Search results for "Toxic proteins"

showing 10 items of 19 documents

Global Functional Analyses of Cellular Responses to Pore-Forming Toxins

2011

Here we present the first global functional analysis of cellular responses to pore-forming toxins (PFTs). PFTs are uniquely important bacterial virulence factors, comprising the single largest class of bacterial protein toxins and being important for the pathogenesis in humans of many Gram positive and Gram negative bacteria. Their mode of action is deceptively simple, poking holes in the plasma membrane of cells. The scattered studies to date of PFT-host cell interactions indicate a handful of genes are involved in cellular defenses to PFTs. How many genes are involved in cellular defenses against PFTs and how cellular defenses are coordinated are unknown. To address these questions, we pe…

MAPK/ERK pathwayTranscription GeneticImmunology/Innate ImmunityMessengerInteractomeInfectious Diseases/Bacterial InfectionsRNA interference2.1 Biological and endogenous factorsAetiologyBiology (General)Genes HelminthCaenorhabditis elegansOligonucleotide Array Sequence AnalysisGenetics0303 health sciencesGenomebiologyReverse Transcriptase Polymerase Chain ReactionGenetics and Genomics/Functional Genomics030302 biochemistry & molecular biologyrespiratory systemCell biologyInfectious DiseasesMedical MicrobiologyRNA InterferenceSignal transductionDNA microarrayTranscriptionBiotechnologyResearch ArticleSignal TransductionPore Forming Cytotoxic ProteinsQH301-705.5Virulence FactorsMAP Kinase Signaling System1.1 Normal biological development and functioningBacterial ToxinsImmunologyMicrobiologyDNA-binding proteinCell Line03 medical and health sciencesBacterial ProteinsGeneticUnderpinning researchVirologyEscherichia coliHelminthGeneticsAnimalsHumansRNA MessengerCaenorhabditis elegansCaenorhabditis elegans ProteinsMolecular BiologyGene030304 developmental biologyGenome HelminthCell MembraneGenetics and GenomicsRC581-607biology.organism_classificationrespiratory tract diseasesTranscription Factor AP-1Emerging Infectious DiseasesGenesRNAParasitologyGeneric health relevanceRNA HelminthImmunologic diseases. AllergyPLoS Pathogens
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Toxic Proteins and Peptides

1994

Many animals produce poisonous substances which, even at a relatively low dose, are deleterious or lethal to other organisms, including man. They may serve on the one hand to disable or kill prey, or on the other hand as a protection or defence against predators. These substances are mostly produced by special glands, and both poison reservoirs and specialized structures for delivering the secretion, e.g. stings or modified mouthparts or fangs, are usually also present. In accordance with the aims of this book, we will deal with the comparative biochemistry of the animal toxins as natural products with special structures and functions; a discussion of the mechanisms of their pharmacological…

Comparative BiochemistryBiochemistryToxic proteinsLow doseToxicityAntimicrobial peptidesSecretionBiologySecondary metabolismArthropod mouthparts
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Cigarette smoke promotes inflammasome‐independent activation of caspase‐1 and ‐4 leading to gasdermin D cleavage in human macrophages

2022

Mechanisms and consequences of gasdermin D (GSDMD) activation in cigarette smoke (CS)-associated inflammation and lung disease are unknown. GSDMD is a downstream effector of caspase-1, -8, and -4. Upon cleavage, GSDMD generates pores into cell membranes. Different degrees of GSDMD activation are associated with a range of physiological outputs ranging from cell hyperactivation to pyroptosis. We have previously reported that in human monocyte-derived macrophages CS extract (CSE) inhibits the NLRP3 inflammasome and shifts the response to lipopolysaccharide (LPS) towards the TLR4-TRIF axis leading to activation of caspase-8, which, in turn, activates caspase-1. In the present work, we investig…

InflammationLipopolysaccharidesPore Forming Cytotoxic Proteinsalveolar macrophages caspasecigarette smoke inflammasome lung Caspase 1 Caspases Caspases Initiator Humans Inflammation Intracellular Signaling Peptides and Proteins Lipopolysaccharides Lipopolysaccharides NLR Family Pyrin Domain-Containing 3 Protein Phosphate-Binding Proteins Pore Forming Cytotoxic Proteins Tobacco Cigarette Smoking Inflammasomes.InflammasomesSettore BIO/16 - Anatomia UmanaMacrophagesCaspase 1Intracellular Signaling Peptides and ProteinsPhosphate-Binding ProteinsBiochemistryCaspases InitiatorCigarette SmokingCaspasesNLR Family Pyrin Domain-Containing 3 ProteinTobaccoGeneticsHumansMolecular BiologyBiotechnologyThe FASEB Journal
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Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane

