Search results for "Exotoxin"

showing 10 items of 22 documents

Separation of T-cell-stimulating activity from streptococcal M protein

1992

The superantigenic properties of M protein type 5 of Streptococcus pyogenes have been implicated as an important pathogenicity factor in streptococcal autoimmune diseases. Here we show that after a single purification step by affinity chromatography on immobilized albumin or fibrinogen, M protein has no mitogenic activity for T cells. We demonstrate that the superantigenicity of M proteins of type 5 and type 1 is due to contamination with the highly potent pyrogenic exotoxins of S. pyogenes in the range of 0.1 to 0.01%. These results raise a general caveat for work with these extremely active T-cell mitogens, because the mitogenicity of other streptococcal or staphylococcal proteins could b…

AntigenicityMyeloma proteinT-LymphocytesT cellImmunologyExotoxinschemical and pharmacologic phenomenaBiologyLymphocyte Activationmedicine.disease_causeMicrobiologyMicrobiologyBacterial ProteinsAffinity chromatographymedicineSuperantigenHumansAntigens BacterialMembrane Proteinshemic and immune systemsInfectious Diseasesmedicine.anatomical_structureMembrane proteinStreptococcus pyogenesParasitologyMitogensCarrier ProteinsExotoxinBacterial Outer Membrane ProteinsResearch ArticleInfection and Immunity
researchProduct

Stimulation of human T cells by microbial 'superantigens'.

1991

The enterotoxins and the TSST of S. aureus, the erythrogenic toxins A and C of S. pyogenes and a still uncharacterized exoprotein of M. arthritidis belong to a family of exotoxins that have in common a potent mitogenic activity for T lymphocytes of several species. These proteins stimulate CD4+ and C8+ T cells, as well as a fraction of gamma delta TCR-bearing T cells by cross-linking variable parts of the T cell antigen receptor with MHC class II molecules on accessory or target cells. They are functionally bivalent molecules having distinct interaction sites for variable parts of the TCR and for nonpolymorphic parts of the MHC class II molecule. For alpha beta TCR-bearing T cells the V bet…

Antigens BacterialT cellReceptors Antigen T-Cell alpha-betaT-LymphocytesImmunologyCD1CD28ExotoxinsStreptamerMHC restrictionBiologyIn Vitro TechniquesLymphocyte ActivationMicrobiologyInterleukin 21Enterotoxinsmedicine.anatomical_structuremedicineCytotoxic T cellHumansMitogensAntigen-presenting cellImmunologic research
researchProduct

Update on the detection of beta-exotoxin in Bacillus thuringiensis strains by HPLC analysis.

2001

Aims: The current work aimed to study the presence of β-exotoxin by high-performance liquid chromatography (HPLC) in supernatant fluids from final whole cultures of the 69 type strains and 13 subtypes of Bacillus thuringiensis strains, as well as from some insecticidal strains. Methods and Results: Results from HPLC and bioassays with Ephestia kuhniella (Lepidoptera Pyralidae) were compared. Type I β-exotoxin was only detected in type strains representing serotypes H1, H9 and H10a,10b. Discrepancies between HPLC and bioassays were found in H8a,8b and some insecticidal strains, which suggests the occurrence of another soluble toxin different from type I β-exotoxin, possibly type II β-exotoxi…

Bacillus (shape)BacillaceaeAdenosineInsectabiologyToxinEphestiaBacillus thuringiensisSugar AcidsGeneral Medicinebiology.organism_classificationmedicine.disease_causeApplied Microbiology and BiotechnologyBacillalesMicrobiologyBacillus thuringiensismedicinebacteriaBioassayAnimalsBiological AssayExotoxinChromatography High Pressure LiquidBiotechnologyJournal of applied microbiology
researchProduct

Small GTP-binding proteins of the Rho- and Ras-subfamilies are not involved in the actin rearrangements induced by attaching and effacingEscherichia …

