Search results for "toxins"

showing 10 items of 799 documents

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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Heat shock protein-antigen fusions lose their enhanced immunostimulatory capacity after endotoxin depletion.

2008

Heat shock proteins (HSPs) induce cross-presentation of antigens by dendritic cells (DC) as well as DC maturation. These properties make HSP antigen complexes good candidates to prime CD8 T cell responses against tumor-associated antigens. In this study, we analyzed four different members of the HSP70 family fused to a fragment of ovalbumin (OVA) as a model tumor antigen. E. coli-derived recombinant HSP70-OVA fusion proteins efficiently primed antigen-specific cytotoxic T cells in short-term in vivo immunization assays. Because of concerns that the adjuvant effect of HSPs may be due to endotoxin contamination, we studied this issue in detail. Induction of OVA-specific cytotoxicity was signi…

Cytotoxicity ImmunologicCpG OligodeoxynucleotideOvalbuminRecombinant Fusion ProteinsImmunologyReceptors Antigen T-CellMice TransgenicBiologyCD8-Positive T-LymphocytesLymphocyte ActivationMiceImmune systemCross-PrimingAntigenAdjuvants ImmunologicHeat shock proteinNeoplasmsCytotoxic T cellAnimalsHSP70 Heat-Shock ProteinsAntigensMolecular BiologyTLR9Dendritic CellsMolecular biologyFusion proteinTumor antigenEndotoxinsMice Inbred C57BLOligodeoxyribonucleotidesT-Lymphocytes CytotoxicMolecular immunology
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Transcription of genes in the biosynthetic pathway for fumonisin mycotoxins is epigenetically and differentially regulated in the fungal maize pathog…

2012

ABSTRACT When the fungal pathogen Gibberella moniliformis (anamorph, Fusarium verticillioides ) colonizes maize and maize-based products, it produces class B fumonisin (FB) mycotoxins, which are a significant threat to human and animal health. FB biosynthetic enzymes and accessory proteins are encoded by a set of clustered and cotranscribed genes collectively named FUM, whose molecular regulation is beginning to be unraveled by researchers. FB accumulation correlates with the amount of transcripts from the key FUM genes, FUM1 , FUM21 , and FUM8 . In fungi in general, gene expression is often partially controlled at the chromatin level in secondary metabolism; when this is the case, the deac…

DISRUPTIONTranscription GeneticFUM21[SDV]Life Sciences [q-bio]DIVERSITYPROTEINFusarium verticillioidesmaizeSECONDARY METABOLISMgene clusterEpigenesis GeneticHistonesFUM8FusariumGene Expression Regulation FungalASPERGILLUSPromoter Regions Genetic2. Zero hungerGenetics0303 health sciencesHistone deacetylase inhibitorhistone acetylationAcetylationArticlesGeneral MedicineChromatinChromatinGENOMEHistoneMultigene Family[SDE]Environmental SciencesTrichostatin AEpigenetics; Fusarium verticillioides; fmonisin synthesismedicine.drugCONIDIATIONChromatin Immunoprecipitationmedicine.drug_classGenes FungalChIPBiologyGFPZea maysMicrobiologyFumonisinsChromatin remodeling03 medical and health sciencesmedicineEpigeneticsMolecular Biology030304 developmental biologyepigenetics030306 microbiologyCLUSTERFumonisins; epigenetics; Fusarium verticillioides; maize; histone acetylation; histone deacetylases; ChIP; Trichostatin A; FUM1; FUM21; FUM8; GFP; gene clusterMycotoxinsChromatin Assembly and DisassemblyFUM1Histone Deacetylase InhibitorsTrichostatin AAcetylationbiology.proteinChromatin immunoprecipitationhistone deacetylases
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The bacterial cytolethal distending toxin (CDT) triggers a G2 cell cycle checkpoint in mammalian cells without preliminary induction of DNA strand br…