2007

Vibrio cholerae cytolysin (VCC) forms oligomeric transmembrane pores in cholesterol-rich membranes. To better understand this process, we used planar bilayer membranes. In symmetric membranes, the rate of the channel formation by VCC has a superlinear dependency on the cholesterol membrane fraction. Thus, more than one cholesterol molecule can facilitate VCC-pore formation. In asymmetric membranes, the rate of pore formation is limited by the leaflet with the lower cholesterol content. Methyl-beta-cyclodextrin, which removes cholesterol from membranes, rapidly inhibits VCC pore formation, even when it is added to the side opposite that of VCC addition. The results suggest that cholesterol i…

Pore Forming Cytotoxic Proteinsgenetic structuresLipid BilayersBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundMonolayermedicineAnimalsMoleculeVibrio choleraePore-forming toxinMembrane GlycoproteinsPerforinCholesterolbeta-CyclodextrinsGeneral Medicineeye diseasesTransmembrane proteinCholesterolMembraneBiochemistrychemistryVibrio choleraeBiophysicsCattlelipids (amino acids peptides and proteins)sense organsCytolysinBiochimie
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Perforin deficiency attenuates inflammation and tumor growth in colitis-associated cancer

2010

Background: Patients with inflammatory bowel disease (IBD) have a markedly increased risk to develop colon cancer, but there are only limited data about the host antitumor response in such colitis-associated cancer. In the present study we aimed at assessing the role of perforin-dependent effector mechanisms in the immune response in a murine model of colitis-associated colon cancer. Methods: Wildtype and perforin-deficient mice were analyzed in a mouse model of colitis-associated colon cancer using azoxymethane (AOM) and dextran sodium sulfate (DSS). Results: Tumors of wildtype mice showed infiltration of CD4+, CD8+ T cells, natural killer (NK) cells, high numbers of apoptotic cells, and e…

CD4-Positive T-LymphocytesCytotoxicity ImmunologicPore Forming Cytotoxic ProteinsT-LymphocytesMedizinInflammationCD8-Positive T-LymphocytesBiologymedicine.disease_causeInflammatory bowel diseaseMiceImmune systemmedicineAnimalsImmunology and AllergyCytotoxic T cellIntestinal MucosaColitisReverse Transcriptase Polymerase Chain ReactionPerforin DeficiencyDextran SulfateGastroenterologyColitismedicine.diseaseSpecific Pathogen-Free OrganismsKiller Cells NaturalMice Inbred C57BLDisease Models AnimalPerforinChronic DiseaseColonic NeoplasmsImmunologybiology.proteinmedicine.symptomCarcinogenesisInflammatory Bowel Diseases
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Blattella germanica displays a large arsenal of antimicrobial peptide genes

2020

Defence systems against microbial pathogens are present in most living beings. The German cockroach Blattella germanica requires these systems to adapt to unhealthy environments with abundance of pathogenic microbes, in addition to potentially control its symbiotic systems. To handle this situation, four antimicrobial gene families (defensins, termicins, drosomycins and attacins) were expanded in its genome. Remarkably, a new gene family (blattellicins) emerged recently after duplication and fast evolution of an attacin gene, which is now encoding larger proteins with the presence of a long stretch of glutamines and glutamic acids. Phylogenetic reconstruction, within Blattellinae, suggests …

0106 biological sciences0301 basic medicinePore Forming Cytotoxic ProteinsGenome InsectEvolutionary biology010603 evolutionary biology01 natural sciencesGenomeArticle03 medical and health sciencesProtein DomainsPhylogeneticsGene duplicationGene expressionGene familyAnimalsAmino Acid SequenceSymbiosisGenePhylogenyRegulation of gene expressionGeneticsGerman cockroachMultidisciplinarybiologyAntimicrobial responsesBlattellidaebiology.organism_classificationGenome evolution030104 developmental biologyGene Expression RegulationEntomology
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An Ovalbumin Peptide-Specific Cytotoxic T Cell Clone with Antigen Self-Presentation Capacity Uses Two Distinct Mechanisms to Kill Target Cells

1993

Abstract Cloned 10BK.1 T cells with specificity for the ovalbumin peptide OVA257-264 are representative of a novel cell type within the CD8 + subset of T cells. In the presence and in the absence of added antigen presenting cells these T cells react toward antigen (Ag) by proliferation and lymphokine production. These data suggest self-presentation of the Ag by 10BK.1 cells. Here we present evidence that 10BK.1 cells exhibit cytotoxic activity that involves two different cytotoxic effector mechanisms. (i) One mechanism is fast killing activity, apparent within 4 hr. Constitutive mouse T cell-specific proteinase-1 (MTSP-1) activity, constitutive expression of MTSP-1 RNA, increased by Ag chal…