1998

Attaching and effacing Escherichia coli (AEEC) are extracellular pathogens that induce the formation of actin-rich structures at their sites of attachment to eukaryotic host cells. We analysed whether small GTP-binding proteins of the Rho- and Ras-subfamilies, which control the cellular actin system, are essential for these bacterial-induced microfilament reorganizations. For this purpose we specifically inactivated them using the Clostridium difficile toxins TcdB-10463 and TcdB-1470. Such treatment led to a dramatic breakdown of the normal actin cytoskeleton, but did not abrogate the bacterial-induced actin rearrangements. Our data therefore indicate that the microfilament reorganizations …

Bacterial ToxinsExotoxinsArp2/3 complexmacromolecular substancesShiga ToxinsMicrofilamentMicrobiologyGTP-Binding ProteinsEscherichia coliGeneticsAnimalsHumansActin-binding proteinCytoskeletonMolecular BiologyActinbiologyClostridioides difficileActin remodelingActin cytoskeletonActinsActin CytoskeletonMicroscopy ElectronBiochemistryMicroscopy Electron Scanningras Proteinsbiology.proteinCattleMDia1HeLa CellsFEMS Microbiology Letters
researchProduct

Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins.

1996

Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin are well-studied prototypes of pore-forming bacterial cytotoxins. Each is produced as a water-soluble single-chain polypeptide that inserts into target membranes to form aqueous transmembrane pores. This review will compare properties of the three toxin prototypes, highlighting the similarities and also the differences in their structure, mode of binding, mechanism of pore formation, and the responses they elicit in target cells. Pore-forming toxins represent the most potent and versatile weapons with which invading microbes damage the host macroorganism.

Bacterial ToxinsLipid BilayersMolecular Sequence Datamedicine.disease_causeBiochemistryMicrobiologyMicrobiologyHemolysin ProteinsBacterial ProteinsEscherichiaGeneticsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologyEscherichia colibiologyToxinEscherichia coli ProteinsCell MembraneHemolysinGeneral Medicinebiology.organism_classificationEnterobacteriaceaeBiochemistryStreptolysinsStreptolysinCytolysinExotoxinArchives of microbiology
researchProduct

Role of iron, capsule, and toxins in the pathogenicity of Vibrio vulnificus biotype 2 for mice

1994

The virulence mechanisms of Vibrio vulnificus biotype 2 have been studied and compared with those of biotype 1 in mice as the experimental animals. Biotype 2 isolates from European eels were as virulent for mice as biotype 1 strains (50% lethal dose, about 10(5) CFU per mouse); a septicemic infection developed in less than 24 h. These strains had several properties in common with biotype 1 organisms including capsule expression, uptake of various iron sources, and production of exoproteins, whose role in mouse virulence has been demonstrated. We also discuss the implication of biotype 2 strains in human infections.

Blood Bactericidal ActivityIronImmunologyExotoxinsVirulenceVibrio vulnificusIn Vitro Techniquesmedicine.disease_causeMicrobiologyMicrobiologyMiceSpecies SpecificityVibrionaceaeVibrio InfectionsmedicineAnimalsHumansVibrioEelsVirulencebiologyToxinLethal dosebiology.organism_classificationVibrioBacterial Typing TechniquesInfectious DiseasesVibrio InfectionsParasitologyBacteriaResearch ArticleInfection and Immunity
researchProduct

The Human T Cell Response to Mitogenic Microbial Exotoxins

1991

Nearly every infectious pathogen has to cope with the host’s adaptive immune response. Common evasion mechanisms in this complex interaction are antigenic variations, the escape to immunologically privileged sites, or the use of immunosuppressive mechanisms. Many bacteria and other microorganisms elaborate 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 antigen recognition and the …

Cellular immunityT cellT lymphocyteBiologymedicine.disease_causeAcquired immune systemMicrobiologyImmune systemmedicine.anatomical_structureAntigenImmunologymedicineSuperantigenExotoxin
researchProduct

