Search results for "Bacteria"

showing 10 items of 4919 documents

Anticancer activity of biogenerated silver nanoparticles: an integrated proteomic investigation

2018

Silver nanoparticles (AgNPs), embedded into a specific polysaccharide (EPS), were biogenerated by Klebsiella oxytoca DSM 29614 under aerobic (AgNPs-EPSaer) and anaerobic conditions (AgNPs-EPSanaer). Both AgNPs-EPS matrices were tested by MTT assay for cytotoxic activity against human breast (SKBR3 and 8701-BC) and colon (HT-29, HCT 116 and Caco-2) cancer cell lines, revealing AgNPs-EPSaer as the most active, in terms of IC50, with a more pronounced efficacy against breast cancer cell lines. Therefore, colony forming capability, morphological changes, generation of reactive oxygen species (ROS), induction of apoptosis and autophagy, inhibition of migratory and invasive capabilities and prote…

0301 basic medicineProgrammed cell deathSettore BIO/11 - Biologia MolecolareMitochondrionmedicine.disease_causeSettore BIO/19 - Microbiologia Generale03 medical and health sciencesproteomicsbreast cancer cellmedicineMTT assaySettore BIO/06 - Anatomia Comparata E Citologiabacteriachemistry.chemical_classificationAnticancer activity; Bacteria; Breast cancer cells; Proteomics; Silver nanoparticles (AgNPs); OncologyReactive oxygen speciesBreast cancer cellsChemistryAutophagysilver nanoparticles (AgNPs)Cell biology030104 developmental biologyanticancer activitysilver nanoparticles (AgNPs); bacteria; breast cancer cells; anticancer activity; proteomicsOncologyApoptosisSKBR3Oxidative stressResearch Paper
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Artefactual band patterns by SDS-PAGE of the Vip3Af protein in the presence of proteases mask the extremely high stability of this protein.

2018

Abstract Vip3 proteins are secretable proteins from Bacillus thuringiensis with important characteristics for the microbiological control of agricultural pests. The exact details of their mode of action are yet to be disclosed and the crystallographic structure is still unknown. Vip3 proteins are expressed as protoxins that have to be activated by the insect gut proteases. A previous study on the peptidase processing of Vip3Aa revealed that the protoxin produced artefactual band patterns by SDS-PAGE due to the differential stability of this protein and the peptidases to SDS and heating (Bel et al., 2017 Toxins 9:131). To determine whether this phenomenon also applies to other Vip3A proteins…

0301 basic medicineProteases030106 microbiologyBacillus thuringiensisSpodopteraSpodopteraCleavage (embryo)Biochemistry03 medical and health sciencesBacterial ProteinsStructural BiologyBacillus thuringiensismedicineAnimalsMode of actionMolecular BiologyPolyacrylamide gel electrophoresisbiologyChemistryProtein StabilityfungiMidgutGeneral Medicinebiology.organism_classificationTrypsin030104 developmental biologyBiochemistryInsect ProteinsElectrophoresis Polyacrylamide Gelmedicine.drugPeptide HydrolasesInternational journal of biological macromolecules
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Protease‐activated receptor signaling in intestinal permeability regulation

2019

Protease-activated receptors (PARs) are a unique class of G-protein-coupled transmembrane receptors, which revolutionized the perception of proteases from degradative enzymes to context-specific signaling factors. Although PARs are traditionally known to affect several vascular responses, recent investigations have started to pinpoint the functional role of PAR signaling in the gastrointestinal (GI) tract. This organ is exposed to the highest number of proteases, either from the gut lumen or from the mucosa. Luminal proteases include the host's digestive enzymes and the proteases released by the commensal microbiota, while mucosal proteases entail extravascular clotting factors and the enzy…

