Search results for "Thermal"

showing 10 items of 3576 documents

Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

2017

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorim…

0301 basic medicineProtein subunitMutantBiophysicsHeterologousBiochemistryChaperoninChaperoninlcsh:Biochemistry03 medical and health sciencesDSC differential scanning calorimetryCCT% chaperoninPf Pyrococcus furiosusDenaturation (biochemistry)lcsh:QD415-436Molecular Biologylcsh:QH301-705.5DLS dynamic light scatteringbiologyITC isothermal titration calorimetryWild typeIsothermal titration calorimetryCell BiologyChaperonopathiesbiology.organism_classificationProtein calorimetryNeuropathyPyrococcus furiosus030104 developmental biologyBiochemistryBiophysiclcsh:Biology (General)Pyrococcus furiosusChaperonopathieCCT5; Chaperonin; Chaperonopathies; Neuropathy; Protein calorimetry; Pyrococcus furiosus; Biophysics; Biochemistry; Molecular Biology; Cell BiologyCCT5Pyrococcus furiosuResearch ArticlePf-CD1 Pyrococcus furiosus chaperonin subunit with the last 22 amino acids deletedBiochemistry and Biophysics Reports
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Modeling the heat inactivation of foodborne pathogens in milk powder : High relevance of the substrate water activity

2017

International audience; Due to the ability of foodborne pathogens to survive in low moisture foods, the decontamination of these products is an important issue in food hygiene. Up to now, such decontamination has mostly been achieved through empirical methods. The intention of this work is to establish a more rational use of heat treatment cycles. The effects of thermal treatment cycles on the inactivation of dried Salmonella Typhimurium, Salmonella Senftenberg, Cronobacter sakazakii and Escherichia coli were assessed. Bacteria were mixed with whole milk powder and dried down to different water activity levels (0.11, 0.25, 0.44 and 0.58). The rate of inactivated bacteria was determined afte…

0301 basic medicineSalmonellaHot TemperatureTime FactorsWater activityFood HandlingThermal resistance030106 microbiologymedicine.disease_causeFoodborne Diseases03 medical and health sciencesCronobacter sakazakiiGram-Negative Bacteria[SDV.IDA]Life Sciences [q-bio]/Food engineeringFood QualitymedicineEscherichia coliAnimalsSalmonella SenftenbergFood scienceEscherichia coliDecontamination2. Zero hungerMicrobial ViabilitybiologyMoisturePredictive microbiologyChemistry[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringWaterHuman decontaminationModels Theoreticalbiology.organism_classificationLow water activity foodCronobacter sakazakii6. Clean waterMilk13. Climate actionSalmonella TyphimuriumFood MicrobiologyPowdersBacteriaFood Science
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Cellular Injuries in Cronobacter sakazakii CIP 103183T and Salmonella enterica Exposed to Drying and Subsequent Heat Treatment in Milk Powder

2018

International audience; Because of the ability of foodborne pathogens to survive in low-moisture foods, their decontamination is an important issue in food protection. This study aimed to clarify some of the cellular mechanisms involved in inactivation of foodborne pathogens after drying and subsequent heating. Individual strains of Salmonella Typhimurium, Salmonella Senftenberg, and Cronobacter sakazakii were mixed into whole milk powder and dried to different water activity levels (0.25 and 0.58); the number of surviving cells was determined after drying and subsequent thermal treatments in closed vessels at 90 and 100 degrees C, for 30 and 120 s. For each condition, the percentage of unc…

0301 basic medicineSalmonellalcsh:QR1-502medicine.disease_causelcsh:Microbiologyperméabilité membranairechemistry.chemical_compound[SDV.IDA]Life Sciences [q-bio]/Food engineeringFood sciencedryingOriginal Researchpropidium iodidebiologyChemistryMicrobiology and Parasitologyplasma-membraneSalmonella entericainfant formulaMicrobiologie et ParasitologieSalmonella entericaAlimentation et Nutritionsaccharomyces-cerevisiaeenterobacter-sakazakiitraitement thermiqueséchageMicrobiology (medical)Water activityMembrane permeabilitydesiccation tolerance030106 microbiologylow-water activityMicrobiologyrespiratory activity03 medical and health sciencesCronobacter sakazakiimedicineFood and NutritionPropidium iodideactivation respiratoireEscherichia colifoodborne pathogensheat treatmentbiology.organism_classificationCronobacter sakazakii030104 developmental biologymembrane permeabilitythermal inactivationSalmonella enterica;Cronobacter sakazakii;membrane permeability;respiratory activity;heat treatment;dryingescherichia-coliBacteria
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Increased RNA virus population diversity improves adaptability

