Search results for "Bacteriolysis"

showing 7 items of 7 documents

Release of macromolecules by Saccharomyces cerevisiae during ageing of French flor sherry wine “Vin jaune”

2003

The French flor sherry wine "Vin jaune" spends 6 years and 3 months in the same barrel under a yeast velum. Because of temperature variations in the cellars, this velum sinks partially into the wine and a deposit of dead yeasts cells accumulates in the bottom of the barrels, favouring the formation of new velum. Growth and autolysis occur simultaneously. This study investigated the evolution of macromolecules released by yeasts during the ageing of "Vin jaune" in a model system closely simulating winemaking. It was observed that the release of macromolecules during the formation of the velums by living yeasts was low but greatly increased when the velums fell and yeast viability decreased. …

Time FactorsFood HandlingAutolysis (wine)Saccharomyces cerevisiaeFlorMannoseWineSaccharomyces cerevisiaeBiologyModels BiologicalMicrobiologychemistry.chemical_compoundBacteriolysisBiomassParticle SizeWinemakingWineProteinsGeneral Medicinebiology.organism_classificationYeastBiochemistrychemistryFermentationFood MicrobiologyCarbohydrate MetabolismFermentationFood ScienceInternational Journal of Food Microbiology
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Delayed lysis confers resistance to the nucleoside analogue 5-fluorouracil and alleviates mutation accumulation in the single-stranded DNA bacterioph…

2014

ABSTRACT Rates of spontaneous mutation determine viral fitness and adaptability. In RNA viruses, treatment with mutagenic nucleoside analogues selects for polymerase variants with increased fidelity, showing that viral mutation rates can be adjusted in response to imposed selective pressures. However, this type of resistance is not possible in viruses that do not encode their own polymerases, such as single-stranded DNA viruses. We previously showed that serial passaging of bacteriophage ϕX174 in the presence of the nucleoside analogue 5-fluorouracil (5-FU) favored substitutions in the lysis protein E (P. Domingo-Calap, M. Pereira-Gomez, and R. Sanjuán, J. Virol. 86: 9640–9646, 2012, doi:10…

Mutation rateImmunologyAdaptation BiologicalMutation MissenseDNA Single-Strandedmedicine.disease_causeMicrobiologyBacteriophage03 medical and health scienceschemistry.chemical_compoundViral ProteinsBacteriolysisMutation RateVirologymedicineBacteriophagesSelection GeneticPolymerase030304 developmental biologyGenetics0303 health sciencesMutationbiology030302 biochemistry & molecular biologyMutagenesisMutation AccumulationResistance mutationbiology.organism_classificationVirologychemistryGenetic Diversity and EvolutionInsect ScienceDNA Viralbiology.proteinMutant ProteinsFluorouracilDNAJournal of virology
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Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties.

1998

A gene encoding a novel cell wall-associated protein of Staphylococcus saprophyticus that binds fibronectin and to sheep erythrocytes has been cloned and sequenced. The 4392 bp open reading frame codes for an amino acid sequence that is quite similar to the Atl, an autolysin, of Staphylococcus aureus and to the AtlE of S. epidermidis. The two regions of most pronounced homology code for an N-acetyl-muramyl-L-alanine amidase and for an endo-beta-N-acetyl-D-glucosaminidase. The cloned protein lysed cells of S. saprophyticus and Micrococcus luteus exogenously. Subcloning localized the enzymatic activities to the regions of high homology and demonstrated that the interposed sequence is responsi…

DNA BacterialStaphylococcusMolecular Sequence DataBiologyMicrobiologyHomology (biology)BacteriolysisAmino Acid SequenceCloning MolecularAdhesins BacterialMolecular BiologyGenePeptide sequenceAllelesStaphylococcus saprophyticusBinding SitesBase SequenceAutolysinSequence Analysis DNAbiology.organism_classificationMolecular biologyFibronectinsBacterial adhesinOpen reading frameSubcloningHemagglutininsBiochemistryGenes BacterialMolecular microbiology
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Isolation and Characterization of Two Klebsiella pneumoniae Phages Encoding Divergent Depolymerases

2020

The emergence of multidrug-resistant bacteria is a major global health concern. The search for new therapies has brought bacteriophages into the spotlight, and new phages are being described as possible therapeutic agents. Among the bacteria that are most extensively resistant to current antibiotics is Klebsiella pneumoniae, whose hypervariable extracellular capsule makes treatment particularly difficult. Here, we describe two new K. pneumoniae phages, &pi

