mole…

DNA BacterialStaphylococcus aureusRecombinant Fusion ProteinsImmunologyMutantMolecular Sequence DataBiologyMicrobiologyEpitopeEnterotoxinsMiceStructure-Activity RelationshipMutant proteinAnimalsAmino Acid SequencePeptide sequencechemistry.chemical_classificationAntigens BacterialMice Inbred BALB CBase SequenceC-terminusFusion proteinMolecular biologyAmino acidInfectious DiseaseschemistryMutationParasitologyGene DeletionConformational epitopeResearch Article
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Transcription analysis of the genes tcdA-E of the pathogenicity locus of Clostridium difficile.

1997

To analyse the transcription pattern of the five tcdA-E genes of the pathogenicity locus (PaLoc) of Clostridium difficile a protocol was established to purify RNA from strain VPI10463. Transcription analysis of the five tcdA-E genes showed that they were all transcribed. In the early exponential phase, a high level of tcdC and low levels of tcdA,B,D,E transcripts were detectable; this was inverted in the stationary phase, suggesting that TcdC might have a negative influence on transcription of the other genes. Three transcription initiation sites, one for tcdA and two for tcdB were determined by primer extension analysis. Readthrough transcripts from outside the locus were not obtainable, s…

DNA BacterialTranscription GeneticBacterial ToxinsMolecular Sequence DataLocus (genetics)Helix-turn-helixBiologymedicine.disease_causeBiochemistryPolymerase Chain ReactionPrimer extensionchemistry.chemical_compoundEnterotoxinsBacterial ProteinsTranscription (biology)medicineAmino Acid SequencePromoter Regions GeneticGeneDNA PrimersRegulation of gene expressionGeneticsBase SequenceSequence Homology Amino AcidVirulenceClostridioides difficileClostridium perfringensMolecular biologyDNA-Binding ProteinsRepressor ProteinschemistryGenes BacterialDNAEuropean journal of biochemistry
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Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransf…

1990

A detailed analysis of the 8130-bp open reading frame (ORF) of gene toxA and of an upstream ORF designated utxA, indicates the presence of a transcription terminator stem-loop for toxA, promoter sequences, and Shine-Dalgarno boxes for toxA and utxA. No transcription terminator between toxA and utxA is suggested by the sequence. ToxA contains two domains, one-third (C-terminal) with a repetitive structure and the residual two-thirds with no repetitions. The 2499-bp sequence encoding the repetitive structure is composed of nine groups of different short repetitive oligodeoxyribonucleotides (SRONs). A combination of these SRONs codes for five groups of combined repetitive oligopeptides (CROPs)…

DNA BacterialTranscription GeneticSequence analysisBacterial ToxinsMolecular Sequence DataRestriction MappingBiologyHomology (biology)Conserved sequenceEnterotoxinsOpen Reading FramesSequence Homology Nucleic AcidGeneticsAmino Acid SequencePeptide sequenceGeneRepetitive Sequences Nucleic AcidGeneticsBase SequenceNucleic acid sequenceStreptococcusGeneral MedicineMolecular biologyOpen reading frameTerminator (genetics)Genes BacterialGlucosyltransferasesGene
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Cloning and expression of a cDNA copy of the viral K28 killer toxin gene in yeast

1995

The killer toxin K28, secreted by certain killer strains of the yeast Saccharomyces cerevisiae is genetically encoded by a 1.9 kb double-stranded RNA, M-dsRNA (M28), that is present within the cell as a cytoplasmically inherited virus-like particle (VLP). For stable maintenance and replication, M28-VLPs depend on a second dsRNA virus (LA), which has been shown to encode the major capsid protein (cap) and a capsid-polymerase fusion protein (cap-pol) that provides the toxin-coding M-satellites with their transcription and replicase functions. K28 toxin-coding M28-VLPs were isolated, purified and used in vitro for the synthesis of the single-stranded M28 transcript, which was shown to be of pl…

DNA ComplementarySaccharomyces cerevisiae ProteinsTranscription GeneticMolecular Sequence DataGene ExpressionRNA-dependent RNA polymeraseSaccharomyces cerevisiaeBiologyOpen Reading FramesTranscription (biology)Complementary DNAGene expressionGeneticsAmino Acid SequenceCloning MolecularProtein PrecursorsMolecular BiologyGeneRNA Double-StrandedBase SequenceSequence Analysis RNANucleic acid sequenceRNARNA FungalDNA-Directed RNA PolymerasesSequence Analysis DNAMycotoxinsMolecular biologyKiller Factors YeastOpen reading frameProtein BiosynthesisNucleic Acid ConformationRNA ViralMolecular and General Genetics MGG
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Cytotoxic Activity of Organotin(IV) Derivatives with Triazolopyrimidine Containing Exocyclic Oxygen Atoms

2020

In this study cytotoxicity of organotin(IV) compounds with 1,2,4-triazolo[1,5-a]pyrimidines, Me3Sn(5tpO) (1), n-Bu3Sn(5tpO) (2), Me3Sn(mtpO) (3), n-Bu3Sn(mtpO) (4), n-Bu3Sn(HtpO2) (5), Ph3Sn(HtpO2) (6) where 5HtpO = 4,5-dihydro-5-oxo-[1,2,4]triazolo-[1,5-a]pyrimidine, HmtpO = 4,7-dihydro-5-methyl-7-oxo-[1,2,4]triazolo-[1,5-a]pyrimidine, and H2tpO2 = 4,5,6,7-tetrahydro-5,7- dioxo-[1,2,4]triazolo-[1,5-a]-pyrimidine, was assessed on three different human tumor cell lines: HCT-116 (colorectal carcinoma), HepG2 (hepatocarcinoma) and MCF-7 (breast cancer). While 1 and 3 were inactive, compounds 2, 4, 5 and 6 inhibited the growth of the three tumor cell lines with IC50 values in the submicromolar …

