Search results for "Bacterial Toxin"

showing 10 items of 192 documents

Subcytocidal attack by staphylococcal alpha-toxin activates NF-kappaB and induces interleukin-8 production.

2001

ABSTRACTFormation of transmembrane pores by staphylococcal alpha-toxin can provoke a spectrum of events depending on target cell species and toxin dose, and in certain cases, repair of the lesions has been observed. Here, we report that transcriptional processes are activated as a response of cells to low toxin doses. Exposure of monocytic (THP-1) or epithelial (ECV304) cells to 40 to 160 ng/ml alpha-toxin provoked a drop in cellular ATP level that was followed by secretion of substantial amounts of interleukin-8 (IL-8). Cells transfected with constructs comprising the proximal IL-8 promoter fused to luciferase or to green fluorescent protein cDNA exhibited enhanced reporter gene expression…

StaphylococcusImmunologyBacterial ToxinsBiologymedicine.disease_causeMicrobiologyCell LineHemolysin ProteinsAdenosine TriphosphatemedicineHumansSecretionLuciferaseInterleukin 8Promoter Regions GeneticRegulation of gene expressionReporter geneCellular Microbiology: Pathogen-Host Cell Molecular InteractionsToxinInterleukin-8NF-kappa BTransfectionMolecular biologyInfectious DiseasesCell cultureParasitologyCaltech Library ServicesInfection and immunity
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Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B

1995

Strain 1470 is the standard typing strain for serogroup F of Clostridium difficile containing both toxin genes, toxA-1470 and toxB-1470. A polymerase chain reaction (PCR)-based approach to the sequencing of the total toxB-1470 gene identified an open reading frame (ORF) of 7104 nucleotides. In comparison with the previously sequenced toxB of C. difficile VP10463, the toxB-1470 gene has 16 additional nucleotides, 13 within the 5'-untranslated region and three within the coding region. The M(r) of ToxB-1470 is 269,262, with an isoelectric point (IP) of 4.16. The equivalent values for ToxB are M(r) 269,709 and IP 4.13. In comparison with ToxB, ToxB-1470 differs primarily in the N-terminal regi…

SwineSequence analysisBacterial ToxinsMolecular Sequence DataRestriction MappingClostridium sordelliiMicrobiologyCell LineMicrobiologyOpen Reading FramesBacterial ProteinsAnimalsCoding regionAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceGeneClostridiumBase SequencebiologyClostridioides difficileCytotoxinsSequence Analysis DNAClostridium difficileClostridium novyibiology.organism_classificationActinsOpen reading frameGenes BacterialEndothelium VascularMolecular Microbiology
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Unexpected Modulation of Recall B and T Cell Responses after Immunization with Rotavirus-like Particles in the Presence of LT-R192G

2010

LT-R192G, a mutant of the thermolabile enterotoxin of E. coli, is a potent adjuvant of immunization. Immune responses are generally analyzed at the end of protocols including at least 2 administrations, but rarely after a prime. To investigate this point, we compared B and T cell responses in mice after one and two intrarectal immunizations with 2/6 rotavirus-like particles (2/6-VLP) and LT-R192G. After a boost, we found, an unexpected lower B cell expansion measured by flow cytometry, despite a secondary antibody response. We then analyzed CD4(+)CD25(+)Foxp3(+) regulatory T cells (Tregs) and CD4(+)CD25(+)Foxp3(-) helper T cells after in vitro (re)stimulation of mesenteric lymph node cells …

T-LymphocytesHealth Toxicology and Mutagenesismedicine.medical_treatmentT cellBacterial ToxinsDose-Response Relationship Immunologiclcsh:Medicinechemical and pharmacologic phenomenaBiologyToxicologyArticleregulatory T cellsEnterotoxinsMiceInterleukin 21Immune systemB-1a lymphocyteAdjuvants ImmunologicAntigenmedicineAnimalsIL-2 receptorCD25B cellB-LymphocytesMice Inbred BALB CB lymphocytemucosal immunizationEscherichia coli Proteinslcsh:RRotavirus VaccinesVirionFOXP3LT-R192Ghemic and immune systemsrotavirusmedicine.anatomical_structureFoxp3ImmunologyFemaleImmunizationAdjuvantToxins
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Glucosylation of Rho proteins by Clostridium difficile toxin B.

