Search results for "toxins"

showing 10 items of 799 documents

Tools for Pathogen Proteomics: Fishing with Biomimetic Nanosponges

2017

The identification of the major virulence factors that drive pathogenicity is critical for gaining insight into the underlying molecular mechanisms of diseases. Although genetic approaches combined with functional analyses have markedly increased the rate of virulence factor discovery, the divergence between genome and proteome can impair the identification of important markers, in particular, of those that act in concert or depend on specific environmental factors. Recently, membrane-coated nanomaterials mimicking source cells of interest have emerged as powerful tools that can be used for improved tumor targeting and as "nanotraps" to capture chemokines and bacterial toxins. In this issue…

Proteomics0301 basic medicineProteomeVirulence FactorsBacterial ToxinsQuantitative proteomicsGeneral EngineeringGeneral Physics and AstronomyVirulenceComputational biologyBiologyProteomicsBioinformaticsGenomeVirulence factor03 medical and health sciences030104 developmental biologyBiomimeticsProteomeGeneral Materials ScienceIdentification (biology)PathogenACS Nano
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Metal stresses modify soluble proteomes and toxin profiles in two Mediterranean strains of the distributed dinoflagellate Alexandrium pacificum

2022

WOS:000789651000009; HABs involving Alexandrium pacificum have been reported in metal-contaminated ecosystems, suggesting that this distributed species adapts to and/or can tolerate the effects of metals. Modifications in soluble proteomes and PST contents were characterized in two Mediterranean A. pacificum strains exposed to mono- or polymetallic stresses (zinc, lead, copper, cadmium). These strains were isolated from two anthropized locations: Santa Giusta Lagoon (Italy, SG C10-3) and the Tarragona seaport (Spain, TAR C5-4F). In both strains, metals primarily downregulated key photosynthesis proteins. Metals also upregulated other proteins involved in photosynthesis (PCP in both strains)…

ProteomicsEnvironmental EngineeringProteomeParalytic shellfish toxins[SDE.MCG]Environmental Sciences/Global Changeschemistry.chemical_elementmedicine.disease_causePhotosynthesiscomplex mixturesMicrobiologychemistry.chemical_compoundTar (tobacco residue)BiosynthesismedicineEnvironmental ChemistryWaste Management and DisposalEcosystemCadmiumbiologyStrain (chemistry)Harmful algal bloomToxinChemistryDinoflagellatebiology.organism_classificationPollutionADKMetalsDinoflagellida[SDE.BE]Environmental Sciences/Biodiversity and Ecology
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Proteomics evaluation of enniatins acute toxicity in rat liver

2021

Abstract Enniatins (ENs) are emerging mycotoxins produced by Fusarium fungi which are cytotoxic also at low concentrations due to its ionophoric properties. The aim of this study was to evaluate the hepatic toxicity of ENs exposure at different concentrations in Wistar rats through a proteomic approach. Animals were intoxicated by oral gavage with medium (EN A 256, ENA1 353, ENB 540, ENB1 296 μg/mL) and high concentrations (ENA 513, ENA1 706, ENB 1021, ENB1 593 μg/mL) of an ENs mixture and sacrificed after 8 h. Protein extraction was performed using powdered liver. Peptides were analyzed using a liquid chromatography coupled with a quadrupole time-of-flight mass spectrometer. Proteins were …

ProteomicsFusariumToxicologyProteomicsmedicine.disease_cause03 medical and health sciences0404 agricultural biotechnologyTandem Mass SpectrometryIn vivoDepsipeptidesIn vivoProtein purificationmedicineAnimalsRats Wistar030304 developmental biology0303 health sciencesbiologyChemistry04 agricultural and veterinary sciencesGeneral MedicineMetabolismMycotoxinsbiology.organism_classification040401 food scienceAcute toxicityRatsLiverBiochemistryOxidative stressElectron transport chainFemaleNAD+ kinaseBiomarkersOxidative stressChromatography LiquidFood ScienceFood and Chemical Toxicology
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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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Proteome analysis of the fungus Aspergillus carbonarius under ochratoxin A producing conditions