Rapid whole protein quantification of staphylococcal enterotoxin B by liquid chromatography

2012

Abstract Food poisoning caused by Staphylococcus aureus is one of the most important foodborne diseases in the world. The ability of these bacteria to produce one or more enterotoxins in milk and dairy products is linked to staphylococcal food poisoning. Enterotoxin B (SEB) is an exotoxin produced by S. aureus and is one of the compounds most frequently involved in staphylococcal food poisoning worldwide. In this work, 20 samples of milk collected from restaurants have been studied for the presence of S. aureus enterotoxigenic strains. All the isolates from milk samples have been analysed by liquid chromatography-coupled with diode array detector for the rapid identification and quantificat…

Detection limitFood poisoningChromatographyGeneral MedicineEnterotoxinBiologymedicine.diseasemedicine.disease_causebiology.organism_classificationAnalytical ChemistryMicrobiologyStaphylococcal Food PoisoningStaphylococcus aureusChromatography detectormedicineFood scienceExotoxinBacteriaFood ScienceFood Chemistry
researchProduct

Toxic and enzymatic activities of Vibrio vulnificus biotype 2 with respect to host specificity

1996

In this work, the enzymatic activities of selected strains of biotypes 1 and 2 of Vabrio vulnificus were analyzed by using conventional methods and the API ZYM system. The toxic activities of extracellular products (ECPs) were further evaluated by in vitro and in vivo experiments. The ECPs of both biotypes (i) showed high-level hydrolytic activities, (ii) displayed cytotoxicity for fish cell lines, and (iii) were lethal for eels. Exotoxins seem to be proteinaceous since heat treatment of ECP samples destroyed their toxicity. Only biotype 2 strains were virulent for cels, suggesting that host specificity must be related to differences in cell surface properties. Infectivity trials with other…

Hot TemperatureBacterial ToxinsExotoxinsVirulenceVibrio vulnificusBiologyApplied Microbiology and BiotechnologyCell LineMicrobiologyfluids and secretionsSpecies SpecificityVibrionaceaeExtracellularAnimalsCytotoxicityVibrioInfectivityEelsCell DeathVirulenceEcologyHydrolysisFishesbiology.organism_classificationVibrioBacterial Typing TechniquesBacteriaResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
researchProduct

Staphylococcal alpha-toxin provokes neutrophil-dependent cardiac dysfunction: role of ICAM-1 and cys-leukotrienes.

2002

The role of polymorphonuclear neutrophils (PMN) in septic myocardial dysfunction is presently unknown. Staphylococcus aureus infections are frequently associated with septic sequelae. Therefore, we perfused isolated rat hearts with low doses of α-toxin, the major staphylococcal exotoxin, followed by application of human PMN, N-formyl-methionyl-leucyl-phenylalanine, and arachidonic acid. In contrast to sham-perfused hearts (no α-toxin), a rise in coronary perfusion pressure (CPP) and a reduction of contractile function were noted, and cardiac expression of intercellular adhesion molecule (ICAM)-1 was detected by immunohistochemical methods and real-time PCR. Histological analysis and myelope…

LeukotrienesHeart diseasePhysiologyNeutrophilsNeutrophileBacterial ToxinsExotoxinsThiophenesIn Vitro Techniquesmedicine.disease_causePathogenesisHemolysin ProteinsPhysiology (medical)medicineAnimalsHumansICAM-1Arachidonic AcidToxinbusiness.industryMyocardiumHydrazonesHeartmedicine.diseaseIntercellular Adhesion Molecule-1RatsN-Formylmethionine Leucyl-PhenylalaninePerfusionStaphylococcus aureusImmunologyCirculatory systemCardiology and Cardiovascular MedicinebusinessOligonucleotide ProbesExotoxinAmerican journal of physiology. Heart and circulatory physiology
researchProduct