0301 basic medicineProteasesCell typeProtease-activated receptorReceptors Proteinase-ActivatedBiologyBiochemistryPermeabilityEpitheliumInflammatory bowel disease03 medical and health sciencesGastrointestinal cancer0302 clinical medicineImmune systemmedicineAnimalsHumansProtease-activated receptorIntestinal MucosaSymbiosisReceptorMolecular BiologyMicrobial proteasesGastrointestinal NeoplasmsClotting factorIntestinal permeabilityCoagulationMicrobiotaEpithelial barrier functionCell BiologyInflammatory Bowel Diseasesmedicine.diseaseIntestinal epitheliumTissue factorGastrointestinal MicrobiomeCell biologyIntestineGastrointestinal TractDisease Models Animal030104 developmental biologyGene Expression RegulationBacterial Translocation030220 oncology & carcinogenesisPeptide HydrolasesSignal Transduction
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Insights into the Structure of the Vip3Aa Insecticidal Protein by Protease Digestion Analysis

2017

Vip3 proteins are secretable proteins from Bacillus thuringiensis whose mode of action is still poorly understood. In this study, the activation process for Vip3 proteins was closely examined in order to better understand the Vip3Aa protein stability and to shed light on its structure. The Vip3Aa protoxin (of 89 kDa) was treated with trypsin at concentrations from 1:100 to 120:100 (trypsin:Vip3A, w:w). If the action of trypsin was not properly neutralized, the results of SDS-PAGE analysis (as well as those with Agrotis ipsilon midgut juice) equivocally indicated that the protoxin could be completely processed. However, when the proteolytic reaction was efficiently stopped, it was revealed t…

0301 basic medicineProteasesHealth Toxicology and MutagenesisSize-exclusion chromatographyBeta sheetBacillus thuringiensislcsh:MedicineBiologyToxicologyCleavage (embryo)ArticleProtein Structure Secondary03 medical and health sciencestrypsin inhibitorsBacterial ProteinsSDS-PAGE artefactprotease stabilitymedicinebacterial secreted proteinsAnimalsTrypsinMode of actionProtein secondary structureVip proteinsIntestinal Secretionslcsh:Rtoxin activationVip proteins; bacterial secreted proteins; toxin activation; proteolytic activation; trypsin inhibitors; <i>Bacillus thuringiensis</i>; SDS-PAGE artefact; protease stabilityTrypsinMolecular biologyLepidoptera030104 developmental biologyBiochemistryproteolytic activationLarvaProteolysisPeptidesAlpha helixmedicine.drugToxins
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Analysis of cross-resistance to Vip3 proteins in eight insect colonies, from four insect species, selected for resistance to Bacillus thuringiensis i…

2018

Abstract Bacillus thuringiensis Vip3 proteins are synthesized and secreted during the vegetative growth phase. They are activated by gut proteases, recognize and bind to midgut receptors, form pores and lyse cells. We tested the susceptibility to Vip3Aa and Vip3Ca of Cry1A-, Cry2A-, Dipel- and Vip3-resistant insect colonies from different species to determine whether resistance to other insecticidal proteins confers cross-resistance to Vip3 proteins. As expected, the colonies resistant to Cry1A proteins, Dipel (Helicoverpa armigera, Trichoplusia ni, Ostrinia furnacalis and Plodia interpunctella) or Cry2Ab (H. armigera and T. ni) were not cross-resistant to Vip3 proteins. In contrast, H. arm…

0301 basic medicineProteasesInsectabiologymedia_common.quotation_subjectfungi030106 microbiologyBacillus thuringiensisMidgutInsectHelicoverpa armigerabiology.organism_classificationMicrobiologyInsecticide Resistance03 medical and health sciencesBacterial ProteinsBacillus thuringiensisTrichoplusiaAnimalsPest Control BiologicalEcology Evolution Behavior and SystematicsCross-resistancemedia_commonOstrinia furnacalisJournal of Invertebrate Pathology
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Ephestia kuehniella tolerance to Bacillus thuringiensis Cry1Aa is associated with reduced oligomer formation