2021

The replication machinery of most RNA viruses lacks proofreading mechanisms. As a result, RNA virus populations harbor a large amount of genetic diversity that confers them the ability to rapidly adapt to changes in their environment. In this work, we investigate whether further increasing the initial population diversity of a model RNA virus can improve adaptation to a single selection pressure, thermal inactivation. For this, we experimentally increased the diversity of coxsackievirus B3 (CVB3) populations across the capsid region. We then compared the ability of these high diversity CVB3 populations to achieve resistance to thermal inactivation relative to standard CVB3 populations in an…

0301 basic medicineSciencevirusesThermal StabilityBiologyMicrobiologíaArticleCell Line03 medical and health sciencesCapsidVirologyHumansRNA VirusesExperimental EvolutionGeneticsGenetic diversityExperimental evolutionMultidisciplinary030102 biochemistry & molecular biologyQRComputational BiologyGenetic VariationRNARNA virusBiodiversityDirected evolutionbiology.organism_classificationDeep Mutational ScanningBiological Evolution030104 developmental biologyAmino Acid SubstitutionExperimental evolutionCapsidMutationEpistasisMedicineCapsid ProteinsAdaptationhuman activities
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2020

Worldwide, tons of lignin is produced annually in pulping plants and it is mainly considered as a waste material. Usually lignin is burned to produce energy for the pulping reactors. The production of value-added materials from renewable materials like lignin, has proved to be challenging. In this study, the effects of addition of three different types of lignin in the production of tannin/furanic foams is investigated. The foams were matured, first at 373 K and finally carbonized at 1073 K and the properties of them including mechanical strength, specific surface area and pore development are investigated before and after thermal treatment. According to the results, higher mechanical stren…

0301 basic medicineSolid-state chemistryMultidisciplinaryMaterials scienceCarbonizationCatalyst supportThermal treatmentCatalysis03 medical and health scienceschemistry.chemical_compound030104 developmental biology0302 clinical medicineAdsorptionChemical engineeringchemistrySpecific surface areaLignin030217 neurology & neurosurgeryHeliyon
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Characterization of Hydrothermal Processing Influence on Strontium Substituted Apatite by Investigating Stable Oxygen Isotope Ratio and Antibacterial…

2018

Synthetic hydroxyapatite (HAp) has weak antibacterial and mechanical properties. The antibacterial activity of HAp can be enhanced by strontium cation substitution and incorporation of peroxide ion via hydrothermal processing at 100 °C and 150 °C temperature using 50% H2O2 solution. The starting reagents and products of HAp processing were analyzed by thermal conversion elemental analyser – isotopic ratio mass spectrometer in order to determine the δ18O values. Using different host materials it could be possible to determine differences of δ18O values between untreated and hydrothermally treated HAp samples. The enhanced antibacterial properties of processed HAp samples were investigated us…

0301 basic medicineStrontiumMechanical Engineeringchemistry.chemical_elementOxygen isotope ratio cycleApatiteHydrothermal circulationCharacterization (materials science)03 medical and health scienceschemistry.chemical_compound030104 developmental biologychemistryMechanics of Materialsvisual_artvisual_art.visual_art_mediumGeneral Materials ScienceHydrogen peroxideAntibacterial activityNuclear chemistryKey Engineering Materials
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Additives for vaccine storage to improve thermal stability of adenoviruses from hours to months

2016

Up to 80% of the cost of vaccination programmes is due to the cold chain problem (that is, keeping vaccines cold). Inexpensive, biocompatible additives to slow down the degradation of virus particles would address the problem. Here we propose and characterize additives that, already at very low concentrations, improve the storage time of adenovirus type 5. Anionic gold nanoparticles (10−8–10−6 M) or polyethylene glycol (PEG, molecular weight ∼8,000 Da, 10−7–10−4 M) increase the half-life of a green fluorescent protein expressing adenovirus from ∼48 h to 21 days at 37 °C (from 7 to >30 days at room temperature). They replicate the known stabilizing effect of sucrose, but at several orders of…

