Search results for "Bacterial toxins"

showing 10 items of 192 documents

Morphological changes in adherent cells induced by Clostridium difficile toxins.

1991

Mice Inbred BALB CClostridioides difficileCytotoxinsMacrophagesBacterial ToxinsClostridium difficileBiologyIn Vitro TechniquesBiochemistryMicrobiologyEnterotoxinsMiceMicroscopy ElectronBacterial ProteinsCell AdhesionAnimalsBiochemical Society transactions
researchProduct

Characterization ofBacillus thuringiensisisolated from infections in burn wounds

1997

Four strains of Bacillus thuringiensis were isolated from infections in burn wounds and from water used in the treatment of burn wounds. The strains produced large parasporal inclusion bodies composed of 141, 83, and 81 kDa protoxins. The four strains were tested for insecticidal activity against larvae of Pieris brassicae and Aedes aegypti but showed no activity; Vero cell assays for the production of enterotoxins were also negative. Attempts to classify the strains according to flagellar H-serotype showed them all to be non-flagellated. Apart from two occupational health accidents that occurred during the handling of highly concentrated B. thuringiensis fluids, this is the first report of…

Microbiology (medical)Bacterial ToxinsImmunologyBacillus thuringiensisBacillus cereusAedes aegyptiEnterotoxinMicrobiologyMicrobiologyHemolysin ProteinsBacterial ProteinsAedesBacillus thuringiensisChlorocebus aethiopsAnimalsHumansImmunology and AllergyVero CellsPieris brassicaeBacillus thuringiensis Toxinsbiologybacillus thurigiensisinfectionsfungiGeneral Medicinebiology.organism_classificationBacillalesVirologyEndotoxinsInfectious DiseasesWound InfectionVero cellBurnsButterfliesBacteriaFEMS Immunology & Medical Microbiology
researchProduct

In vivo effects of intravascularly applied Escherichia coli hemolysin: dissociation between induction of granulocytopenia and lethality in monkeys.

1993

The effects of intravascular application of endotoxin-depleted Escherichia coli hemolysin (HlyA) was studied in rabbits and monkeys. In rabbits, bolus application of HlyA calculated to effect final blood levels of approximately 2-3 HU/ml (200-300 ng/ml) caused an acute fall of polymorphonuclear blood leukocytes to less than 20% of starting levels within 5 min. Additionally, platelet counts dropped to approximately 30% of starting levels, whereas lymphocyte counts varied considerably and seldom fell to less than 50%. Nine out ten animals that received 2-4 HU/ml toxin died within 90 min post application. These animals presented with signs of acute respiratory failure and post mortem inspectio…

Microbiology (medical)Blood Plateletsmedicine.medical_specialtyPathologyLymphocyteImmunologyBacterial ToxinsSpleenBlood PressurePulmonary EdemaBiologyPulmonary sequestrationLethal Dose 50Hemolysin ProteinsBacterial ProteinsIn vivoInternal medicinemedicineEscherichia coliImmunology and AllergyAnimalsLungLeukopeniaLungDose-Response Relationship DrugPancreatic ElastaseEscherichia coli ProteinsElastaseGeneral Medicinemedicine.diseasePulmonary edemaBlood Cell CountCapillariesMacaca fascicularisEndocrinologymedicine.anatomical_structureInjections Intra-ArterialLiverInjections IntravenousRabbitsmedicine.symptomSpleenAgranulocytosisGranulocytesMedical microbiology and immunology
researchProduct

Specific DNA probes to detect Escherichia coli strains producing cytotoxic necrotising factor type 1 or type 2

1994

Cytotoxic necrotising factors type 1 (CNF1) and type 2 (CNF2) are produced by many Escherichia coli strains isolated from man and animals with intestinal or extra-intestinal colibacillosis. In most laboratories, CNF-producing strains are detected by a cell cytotoxicity assay and confirmed with a neutralisation assay or a mouse footpad assay. In this study, we sought to determine whether DNA probes could detect clinical isolates of E. coli producing CNF2 or CNF1, or both, without the need for cell cultures or animal assays. Two internal fragments of the gene encoding CNF2 were used as DNA probes: a 875-bp XhoI-PstI DNA fragment and an adjacent 335-bp PstI-ClaI fragment. A positive response w…

Microbiology (medical)DNA BacterialDiarrhea[SDV]Life Sciences [q-bio]Bacterial ToxinsRestriction MappingSEQUENCE GENIQUEmedicine.disease_causeMicrobiologyMicrobiologychemistry.chemical_compoundNucleic acid thermodynamicsRestriction mapmedicineEscherichia coliAnimalsHumansSONDE D'ADNEscherichia coliGeneVero CellsEscherichia coli InfectionsbiologyCytotoxinsHybridization probeEscherichia coli ProteinsNucleic Acid HybridizationGeneral Medicinebiology.organism_classificationEnterobacteriaceaeMolecular biology[SDV] Life Sciences [q-bio]chemistryGenes BacterialFACTEUR CYTOTOXIQUE NECROSANTAutoradiographyMolecular probeDNA ProbesDNAHeLa Cells
researchProduct

Cloning of Clostridium difficile toxin B gene and demonstration of high N-terminal homology between toxin A and B.