1999

The bacterial cytolethal distending toxin (CDT) was previously shown to arrest the tumor-derived HeLa cell line in the G2-phase of the cell cycle through inactivation of CDK1, a cyclin-dependent kinase whose state of activation determines entry into mitosis. We have analysed the effects induced in HeLa cells by CDT, in comparison to those induced by etoposide, a prototype anti-tumoral agent that triggers a G2 cell cycle checkpoint by inducing DNA damage. Both CDT and etoposide inhibit cell proliferation and induces the formation of enlarged mononucleated cells blocked in G2. In both cases, CDK1 from arrested cells could be re-activated both in vitro by dephosphorylation by recombinant Cdc25…

DNA ReplicationG2 PhaseCancer ResearchCAFFEINECell cycle checkpointCytolethal distending toxinDNA damageRecombinant Fusion Proteins[SDV]Life Sciences [q-bio]Bacterial ToxinsBiologyS Phase03 medical and health sciencesCDC2 Protein KinaseGeneticsHumanscdc25 PhosphatasesCHEK1PhosphorylationMolecular BiologyMitosisEtoposide030304 developmental biology0303 health sciences030306 microbiologyCell growthDNA NeoplasmG2-M DNA damage checkpointCell cycleAntineoplastic Agents PhytogenicNeoplasm Proteins3. Good healthCell biology[SDV] Life Sciences [q-bio]BiochemistryAGENT ANTITUMEURProtein Processing Post-TranslationalCell DivisionDNA DamageHeLa Cells
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Domain organization and evolution of multifunctional autoprocessing repeats-in-toxin (MARTX) toxin in Vibrio vulnificus.

2011

ABSTRACT The objective of this study was to analyze multifunctional autoprocessing repeats-in-toxin (MARTX) toxin domain organization within the aquatic species Vibrio vulnificus as well as to study the evolution of the rtxA1 gene. The species is subdivided into three biotypes that differ in host range and geographical distribution. We have found three different types (I, II, and III) of V. vulnificus MARTX (MARTX Vv ) toxins with common domains (an autocatalytic cysteine protease domain [CPD], an α / β-hydrolase domain, and a domain resembling that of the LifA protein of Escherichia coli O127:H6 E2348/69 [Efa/LifA]) and specific domains (a Rho-GTPase inactivation domain [RID], a domain of …

DNA BacterialGene Transfer HorizontalBacterial ToxinsMolecular Sequence DataVibrio vulnificusmedicine.disease_causeApplied Microbiology and BiotechnologyBacterisMicrobiologyEvolution MolecularVibrionaceaemedicineEvolutionary and Genomic MicrobiologyVibrio vulnificusGeneEscherichia coliGenètica bacterianaGeographyEcologybiologyToxinSequence Analysis DNAbiology.organism_classificationCysteine proteaseBacterial Typing TechniquesProtein Structure TertiaryHorizontal gene transferBacteris patògensBacteriaFood ScienceBiotechnology
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Identification of a clone of Escherichia coli O103:H2 as a potential agent of hemolytic-uremic syndrome in France

1993

In a French multicenter study, six verocytotoxin-producing Escherichia coli strains were isolated from the stools of 6 of 69 children suffering from hemolytic-uremic syndrome. All strains belonged to serotype O103:H2, a serotype commonly associated with diarrhea in weaned rabbits in France. To determine whether the strains from humans and rabbits were genetically related, they were compared by analyzing their esterase electropherotypes and the restriction fragment length polymorphisms of the ribosomal DNA regions. A common clonal origin of these pathogenic strains was suggested by their identical esterase electropherotypes and their identical ribotypes, in addition to their identical seroty…

DNA BacterialMicrobiology (medical)SerotypeBacterial ToxinsMolecular Sequence DataClone (cell biology)VirulenceVerocytotoxinShiga Toxin 1medicine.disease_causePolymerase Chain Reactionlaw.inventionMicrobiology03 medical and health scienceschemistry.chemical_compoundlawEscherichia colimedicineHumansSerotyping[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyEscherichia coliEscherichia coli InfectionsComputingMilieux_MISCELLANEOUSPolymerase chain reaction030304 developmental biology0303 health sciencesBase SequenceVirulencebiology030306 microbiologyInfantCorrectionbiology.organism_classificationEnterobacteriaceae3. Good healthBacterial adhesinPOUVOIR PATHOGENE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologychemistryChild PreschoolHemolytic-Uremic SyndromeFranceResearch ArticleJournal of Clinical Microbiology
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Comparative sequence analysis of the Clostridium difficile toxins A and B.