Models Molecular0301 basic medicineKlebsiellaPhage therapyKlebsiella pneumoniae<i>Klebsiella pneumoniae</i>virusesmedicine.medical_treatmentAntibioticsMolecular Conformationlcsh:ChemistryBacteriophagebacteriophagewide infection rangeBacteriophagesAntigens Virallcsh:QH301-705.5PhylogenySpectroscopybiologyGeneral Medicine3. Good healthComputer Science ApplicationsKlebsiella pneumoniaePhenotypephage therapyPhage therapymedicine.drug_class030106 microbiologyGenome ViralArticleHost SpecificityCatalysisMicrobiologyInorganic ChemistryViral Proteins03 medical and health sciencesPodoviridaeBacteriolysismedicineAmino Acid SequencePhysical and Theoretical ChemistryBacteriophageMolecular BiologyTropismWhole Genome SequencingOrganic ChemistryComputational BiologyGenetic VariationMolecular Sequence Annotationbiology.organism_classificationKlebsiella Infections030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Wide infection rangeBacteriaInternational Journal of Molecular Sciences
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Molecular Characterization of a Variant of Bacillus anthracis-Specific Phage AP50 with Improved Bacteriolytic Activity▿ †

2008

ABSTRACT The genome sequence of a Bacillus anthracis -specific clear plaque mutant phage, AP50c, contains 31 open reading frames spanning 14,398 bp, has two mutations compared to wild-type AP50t, and has a colinear genome architecture highly similar to that of gram-positive Tectiviridae phages. Spontaneous AP50c-resistant B. anthracis mutants exhibit a mucoid colony phenotype.

virusesMutantMolecular Sequence DataMutation MissenseGenetics and Molecular BiologyBacillus PhagesGenome ViralViral Plaque AssayApplied Microbiology and BiotechnologySyntenyBacteriophageBacteriolysisGene OrderPoint MutationBacillus (shape)Whole genome sequencingGeneticsEcologybiologyBase SequenceTectivirusVirionSequence Analysis DNAbiology.organism_classificationBacillus anthracisOpen reading frameBacillus anthracisDNA ViralTectiviridaeFood ScienceBiotechnologyTectiviridae
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Phage-borne factors and host LexA regulate the lytic switch in phage GIL01.

2011

ABSTRACT The Bacillus thuringiensis temperate phage GIL01 does not integrate into the host chromosome but exists stably as an independent linear replicon within the cell. Similar to that of the lambdoid prophages, the lytic cycle of GIL01 is induced as part of the cellular SOS response to DNA damage. However, no CI-like maintenance repressor has been detected in the phage genome, suggesting that GIL01 uses a novel mechanism to maintain lysogeny. To gain insights into the GIL01 regulatory circuit, we isolated and characterized a set of 17 clear plaque ( cp ) mutants that are unable to lysogenize. Two phage-encoded proteins, gp1 and gp7, are required for stable lysogen formation. Analysis of …

Gene Expression Regulation ViralvirusesBacteriophages Transposons and PlasmidsBacillus thuringiensisBacillus PhagesBiologyMicrobiologyHost-Parasite InteractionsBacteriolysisLysogenBacterial ProteinsLysogenic cycleHost chromosomeSOS responseSOS Response GeneticsMolecular BiologyLysogenyGeneticsBinding SitesSerine Endopeptidasesbiochemical phenomena metabolism and nutritionBacillus PhageTemperatenessLytic cycleDNA ViralbacteriaVirus ActivationRepressor lexAProtein BindingJournal of bacteriology
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Molecular characterisation, evolution and expression analysis of g-type lysozymes in Ciona intestinalis

2017

Lysozyme is an important defense molecule of the innate immune system. Known for its bactericidal properties, lysozyme catalyzes the hydrolysis of b-(1,4)-glycosidic bonds between the N-acetyl glucosamine and N-acetyl muramic acid in the peptidoglycan layer of bacterial cell walls. In this study, the complete coding sequence of four g-type lysozymes were identified in Ciona intestinalis. Phylogenetic analysis and modelling supported the hypothesis of a close relationship with the vertebrate g-type lysozymes suggesting that the C. intestinalis g-type lysozyme genes (CiLys-g1, Cilys-g2, CiLys-g3, CiLys-g4) share a common ancestor in the chordate lineage. Protein motif searches indicated that …

0301 basic medicineLipopolysaccharidesImmunologySettore BIO/05 - ZoologiaChordateBacterial cell structureMicrobiologyEvolution Molecular03 medical and health scienceschemistry.chemical_compound0302 clinical medicineBacteriolysisGeeseAnimalsCiona intestinalisCloning MolecularStructural motifGeneCells CulturedPhylogenyInnate immune systembiologyBacterial Infectionsbiology.organism_classificationBiological EvolutionImmunity InnateCiona intestinalisAscidian Lysozymes g-type Inflammation LPS Ciona intestinalis030104 developmental biologyBiochemistrychemistry030220 oncology & carcinogenesisPharynxMuramidasePeptidoglycanLysozymeTranscriptomeDevelopmental Biology
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