2016

The basis of the different susceptibility of Ephestia kuehniella to the Cry1Aa and Cry1Ac δ-endotoxins from Bacillus thuringiensis kurstaki BNS3 was studied. Both toxins bound specifically to the BBMV of E. kuehniella. The result of the ligand blot showed that Cry1Ac bound to three putative receptors of about 100, 65 and 80 kDa and Cry1Aa interacted only with a 100 kDa protein. Pronase digestion of the BBMV-bound toxins was used to analyze the toxin insertion. Both toxins inserted into the BBMV as monomers however, a 14 kDa peptide of α4-α5 which correspond to the oligomeric form of this peptide was detected in case of Cry1Ac only. Analysis of the in vitro oligomerisation of these toxins in…

0301 basic medicineProtein ConformationBacillus thuringiensisBiophysicsPeptidemedicine.disease_causeBiochemistryOligomerHemolysin Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsBacillus thuringiensismedicineAnimalsReceptorMolecular Biologychemistry.chemical_classificationBacillus thuringiensis Toxins030102 biochemistry & molecular biologybiologyToxinfungiCell BiologyLigand (biochemistry)biology.organism_classificationEndotoxinsLepidopteraBlot030104 developmental biologyBiochemistryCry1AcchemistryProtein MultimerizationBiochemical and Biophysical Research Communications
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Mcl-1 and Bok transmembrane domains : Unexpected players in the modulation of apoptosis

2020

The Bcl-2 protein family comprises both proand antiapoptotic members that control the permeabilization of the mitochondrial outer membrane, a crucial step in the modulation of apoptosis. Recent research has demonstrated that the carboxyl-terminal transmembrane domain (TMD) of some Bcl-2 protein family mem-bers can modulate apoptosis; however, the transmembrane interactome of the antiapoptotic protein Mcl-1 remains largely unexplored. Here, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes with full-length Mcl-1 protein with regards to its antiapoptotic function, and induces cell death in a Bok-dependent manner. While the Bok TMD oligomers locate p…

0301 basic medicineProtein familyMitochondrionBCL-X(L)Endoplasmic ReticulumInteractome114 Physical sciences03 medical and health sciencesBok0302 clinical medicineProtein DomainsMITOCHONDRIAhemic and lymphatic diseasesAnimalsHumansBcl-2Inner mitochondrial membraneMultidisciplinaryCell DeathChemistryEndoplasmic reticulumapoptosisMcl-1PATHWAYSLOCALIZATIONBiological SciencesTransmembrane protein3. Good healthCell biologytransmembraneTransmembrane domainstomatognathic diseasesGLYCOPHORIN-A DIMERIZATION030104 developmental biologyHELIX PACKINGProto-Oncogene Proteins c-bcl-2BAX030220 oncology & carcinogenesisMitochondrial MembranesPROSURVIVAL BCL-2 PROTEINSMOTIFSURVIVALMyeloid Cell Leukemia Sequence 1 Protein1182 Biochemistry cell and molecular biologyBacterial outer membraneHeLa Cells
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Under control: how a dietary additive can restore the gut microbiome and proteomic profile, and improve disease resilience in a marine teleostean fis…

2017

[Background]: The constant increase of aquaculture production and wealthy seafood consumption has forced the industry to explore alternative and more sustainable raw aquafeed materials, and plant ingredients have been used to replace marine feedstuffs in many farmed fish. The objective of the present study was to assess whether plant-based diets can induce changes in the intestinal mucus proteome, gut autochthonous microbiota and disease susceptibility of fish, and whether these changes could be reversed by the addition of sodium butyrate to the diets. Three different trials were performed using the teleostean gilthead sea bream (Sparus aurata) as model. In a first preliminary short-term tr…