Cytotoxicity ImmunologicPore Forming Cytotoxic ProteinsOvalbuminImmunologyAntigen presentationAntigen-Presenting CellsBiologyCytoplasmic GranulesLymphocyte ActivationGranzymesCell LineMiceInterleukin 21AntigenAnimalsCytotoxic T cellIL-2 receptorAntigen-presenting cellLymphotoxin-alphaMembrane GlycoproteinsCD40PerforinTumor Necrosis Factor-alphaSerine EndopeptidasesDegranulationMolecular biologyClone Cellsbiology.proteinInterleukin-2T-Lymphocytes CytotoxicCellular Immunology
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A lipocentric view of peptide-induced pores

2010

Although lipid membranes serve as effective sealing barriers for the passage of most polar solutes, nonmediated leakage is not completely improbable. A high activation energy normally keeps unassisted bilayer permeation at a very low frequency, but lipids are able to self-organize as pores even in peptide-free and protein-free membranes. The probability of leakage phenomena increases under conditions such as phase coexistence, external stress or perturbation associated to binding of nonlipidic molecules. Here, we argue that pore formation can be viewed as an intrinsic property of lipid bilayers, with strong similarities in the structure and mechanism between pores formed with participation …

Pore Forming Cytotoxic ProteinsCell Membrane PermeabilityMembrane permeabilityMembrane lipidsPore energeticsBiophysicsThermal fluctuationsReviewMolecular Dynamics SimulationSurface tensionMembrane LipidsAnti-Infective AgentsLipid bilayerChemistryBilayerLipidic poreGeneral MedicinePermeationCrystallographyMembrane permeabilityMembraneBiophysicsAntimicrobial peptidePore structurePorosityPore-forming proteinsEuropean Biophysics Journal
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Gamma delta T cells inhibit in vitro growth of the asexual blood stages of Plasmodium falciparum by a granule exocytosis-dependent cytotoxic pathway …

2004

Several reports have stated the ability of gamma delta T cells to inhibit the growth of the asexual blood stages of Plasmodium falciparum in vitro. However, little information is available about the mechanisms involved. In this study, in vitro systems were used to study the role of the granule exocytosis-dependent cytotoxic pathway in the growth inhibition/killing of P. falciparum by human gamma delta T cells. Our results show that the inhibition requires cell-to-cell contact and that gamma delta T cells kill the asexual blood stages of P. falciparum through a granule exocytosis-dependent cytotoxic pathway after recognition of certain ligands or molecules expressed on the surface of infecte…

Antigens Differentiation T-LymphocytePore Forming Cytotoxic ProteinsT-LymphocytesImmunologyPlasmodium falciparumReceptors Antigen T-CellCell CommunicationCytoplasmic GranulesExocytosischemistry.chemical_compoundImmunology and AllergyCytotoxic T cellAnimalsHumansRNA MessengerGranulysinMembrane GlycoproteinsbiologyPerforinDegranulationPlasmodium falciparumbiology.organism_classificationIn vitroCell biologyPerforinchemistrybiology.proteinGrowth inhibitionCD8European journal of immunology
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Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as beta-barrel toxins from gram-positive organisms.

2009

Vibrio cholerae cytolysin (VCC) forms SDS-stable heptameric beta-barrel transmembrane pores in mammalian cell membranes. In contrast to structurally related pore formers of gram-positive organisms, no oligomeric prepore stage of assembly has been detected to date. In the present study, disulfide bonds were engineered to tie the pore-forming amino acid sequence to adjacent domains. In their nonreduced form, mutants were able to bind to rabbit erythrocytes and to native erythrocyte membranes suspended in PBS solution and form SDS-labile oligomers. These remained nonfunctional and represented the long-sought VCC prepores. Disulfide bond reduction in these oligomers released the pore-forming se…

Models MolecularPore Forming Cytotoxic ProteinsMutantBiologyIn Vitro Techniquesmedicine.disease_causeGram-Positive BacteriaBiochemistryModels Biologicalchemistry.chemical_compoundProtein structureGeneticsmedicineAnimalsCysteineProtein Structure QuaternaryMolecular BiologyPeptide sequenceVibrio choleraeCytotoxinsErythrocyte MembraneTransmembrane proteinRecombinant ProteinsMonomerMembraneBiochemistrychemistryVibrio choleraeMutagenesis Site-DirectedCytolysinRabbitsBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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