1995

TOXIN A and B, the major virulence factors of Clostridium difficile, are the causative agents of antibiotic-associated pseudomembran-ous colitis. In cultured cell lines their potent cytotoxicity results from their ability to induce disaggregation of the microfilament cytoskeleton1,2. Toxin B acts on the low-molecular-mass GTPase Rho A3,4, which is involved in the regulation of the actin cytoskeleton. We report here that toxin B catalyses the incorporation of up to one mole of glucose per mole of RhoA at the amino acid thre-onine at position 37. The modification was identified and localized by tandem electrospray mass spectrometry. UDP-glucose selectively serves as cosubstrate for the monogl…

ThreonineRHOAGlycosylationBacterial ToxinsMolecular Sequence DataClostridium difficile toxin AClostridium difficile toxin Bmacromolecular substancesmedicine.disease_causeMicrofilamentCatalysisMass SpectrometryGTP PhosphohydrolasesBacterial ProteinsGTP-Binding ProteinsmedicineTumor Cells CulturedAnimalsAmino Acid SequenceCytoskeletonActinCells CulturedCytoskeletonMultidisciplinarybiologyToxinClostridioides difficileActin cytoskeletonActinsRecombinant ProteinsRatsGlucoseMarsupialiaBiochemistryGlucosyltransferasesbiology.proteinrhoA GTP-Binding ProteinNature
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Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
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Potential of the Bacillus thuringiensis Toxin Reservoir for the Control of Lobesia botrana (Lepidoptera: Tortricidae), a Major Pest of Grape Plants▿

2006

ABSTRACT The potential of Bacillus thuringiensis Cry proteins to control the grape pest Lobesia botrana was explored by testing first-instar larvae with Cry proteins belonging to the Cry1, Cry2, and Cry9 groups selected for their documented activities against Lepidoptera. Cry9Ca, a toxin from B. thuringiensis , was the protein most toxic to L. botrana larvae, followed in decreasing order by Cry2Ab, Cry1Ab, Cry2Aa, and Cry1Ia7, with 50% lethal concentration values of 0.09, 0.1, 1.4, 3.2, and 8.5 μg/ml of diet, respectively. In contrast, Cry1Fa and Cry1JA were not active at the assayed concentration (100 μg/ml). In vitro binding and competition experiments showed that none of the toxins teste…

Tortricidaeanimal structuresBacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsmedicine.disease_causeLobesia botranaApplied Microbiology and BiotechnologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsLobesia botranaBacillus thuringiensisBotanymedicineInvertebrate MicrobiologyAnimalsVitisPest Control BiologicalCry proteinsPlant DiseasesEcologybiologyBacillus thuringiensis ToxinsToxinbusiness.industryfungiPest controlfood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticultureLarvaPEST analysisbusinessFood ScienceBiotechnology
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UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii.

1996

Abstract We have previously isolated a fibroblast mutant cell with high resistance to the two Rho-modifying glucosyltransferase toxins A and B of Clostridium difficile. We demonstrate here a low level of UDP-glucose in the mutant, which explains its toxin resistance since: (i) to obtain a detectable toxin B-mediated Rho modification in lysates of mutant cells, addition of UDP-glucose was required, and it promoted the Rho modification dose-dependently; (ii) high pressure liquid chromatography analysis of nucleotide extracts of cells indicated that the level of UDP-glucose in the mutant (0.8 nmol/106 cells) was lower than in the wild type (3.7 nmol/106 cells); and (iii) sensitivity to toxin B…

Uridine Diphosphate GlucoseMicroinjectionsMutantBacterial ToxinsClostridium difficile toxin AClostridium sordelliiClostridium difficile toxin Bmedicine.disease_causeBiochemistryMicrobiologyCell LineCricetulusBacterial ProteinsGTP-Binding ProteinsCricetinaemedicineAnimalsMolecular BiologyClostridiumbiologyToxinClostridioides difficileWild typeCell BiologyClostridium difficilebiology.organism_classificationGlucosyltransferasesMutationbiology.proteinGlucosyltransferaseThe Journal of biological chemistry
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Staphylococcus aureus alpha toxin mediates polymorphonuclear leukocyte-induced vasocontraction and endothelial dysfunction.