DenticityCellPharmaceutical Science01 natural sciencesAnalytical Chemistrychemistry.chemical_compoundDrug DiscoveryOrganotin CompoundstriazolopyrimidineCytotoxicityMembrane Potential MitochondrialCytotoxinsapoptosisBiological activityHep G2 CellsG2 Phase Cell Cycle CheckpointsGene Expression Regulation Neoplasticmedicine.anatomical_structureChemistry (miscellaneous)Mitochondrial MembranesMCF-7 CellsMolecular MedicineCyclin-Dependent Kinase Inhibitor p21crystal structurein vitro anticancer activityPyrimidineCell SurvivalStereochemistryorganotin(iv)010402 general chemistryArticlelcsh:QD241-441Inhibitory Concentration 50Structure-Activity Relationshiplcsh:Organic chemistrymedicineHumansPhysical and Theoretical ChemistryMetallodrug010405 organic chemistryLigandOrganic ChemistryTriazolesHCT116 CellsapoptosiG1 Phase Cell Cycle Checkpoints0104 chemical sciencesPyrimidineschemistrymetallodrugsCell cultureApoptosisDrug DesignTumor Suppressor Protein p53Reactive Oxygen SpeciesMolecules
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DNA binding, nuclease activity, DNA photocleavage and cytotoxic properties of Cu(II) complexes of N-substituted sulfonamides.

2013

Abstract Ternary copper(II) complexes [Cu(NST)2(phen)] (1) and [Cu(NST)2(NH3)2]·H2O (2) [HNST = N-(4,5-dimethylthiazol-2-yl)naphthalene-1-sulfonamide] were prepared and characterized by physico-chemical techniques. Both 1 and 2 were structurally characterized by X-ray crystallography. The crystal structures show the presence of a distorted square planar CuN4 geometry in which the deprotonated sulfonamide, acting as monodentate ligand, binds to the metal ion through the thiazole N atom. Both complexes present intermolecular π–π stacking interactions between phenanthroline rings (compound 1) and between naphthalene rings (compound 2). The interaction of the complexes with CT DNA was studied b…

DenticityStereochemistryCell SurvivalUltraviolet RaysPhenanthrolineRadicalStackingAscorbic AcidNaphthalenesBiochemistryFluorescence spectroscopyInorganic Chemistrychemistry.chemical_compoundInhibitory Concentration 50Coordination ComplexesCell Line TumorAnimalsHumansDNA CleavageThiazoleNucleaseSulfonamidesBinding SitesbiologyCytotoxinsHydroxyl RadicalDNAHydrogen PeroxidePhotochemical ProcessesKineticschemistrybiology.proteinCattleDNACopperPhenanthrolinesJournal of inorganic biochemistry
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Optimization of Matrix Solid-Phase Dispersion method for simultaneous extraction of aflatoxins and OTA in cereals and its application to commercial s…

2010

Abstract A method based on Matrix Solid-Phase Dispersion (MSPD) has been developed for the determination of 5 mycotoxins (ochratoxin A and aflatoxins B and G) in different cereals. Several dispersants, eluents and ratios were tested during the optimization of the process in order to obtain the best results. Finally, samples were blended with C 18 and the mycotoxins were extracted with acetonitrile. Regarding to matrix effects, the results clearly demonstrated the necessity to use a matrix-matched calibration to validate the method. Analyses were performed by liquid chromatography–triple quadrupole-tandem mass spectrometry (LC–QqQ-MS/MS). The recoveries of the extraction process ranged from …

Detection limitOchratoxin AAflatoxinCereals analysisMatrix Solid-Phase DispersionChromatographyChemistryExtraction (chemistry)Ochratoxin ACoffeeOchratoxinsMass SpectrometryAnalytical ChemistryMatrix (chemical analysis)chemistry.chemical_compoundAflatoxinsLimit of Detectionmedia_common.cataloged_instanceSample preparationEuropean unionEdible GrainMycotoxinChromatography Liquidmedia_commonTalanta
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Extraction and analysis of ochratoxin A in bread using pressurised liquid extraction and liquid chromatography.

2005

A pressurised liquid extraction (PLE) method for the analysis of ochratoxin A (OTA) in bread samples is given. Parameters such as solvent, temperature, pressure and time were investigated thoroughly. The optimized PLE conditions were: methanol as extraction solvent, 80 degrees C, 2000 psi and a 5-min cycle. OTA was determined by liquid chromatography coupled with fluorescence detection and confirmed by methyl ester derivatization. Under these conditions OTA recovery is 92.3% with a RSD of 5%. Limits of detection and quantification were 0.02 and 0.06 microg/kg, respectively. The proposed method was applied to 20 bread samples, finding two positive samples with OTA levels below the maximum pe…

Detection limitOchratoxin AChromatographyChemistryOrganic ChemistryExtraction (chemistry)TemperatureGeneral MedicineBreadBiochemistryHigh-performance liquid chromatographyOchratoxinsAnalytical Chemistrychemistry.chemical_compoundSpectrometry FluorescencePressureSolventsmedia_common.cataloged_instanceSample preparationEuropean unionDerivatizationOchratoxinmedia_commonChromatography LiquidJournal of chromatography. A
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