2011

Aspergillus carbonarius is an important ochratoxin A producing fungus that is responsible for mycotoxin contamination of grapes and wine. In this study, the proteomes of highly (W04-40) and weakly (W04-46) OTA-producing A. carbonarius strains were compared to identify proteins that may be involved in OTA biosynthesis. Protein samples were extracted from two biological replicates and subjected to two dimensional gel electrophoresis analysis and mass spectrometry. Expression profile comparison (PDQuest software), revealed 21 differential spots that were statistically significant and showed a two-fold change in expression, or greater. Among these, nine protein spots were identified by MALDI-MS…

ProteomicsOchratoxin AProteomeFungusPolymerase Chain ReactionMicrobiologyMicrobiologyFungal Proteinschemistry.chemical_compoundBiosynthesisGene expressionRNA MessengerMycotoxinchemistry.chemical_classificationTwo-dimensional gel electrophoresisbiologyGeneral Medicinebiology.organism_classificationOchratoxinsAmino acidAspergillusBiochemistrychemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomeFood MicrobiologyFood ScienceInternational Journal of Food Microbiology
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Rho protein inactivation induced apoptosis of cultured human endothelial cells.

2002

Small GTP-binding Rho GTPases regulate important signaling pathways in endothelial cells, but little is known about their role in endothelial cell apoptosis. Clostridial cytotoxins specifically inactivate GTPases by glucosylation [ Clostridium difficile toxin B-10463 (TcdB-10463), C. difficile toxin B-1470 (TcdB-1470)] or ADP ribosylation ( C. botulinum C3 toxin). Exposure of human umbilical cord vein endothelial cells (HUVEC) to TcdB-10463, which inhibits RhoA/Rac1/Cdc42, or to C3 toxin, which inhibits RhoA, -B, -C, resulted in apoptosis, whereas inactivation of Rac1/Cdc42 with TcdB-1470 was without effect, suggesting that Rho inhibition was responsible for endothelial apoptosis. Disruptio…

Pulmonary and Respiratory Medicinerac1 GTP-Binding Proteinrho GTP-Binding ProteinsProgrammed cell deathUmbilical VeinsEndotheliumPhysiologyBacterial ToxinsCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisBcl-2-associated X proteinBacterial ProteinsPhysiology (medical)Proto-Oncogene ProteinsmedicineCyclic AMPIn Situ Nick-End LabelingHumanscdc42 GTP-Binding ProteinCells Culturedbcl-2-Associated X ProteinAdenosine Diphosphate RibosebiologyCaspase 3Intracellular Signaling Peptides and ProteinsCell BiologyCaspase 9Cell biologyNeoplasm ProteinsEndothelial stem cellmedicine.anatomical_structureCdc42 GTP-Binding ProteinProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisCaspasesbiology.proteinMyeloid Cell Leukemia Sequence 1 ProteinEndothelium VascularSignal transductionCarrier ProteinsrhoA GTP-Binding ProteinBH3 Interacting Domain Death Agonist ProteinSignal TransductionAmerican journal of physiology. Lung cellular and molecular physiology
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Cercospora beticola toxins. Part XVII. The role of the beticolin/Mg2+ complexes in their biological activity Study of plasma membrane H+-ATPase, vacu…

1996

Beticolin-1 and beticolin-2, yellow toxins produced by the phytopathogenic fungus Cercospora beticola, inhibit the plasma membrane H(+)-ATPase. Firstly, since beticolins are able to form complexes with Mg2+, the role of the beticolin/Mg2+ complexes in the inhibition of the plasma membrane proton pump has been investigated. Calculations indicate that beticolins could exist under several forms, in the H(+)-ATPase assay mixture, both free or complexed with Mg2+. However, the percentage inhibition of the H(+)-ATPase activity is correlated to the concentration of one single form of beticolin, the dimeric neutral complex Mg2H2B2, which appears to be the active form involved in the H(+)-ATPase inh…

Pyrophosphatase H+-StereochemistryATPaseAcid PhosphatasePhosphataseBiophysicsBiological Transport ActiveHeterocyclic Compounds 4 or More RingsZea maysBiochemistryMagnesium ion complexH+- PyrophosphataseMagnesiumEnzyme InhibitorsPyrophosphatasesInhibitionchemistry.chemical_classificationATPase H+-biologyChemistryVacuolar hCell MembraneSubstrate (chemistry)Biological activityCell BiologyMycotoxinsAlkaline PhosphataseCercospora beticolabiology.organism_classificationInorganic PyrophosphataseProton-Translocating ATPasesBeticolinMembraneEnzymeBiochemistryVacuolesbiology.proteinH+- ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes
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Pdl1 Is a Putative Lipase that Enhances Photorhabdus Toxin Complex Secretion