0301 basic medicineSucroseSucroseTime FactorsvirusesGeneral Physics and AstronomyMetal Nanoparticles02 engineering and technologyvaccinationsvaccine storagePolyethylene Glycolschemistry.chemical_compoundMiceImmunogenicity VaccineDrug StabilityModelsAdenovirus Vaccinesvaccineta318ta317MultidisciplinaryChemistryImmunogenicityadenoviruksetQadenovirus021001 nanoscience & nanotechnologyImmunogenicityOrders of magnitude (mass)Cold Temperaturevaccine; adenovirus; additives; nanoparticlesInfectious DiseasesColloidal goldModels Animaladditives0210 nano-technologyInfectionBiotechnologyHalf-LifeScienceDrug StorageBioengineeringPolyethylene glycolModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyArticleVaccine RelatedExcipients03 medical and health sciencesPEG ratioAnimalsThermal stabilityChromatographyAnimalPreventionRational designta1182General ChemistryBiologicalVirology030104 developmental biologyadenovirusesFeasibility StudiesImmunizationnanoparticlesGoldVaccine
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Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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Biopreservation of Myoglobin in Crowded Environment: A Comparison between Gelatin and Trehalose Matrixes.

2017

Biopreservation by sugar and/or polymeric matrixes is a thoroughly studied research topic with wide technological relevance. Ternary amorphous systems containing both saccharides and proteins are extensively exploited to model the in vivo biopreservation process. With the aim of disentangling the effect of saccharides and polypeptidic crowders (such as gelatin) on the preservation of a model protein, we present here a combined differential scanning calorimetry and UV-vis spectrophotometry study on samples of myoglobin embedded in amorphous gelatin and trehalose + gelatin matrixes at different hydrations, and compare them with amorphous myoglobin-only and myoglobin-Trehalose samples. The res…

0301 basic medicinefood.ingredientSwine010402 general chemistry01 natural sciencesGelatin03 medical and health scienceschemistry.chemical_compoundDifferential scanning calorimetryfoodSpectrophotometryMaterials ChemistrymedicineAnimalsThermal stabilityHorsesPhysical and Theoretical ChemistryGelatine trehalose calorimetry collagen myoglobinmedicine.diagnostic_testCalorimetry Differential ScanningMyoglobinTrehaloseBiopreservationTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesSurfaces Coatings and FilmsAmorphous solid030104 developmental biologychemistryChemical engineeringMyoglobinBiochemistryGelatinSpectrophotometry UltravioletThe journal of physical chemistry. B
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Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2

2016

We show that a peptide from Chikungunya virus nsP3 protein spanning residues 1728–1744 binds the amphiphysin-2 (BIN1) Src homology-3 (SH3) domain with an unusually high affinity (Kd 24 nM). Our NMR solution complex structure together with isothermal titration calorimetry data on several related viral and cellular peptide ligands reveal that this exceptional affinity originates from interactions between multiple basic residues in the target peptide and the extensive negatively charged binding surface of amphiphysin-2 SH3. Remarkably, these arginines show no fixed conformation in the complex structure, indicating that a transient or fluctuating polyelectrostatic interaction accounts for this …

0301 basic medicinenuclear magnetic resonance (NMR)Amino Acid MotifsStatic ElectricityPeptideTarget peptidePlasma protein bindingViral Nonstructural ProteinsBiologyhost-pathogen interactionBiochemistrySH3 domainsrc Homology Domainsamphiphysin SH3Structure-Activity Relationship03 medical and health sciencesProtein structuredynaminHumansShort linear motifprotein structureNuclear Magnetic Resonance BiomolecularMolecular BiologySrc homology 3 domain (SH3 domain)Adaptor Proteins Signal Transducingchemistry.chemical_classificationTumor Suppressor Proteinsta1182Nuclear ProteinsIsothermal titration calorimetryCell Biologyintrinsically disordered protein030104 developmental biologychemistryBiochemistrynsP3Protein Structure and FoldingAmphiphysinBiophysicsPeptidesChikungunya virusProtein BindingJournal of Biological Chemistry
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