Search results for "lipodepsipeptides"

showing 3 items of 3 documents

Pseudomonas corrugata crpCDE is part of the cyclic lipopeptide corpeptin biosynthetic gene cluster and is involved in bacterial virulence in tomato a…

2014

Summary: Pseudomonas corrugataCFBP 5454 produces two kinds of cyclic lipopeptides (CLPs), cormycin A and corpeptins, both of which possess surfactant, antimicrobial and phytotoxic activities. In this study, we identified genes coding for a putative non-ribosomal peptide synthetase and an ABC-type transport system involved in corpeptin production. These genes belong to the same transcriptional unit, designated crpCDE. The genetic organization of this locus is highly similar to other PseudomonasCLP biosynthetic clusters. Matrix-assisted laser desorption ionization-time of flight-mass spectrometry (MALDI-TOF-MS) analysis revealed that transporter and synthetase genomic knock-out mutants were u…

DNA BacteriallipodepsipeptidesABC transporters corpeptins Lux R transcriptional regulators non-ribosomal peptide synthetase Pseudomonas.chromobacterium-violaceumcloningPeptides CyclicLipopeptidesSolanum lycopersicumPseudomonasABC transporters Lux R transcriptional regulators non-ribosomal peptide synthetaseTobaccoPeptide SynthasesLux R transcriptional regulatorsnon-ribosomal peptide synthetasePhylogenyVLAGPlant DiseasesCell-Free SystemVirulenceputisolvin-iisyringae pv.-syringaeSettore AGR/12 - Patologia VegetaleOriginal Articlesgram-negative bacteriapeptideBiosynthetic PathwayssyringomycinRepressor ProteinssyringopeptinFood Quality and DesignABC transportersGenesGenes BacterialMultigene FamilyHost-Pathogen InteractionsMutationTrans-ActivatorsATP-Binding Cassette Transportersquorum-sensing system
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N-acyl-homoserine-lactone quorum sensing in tomato phytopathogenic Pseudomonas spp. is involved in the regulation of lipodepsipeptide production

2012

Pseudomonas corrugata and Pseudomonas mediterranea are two closely related phytopathogenic bacteria both causal agents of tomato pith necrosis. P. corrugata produces phytotoxic and antimicrobial cationic lipodepsipeptides (LDPs) which are thought to act as major virulence factors. Previous studies have demonstrated that P. corrugata CFBP 5454 has an N-acyl homoserine lactone (AHL) quorum sensing (QS) system PcoI/PcoR and that LDP production occurs at high population densities. No molecular studies on virulence have thus far been reported for P. mediterranea. In this study, we show that P. mediterranea also produces LDPs as well as possessing an AHL-dependent QS system, designated PmeI/PmeR,…

Pseudomonas mediterraneaVirulence FactorsLipoproteinsPlant DiseaseHomoserineVirulenceBioengineeringBiologyAcyl-ButyrolactonesPseudomonaAcyl-ButyrolactoneApplied Microbiology and BiotechnologyTomatoMicrobiologychemistry.chemical_compoundSolanum lycopersicumVirulence FactorDepsipeptidesPseudomonasLycopersicon esculentumLipoproteinPromoter Regions GeneticDepsipeptidePlant DiseasesAntimicrobial Cationic PeptideVirulencePseudomonasGeneral MedicineLipodepsipeptidesbiology.organism_classificationPseudomonas corrugataQuorum sensingPseudomonas corrugataQuorum sensingN-Acyl homoserine lactonePhenotypechemistryPseudomonas mediterranea; Pseudomonas corrugata; Quorum sensing; Lipodepsipeptides; Virulence; TomatoMutationLipodepsipeptidePseudomonas mediterraneaBacteriaBiotechnologyAntimicrobial Cationic PeptidesJournal of Biotechnology
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Lipodepsipeptides from Pseudomonas syringae are partially proteolyzed and are not absorbed by humans: An in vitro study

2008

There are some concerns about the use of Pseudomonas-based products as biocontrol agents because of the hemolytic activity shown by their metabolites. The effects of Pseudomonas lipodepsipeptides (LDPs) on mammals via ingestion and the LDP degradation during the digestion and intestinal permeability have not been evaluated. In this research, the susceptibility of different LDPs to degradation was assayed with enzymatic gastrointestinal digestion, and intestinal permeability to LDPs was investigated in an in vitro system based on an intestinal cell layer system. Results demonstrated that trypsin and chymotrypsin hydrolyze up to 50% of the various LDPs, and that proteolysis was further increa…

lipodepsipeptidesProteolysisPseudomonas syringaelipodepsipeptides; Pseudomonas syringae; enzymatic digestionPronaseIn Vitro TechniquesPeptides CyclicRisk AssessmentMicrobiologyMicrobiologyenzymatic digestionmedicinePseudomonas syringaeHumansLife SciencePest Control BiologicalIntestinal permeabilitybiologymedicine.diagnostic_testPseudomonasbiology.organism_classificationTrypsinmedicine.diseaseIntestinal AbsorptionBiochemistryConsumer Product SafetyDigestionDigestionFood Sciencemedicine.drugPseudomonadaceaeJournal of Food Protection
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