2012

The Toxin Complex (TC) is a large multi-subunit toxin first characterized in the insect pathogens Photorhabdus and Xenorhabdus, but now seen in a range of pathogens, including those of humans. These complexes comprise three protein subunits, A, B and C which in the Xenorhabdus toxin are found in a 4∶1∶1 stoichiometry. Some TCs have been demonstrated to exhibit oral toxicity to insects and have the potential to be developed as a pest control technology. The lack of recognisable signal sequences in the three large component proteins hinders an understanding of their mode of secretion. Nevertheless, we have shown the Photorhabdus luminescens (Pl) Tcd complex has been shown to associate with th…

QH301-705.5Protein subunitImmunologyBacterial ToxinsMicrobiologiaXenorhabdusPathogenesisBiologymedicine.disease_causeMicrobiologyVirulence factorXenorhabdusMicrobiology03 medical and health sciencesBacterial ProteinsVirologyPhotorhabdus luminescensManducaGeneticsmedicineEscherichia coliGram NegativeAnimalsSecretionBiology (General)Molecular BiologyEscherichia coliBiologyMicrobial PathogensBacterial Secretion Systems030304 developmental biology0303 health sciences030306 microbiologyToxinMembrane ProteinsLipaseRC581-607biology.organism_classificationBacterial PathogensHost-Pathogen InteractionLarvaBacteris patògensParasitologyImmunologic diseases. AllergyPhotorhabdusProteïnesPhotorhabdusResearch ArticlePLoS Pathogens
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Analysis of mycotoxins in barley using ultra high liquid chromatography high resolution mass spectrometry: comparison of efficiency and efficacy of d…

2012

The effectiveness of four extraction methods (modified QuEChERS, matrix solid-phase dispersion (MSPD), solid-liquid extraction (SLE) and solid-phase extraction (SPE) clean-up) were evaluated for simultaneous determination of 32 mycotoxins produced by the genus Fusarium, Claviceps, Aspergillus, Penicillium and Alternaria in barley by ultra high pressure liquid chromatography coupled to ultra-high resolution mass spectrometry (UHPLC-Orbitrap(®) MS). The efficiency and efficacy of extraction methods were evaluated and compared in number of extracted mycotoxins and obtained recoveries. From the one point of view, QuEChERS procedure was fast and easy, as well as it was able to successfully extra…

QuEChERSTime FactorsFood ContaminationChemical FractionationMass spectrometryOrbitrapQuechersMass SpectrometryAnalytical Chemistrylaw.inventionMatrix (chemical analysis)chemistry.chemical_compoundlawMSPDSolid phase extractionMycotoxinChromatography High Pressure LiquidChromatographybiologyChemistryExtraction (chemistry)Reproducibility of ResultsHordeumSolid-liquid extractionClean-upMycotoxinsbiology.organism_classificationOrbitrapPenicilliumTalanta
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Absence Ochratoxin A in soy sauce

2004

A method is described for the determination of ochratoxin A (OTA) in soy sauce using phosphate-buffered saline (PBS) extraction, an immunoaffinity clean-up, a liquid chromatographic determination with fluorescence detection (LC-FD) and confirmation with LC-FD after methylation of OTA. Recoveries of OTA spiked to soy sauce samples at 0.25 ng/ml level were 90% with relative standard deviations of 4%. The limit of detection was 0.01 ng/ml for OTA using the proposed method. Furthermore, the proposed method was applied to 60 soy sauce samples from China and Japan and none of them were found to contain OTA.

Quality ControlOchratoxin ADetection limitChromatographyImmunochemistryExtraction (chemistry)Soy FoodsFood ContaminationGeneral MedicineOchratoxinsSensitivity and SpecificityMicrobiologyFluorescencechemistry.chemical_compoundchemistryFood scienceChromatography LiquidFood ScienceInternational Journal of Food Microbiology
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