2002

The effect of Staphylococcus aureus alpha toxin (alpha-toxin) on selectin-mediated neutrophil adhesion was investigated in polymorphonuclear leukocyte- (PMN) induced vasocontraction and endothelial dysfunction. Adherence of human PMNs to rat aortic endothelium increased significantly following stimulation of the endothelium with alpha-toxin (0.1, 0.5, and 1 microg/mL). This effect could be significantly attenuated by monoclonal antibodies directed against P-selectin or fucoidin, a carbohydrate known to block selectins. Unstimulated human PMNs (10(6)cells/mL) were added to organ chambers containing rat aortic rings stimulated with alpha-toxin (0.5 microg/mL). PMNs elicited a significant vaso…

Vascular smooth muscleEndotheliumNeutrophilsBacterial ToxinsPharmacologyBiologyIn Vitro TechniquesCritical Care and Intensive Care MedicineMicrocirculationHemolysin ProteinsFibrinolytic AgentsmedicineCell AdhesionAnimalsHumansEndothelial dysfunctionStaphylococcus aureus alpha toxinAortaThrombinAzepinesTriazolesmedicine.diseaseRatsmedicine.anatomical_structureVasoconstrictionImmunologyEmergency MedicineEndothelium Vascularmedicine.symptomVasoconstrictionSelectinBlood vesselShock (Augusta, Ga.)
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Relationships between Staphylococcus aureus genetic background, virulence factors, agr groups (alleles), and human disease

2002

ABSTRACT The expression of most Staphylococcus aureus virulence factors is controlled by the agr locus, which encodes a two-component signaling pathway whose activating ligand is an agr -encoded autoinducing peptide (AIP). A polymorphism in the amino acid sequence of the AIP and of its corresponding receptor divides S. aureus strains into four major groups. Within a given group, each strain produces a peptide that can activate the agr response in the other member strains, whereas the AIPs belonging to different groups are usually mutually inhibitory. We investigated a possible relationship between agr groups and human S. aureus disease by studying 198 S. aureus strains isolated from 14 asym…

[SDE] Environmental SciencesStaphylococcus aureus[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT][SDV]Life Sciences [q-bio]Bacterial ToxinsImmunologyVirulenceLocus (genetics)Biologymedicine.disease_causeMicrobiologylaw.inventionMicrobiology03 medical and health sciencesBacterial ProteinslawPhylogeneticsmedicineHumansAllelePeptide sequenceComputingMilieux_MISCELLANEOUSAllelesPhylogenyPolymerase chain reaction030304 developmental biologyGenetics0303 health sciencesVirulence030306 microbiologyBacterial InfectionsStaphylococcal Infectionsbiochemical phenomena metabolism and nutritionbacterial infections and mycoses[SDV] Life Sciences [q-bio]Infectious DiseasesPOUVOIR PATHOGENEStaphylococcus aureus[SDE]Environmental SciencesTrans-ActivatorsbacteriaFemaleParasitologyAmplified fragment length polymorphismSignal Transduction
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Detection of Escherichia coli strains producing cytotoxic necrotizing factor type two (CNF2) by enzyme-linked immunosorbent assay

1994

Sheep and rabbit antisera were produced against lysates of E. coli strain 711 (pVir). This K-12 strain carries the Vir plasmid which codes for Cytotoxic Necrotizing Factor type 2 (CNF2). Immunoglobulin G (IgG) fractions of both immune sera were subsequently purified by a two-step precipitation method. To increase the specificity for CNF2, the sheep IgG preparation was extensively adsorbed against both a sonicated extract of isogenic K-12 strain 711 and intact phenol-treated cells of vaccine strain 711 (pVir). An enzyme-linked immunosorbent assay (ELISA) was developed to detect clinical isolates of E. coli producing CNF2, using the final preparations of rabbit and sheep IgG in a double sandw…

[SDV]Life Sciences [q-bio]Bacterial ToxinsEnzyme-Linked Immunosorbent Assaymedicine.disease_causeMicrobiologyImmunoglobulin GMicrobiologyHeLa03 medical and health sciencesAntigenNeutralization TestsmedicineEscherichia coliHumansEscherichia coliComputingMilieux_MISCELLANEOUS030304 developmental biologyAntiserum0303 health sciencesGeneral Veterinarybiology030306 microbiologyCytotoxinsEscherichia coli ProteinsGeneral Medicinebiology.organism_classificationEnterobacteriaceae[SDV] Life Sciences [q-bio]FACTEUR CYTOTOXIQUE NECROSANTbiology.proteinAntibodyCell culture assaysHeLa Cells
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