0301 basic medicineProteomicsAliments BiotecnologiaProteomeAquaculturemedicine.disease_causechemistry.chemical_compoundFish DiseasesAquacultureSparus aurataFood science2. Zero hungerPathogen challengebiologyDiet VegetarianSodium butyrate04 agricultural and veterinary sciences3. Good healthIntestineslcsh:QR100-130Microbiology (medical)Fish farmingParasitic Diseases AnimalIntestinal parasiteButyrateMicrobiologylcsh:Microbial ecology03 medical and health sciencesIntestinal healthmedicineAnimals14. Life underwaterMicrobiomeMyxozoaNutricióNutritionPeixos Alimentacióbusiness.industryPhotobacteriumResearchEnteromyxum leeiSodium butyratePhotobacteriumbiology.organism_classificationAnimal FeedSea BreamGastrointestinal Microbiome030104 developmental biologychemistry040102 fisheries0401 agriculture forestry and fisheriesButyric AcidMicrobiomebusinessBacteria
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Elucidating the molecular physiology of lantibiotic NAI-107 production in Microbispora ATCC-PTA-5024.

2016

Background The filamentous actinomycete Microbispora ATCC-PTA-5024 produces the lantibiotic NAI-107, which is an antibiotic peptide effective against multidrug-resistant Gram-positive bacteria. In actinomycetes, antibiotic production is often associated with a physiological differentiation program controlled by a complex regulatory and metabolic network that may be elucidated by the integration of genomic, proteomic and bioinformatic tools. Accordingly, an extensive evaluation of the proteomic changes associated with NAI-107 production was performed on Microbispora ATCC-PTA-5024 by combining two-dimensional difference in gel electrophoresis, mass spectrometry and gene ontology approaches. R…

0301 basic medicineProteomicsfood.ingredientMetabolic networkATP-binding cassette transporterActinomycetes Antibiotic production Differential proteomics 2D-DIGE and mass spectrometry Metabolic pathways Regulatory network Molecular and cellular functionsBiologyBioinformaticsProteomicsGram-Positive Bacteria03 medical and health sciencesfoodBacteriocinsActinomycetesGenetics2D-DIGE and mass spectrometryDifferential proteomics2. Zero hungerGel electrophoresisLipid metabolismRegulatory networkbiology.organism_classificationDrug Resistance MultipleAnti-Bacterial AgentsActinobacteriaMetabolic pathway030104 developmental biologyBiochemistryMicrobisporaMetabolic pathwaysATP-Binding Cassette TransportersAntibiotic productionPeptidesBacteriaMolecular and cellular functionsBiotechnologyResearch ArticleBMC genomics
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Innovative Approaches Using Lichen Enriched Media to Improve Isolation and Culturability of Lichen Associated Bacteria

2016

Lichens, self-supporting mutualistic associations between a fungal partner and one or more photosynthetic partners, also harbor non-photosynthetic bacteria. The diversity and contribution of these bacteria to the functioning of lichen symbiosis have recently begun to be studied, often by culture-independent techniques due to difficulties in their isolation and culture. However, culturing as yet unculturable lichenic bacteria is critical to unravel their potential functional roles in lichen symbiogenesis, to explore and exploit their biotechnological potential and for the description of new taxa. Our objective was to improve the recovery of lichen associated bacteria by developing novel isol…

0301 basic medicinePseudevernia furfuraceaSanitizationMicroorganismlcsh:MedicineLichenologyPlant ScienceMicrobial PhysiologyMedicine and Health SciencesPublic and Occupational Healthlcsh:ScienceLichenskin and connective tissue diseasesFungicidesMultidisciplinaryintegumentary systemMicrobial Growth and DevelopmentAgricultureEquipment SterilizationThallusLaboratory EquipmentInfectious DiseasesLichenologyEngineering and TechnologyBiological CulturesAgrochemicalsResearch ArticleEquipment PreparationInfectious Disease ControlLichensNatamycin030106 microbiologyEquipmentBuffersBiologyResearch and Analysis MethodsMicrobiologyMicrobiologyRamalina farinacea03 medical and health sciencesAscomycotaSymbiosisstomatognathic systemFilter SterilizationBotanyBacteriological TechniquesBacteriaBacterial Growthlcsh:ROrganismsFungiBiology and Life Sciencesbiology.organism_classificationCulture MediaHealth CareDisinfectionstomatognathic diseases030104 developmental biologylcsh:QPreventive MedicineBacteriaDevelopmental Biology
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