1992

The six clones pTB112, pTB324, pTBs12, pCd122, pCd14 and pCd13 cover the tox locus of Clostridium difficile VPI 10463. This region of 19 kb of chromosomal DNA contains four open reading frames including the complete toxB and toxA genes. The two toxins show 63% amino acid (aa) homology, a relatedness that had been predicted by the cross-reactivity of some monoclonal antibodies (mAb) but that is in contrast to the toxin specificity of polyclonal antisera. A special feature of ToxA and ToxB is their repetitive C-termini. We define herein 19 individual CROPs (combined repetitive oligopeptides of 20-50 aa length) in the ToxB C-terminus, which are separable into five homologous groups. Comparison…

DNA BacterialSequence analysisBacterial ToxinsBlotting WesternMolecular Sequence DataRestriction MappingDNA RecombinantLocus (genetics)Cross ReactionsHomology (biology)EnterotoxinsBacterial ProteinsSequence Homology Nucleic AcidGene duplicationGeneticsAmino Acid SequenceMolecular BiologyGeneRepetitive Sequences Nucleic AcidGeneticsbiologyBase SequenceClostridioides difficileNucleic acid sequenceAntibodies MonoclonalNucleic Acid HybridizationMolecular biologyRecombinant ProteinsOpen reading framePolyclonal antibodiesbiology.proteinMoleculargeneral genetics : MGG
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Definition of the single integration site of the pathogenicity locus in Clostridium difficile.

1996

We determined the nucleotide sequence 3.8 kb upstream and 5.2 kb downstream of the toxin genes A and B of Clostridium difficile. Nine ORFs were discovered. Based on PCR-directed approaches, two were attributed to the pathogenicity locus (PaLoc). The other seven were found in every C. difficile isolate obtained from the human gastrointestinal tract, respectless of their toxinogenicity. The ORFs cdu1 and cdu2/2' upstream of the PaLoc displayed similarity to repressors of Gram-positive bacteria (cdu1), and to an Na+/H+ antiporter described for Enterococcus hirae (cdu2/2'). Downstream of the locus a putative ABC transporter (cdd2-4) was identified. With a set of three paired primers used in pol…

DNA BacterialSequence analysisBacterial ToxinsMolecular Sequence DataVirulenceLocus (genetics)BiologyEnterotoxinsOpen Reading FramesBacterial ProteinsSpecies SpecificityGeneticsHumansAmino Acid SequenceORFSGeneGeneticsBase SequenceSequence Homology Amino AcidVirulenceClostridioides difficileNucleic acid sequenceGeneral MedicineMolecular biologyIntestinesTerminator (genetics)DNA Transposable ElementsATP-Binding Cassette TransportersMobile genetic elementsGene
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Development of a real-time PCR assay for detection and quantification of enterotoxigenic members of Bacillus cereus group in food samples

2009

A highly sensitive real-time PCR (qPCR) procedure, targeting the phosphatidylcholine-specific phospholipase C gene (pc-plc), was developed for specific detection and quantification of strains belonging to Bacillus cereus group. The target region was selected based on the enterotoxigenic profiles of 75 Bacillus strains. The inclusivity and exclusivity of the RTi-PCR assay were assessed with 59 isolates of the B. cereus group, 16 other Bacillus spp., and 4 non-Bacillus strains. The assay was also used to construct calibration curves for different food matrices, and it had a wide quantification range of 6 log units using both serial dilutions of purified DNA and calibrated cell suspensions of …

DNA BacterialSerial dilutionEggsMolecular Sequence DataColony Count MicrobialBacillus cereusFood ContaminationPolymerase Chain ReactionSensitivity and SpecificityMicrobiologyMicrobiologyEnterotoxinsBacillus cereusSpecies SpecificityHumansFood microbiologyDetection limitBacillus (shape)ChromatographybiologyfungiInfant NewbornInfantReproducibility of ResultsSequence Analysis DNAGeneral Medicinebiology.organism_classificationBacillalesInfant FormulaCereusCalibrationFood MicrobiologyFood ScienceFood contaminantInternational Journal of Food Microbiology
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