1990

High titered Clostridium sordellii lethal toxin antiserum, cross-reactive with C. difficile cytotoxin B (ToxB), was used to isolate toxB fragments from a C. difficile expression library. Recombinant clones containing toxB fragments of the 5' and 3' end were isolate. A 2.5-kb HincII fragment of chromosomal DNA overlaps both groups of clones. A partial restriction map of the total toxB gene is presented. The gene is positioned upstream of utxA and toxA, toxB has a size of 6.9 kb, corresponding to a 250-kDa polypeptide. A partial sequence of the 5' end of toxB was determined. The sequence contains 398 bp upstream of toxB with a putative Shine-Dalgarno box (AGGAGA) and 609 bp of the toxB open r…

Microbiology (medical)DNA BacterialImmunologyBacterial ToxinsMolecular Sequence DataRestriction MappingClostridium difficile toxin AClostridium difficile toxin BMolecular cloningBiologyCross ReactionsHomology (biology)Restriction mapBacterial ProteinsSequence Homology Nucleic AcidImmunology and AllergyAmino Acid SequenceCloning MolecularPeptide sequenceGeneticsBase SequenceClostridioides difficileNucleic acid sequenceGeneral MedicineMolecular biologyAntibodies BacterialOpen reading frameGenes BacterialDNA ProbesMedical microbiology and immunology
researchProduct

T lymphocyte-stimulating microbial toxins as ?superantigens?

1991

Infectious pathogens generally have to cope with the host's adaptive immune system, i.e., T and B lymphocytes. Common evasion mechanisms in this complex interaction are antigenic variations, the escape to immunologically priviledged sites or the use of immunosuppressive mechanisms. Many bacteria and other microorganisms eleborate soluble factors or toxins that act suppressively on cells of the immune system, such as pore-forming molecules or proteins that interfere with the function of G proteins. Gram-positive cocci and a mycoplasma have developed an extremely potent mechanism of T cell stimulation by closely mimicking recognition of specific antigen. From the functional similarity to anti…

Microbiology (medical)G proteinT-LymphocytesT cellBacterial ToxinsImmunologyBiologyLymphocyte Activationmedicine.disease_causeMicrobiologyMiceMycoplasmaImmune systemAntigenmedicineSuperantigenAnimalsImmunology and AllergyAntigens BacterialGeneral MedicineMycoplasmaT lymphocyteAcquired immune systemmedicine.anatomical_structureImmunologyMitogensMedical Microbiology and Immunology
researchProduct

The Fish Pathogen Vibrio vulnificus Biotype 2: Epidemiology, Phylogeny, and Virulence Factors Involved in Warm-Water Vibriosis

2015

ABSTRACT Vibrio vulnificus biotype 2 is the etiological agent of warm-water vibriosis, a disease that affects eels and other teleosts, especially in fish farms. Biotype 2 is polyphyletic and probably emerged from aquatic bacteria by acquisition of a transferable virulence plasmid that encodes resistance to innate immunity of eels and other teleosts. Interestingly, biotype 2 comprises a zoonotic clonal complex designated as serovar E that has extended worldwide. One of the most interesting virulence factors produced by serovar E is RtxA1 3 , a multifunctional protein that acts as a lethal factor for fish, an invasion factor for mice, and a survival factor outside the host. Two practically id…

Microbiology (medical)Gene Transfer HorizontalVirulence FactorsPhysiologyFish farmingBacterial ToxinsVirulenceVibrio vulnificusMicrobiologyFish DiseasesMicePlasmidReceptors TransferrinGeneticsAnimalsHumansVibrio vulnificusGenePathogenPhylogenyEelsGeneral Immunology and MicrobiologyEcologybiologyCell Biologybiology.organism_classificationImmunity InnateInfectious DiseasesVibrio InfectionsHorizontal gene transferWater MicrobiologyBacterial outer membranePlasmidsMicrobiology Spectrum
researchProduct

Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: the unknown connection

1994

Microbiology (medical)Microbial toxinsSeptic shockBacterial ToxinsImmunologySepsis syndromeGeneral MedicineBiologymedicine.diseasemedicine.disease_causeShock SepticIon ChannelsSystemic Inflammatory Response SyndromeMicrobiologyPathogenesisBacterial ProteinsStaphylococcus aureusShock (circulatory)ImmunologymedicineAnimalsHumansImmunology and Allergymedicine.symptomMedical Microbiology and Immunology
researchProduct

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
researchProduct

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
researchProduct