0000000000398057

AUTHOR

Ml Milat

showing 5 related works from this author

Modulation of the Biological Activity of a Tobacco LTP1 by Lipid Complexation

2004

Plant lipid transfer proteins (LTPs) are small, cysteine-rich proteins secreted into the extracellular space. They belong to the pathogenesis-related proteins (PR-14) family and are believed to be involved in several physiological processes including plant disease resistance, although their precise biological function is still unknown. Here, we show that a recombinant tobacco LTP1 is able to load fatty acids and jasmonic acid. This LTP1 binds to specific plasma membrane sites, previously characterized as elicitin receptors, and is shown to be involved in the activation of plant defense. The biological properties of this LTP1 were compared with those of LTP1-linolenic and LTP1-jasmonic acid…

Phytophthora0106 biological sciences[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringCyclopentanesPlasma protein bindingBiologyFatty Acid-Binding ProteinsLigands01 natural sciencesMass SpectrometryFatty acid-binding proteinCell membrane03 medical and health scienceschemistry.chemical_compoundTobacco[SDV.IDA]Life Sciences [q-bio]/Food engineeringExtracellularmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringOxylipinsMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesDose-Response Relationship DrugCircular DichroismJasmonic acidCell MembraneFatty AcidsElicitinBiological activityArticlesCell Biology[SDV.IDA] Life Sciences [q-bio]/Food engineeringLipid MetabolismLipidsRecombinant Proteinsmedicine.anatomical_structureBiochemistrychemistryPHYTOPHTORA PARASITICACarrier ProteinsTRANSFERT LIPIDIQUEPlant lipid transfer proteinsChromatography LiquidProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Cercospora beticola toxins. IX. Relationship between structure of beticolins, inhibition of plasma membrane H+ -ATPase and partition in lipid membran…

1996

Beticolins are yellow toxins produced by the fungus Cercospora beticola. The effect of one of them, beticolin-1, has been investigated on corn root plasma membrane H + -ATPase (EC 3.6.1.35) at different purification levels (plasma membrane fraction. partially, or highly purified enzyme). The results obtained demonstrated that (1) the purified proton pump was inhibited directly by low amounts of the toxin (I 50 =1.62 ± 0.18 μM), (2) the biological effects of beticolin-1 were similar to those of CBT (Cercospora beticola toxin). Furthermore, it was established that the efficiency of the different beticolins was clearly related to their ability to interact with the lipid bilayers, determined by…

0106 biological sciencesSTRUCTUREPhysiologyATPasePlant Science010402 general chemistrymedicine.disease_cause01 natural sciencesProton transportGeneticsmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyLipid bilayerComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationLiposomeChromatographybiologyChemistryToxinCell BiologyGeneral MedicineCercospora beticolabiology.organism_classification0104 chemical sciencesMembraneEnzymeBiochemistrybiology.protein010606 plant biology & botany
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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Are elicitins cryptograms in plant-oomycete communications?

1999

Stimulation of plant natural defenses is an important challenge in phytoprotection prospects. In that context, elicitins, which are small proteins secreted by Phytophthora and Pythium species, have been shown to induce a hypersensitive-like reaction in tobacco plants. Moreover, these plants become resistant to their pathogens, and thus this interaction constitutes an excellent model to investigate the signaling pathways leading to plant resistance. However, most plants are not reactive to elicitins, although they possess the functional signaling pathways involved in tobacco responses to elicitin. The understanding of factors involved in this reactivity is needed to develop agronomic applica…

Phytophthora0106 biological sciences[SDV]Life Sciences [q-bio]Molecular Sequence DataMutagenesis (molecular biology technique)Context (language use)01 natural sciencesHost-Parasite InteractionsEvolution MolecularFungal Proteins03 medical and health sciencesCellular and Molecular NeuroscienceErgosterolGene Expression Regulation FungalTobaccoPlant defense against herbivoryAmino Acid SequenceMolecular BiologyPhylogenyComputingMilieux_MISCELLANEOUSPlant Diseases030304 developmental biologyPharmacologyOomycete0303 health sciencesBase SequencebiologyAlgal Proteinsfungifood and beveragesElicitinCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]Plants ToxicOomycetesBiochemistryMolecular MedicinePhytophthoraSequence AlignmentPlant lipid transfer proteinsFunction (biology)BiotechnologySignal Transduction010606 plant biology & botany
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Listeria phage and phage tail induction triggered by components of bacterial-growth media (phosphate, LiCl, nalidixic acid and acriflavine)

2015

ABSTRACT The detection of Listeria monocytogenes from food is currently carried out using a double enrichment. For the ISO methodology, this double enrichment is performed using half-Fraser and Fraser broths, in which the overgrowth of L. innocua can occur in samples where both species are present. In this study, we analyzed the induction of phages and phage tails of Listeria spp. in these media and in two brain heart infusion (BHI) broths (BHIM [bioMérieux] and BHIK [Biokar]) to identify putative effectors. It appears that Na 2 HPO 4 at concentrations ranging from 1 to 40 g/liter with an initial pH of 7.5 can induce phage or phage tail production of Listeria spp., especially with 10 g/lite…

Nalidixic acidListeriaviruses[SDV]Life Sciences [q-bio]Bacterial growthmedicine.disease_causeApplied Microbiology and BiotechnologyacriflavineMicrobiologyPhosphateschemistry.chemical_compoundListeria sppListeria monocytogenesmedicinephage[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyBacteriophagesLiClinductionphosphate2. Zero hungerEcologybiologynalidixic acidViral Tail ProteinsViral Tail Proteinsbiology.organism_classificationPhosphateCulture Mediachemistry[SDE]Environmental SciencesListeriaBrain heart infusionFood MicrobiologyAcriflavineVirus ActivationLithium ChlorideFood ScienceBiotechnologymedicine.drug
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