Search results for "ANTIMICROBIAL PEPTIDES"

showing 10 items of 76 documents

Stress and immune response to bacterial LPS in the sea urchin Paracentrotus lividus (Lamarck, 1816).

2018

The immune system of the sea urchin species Paracentrotus lividus is highly complex and, as yet, poorly understood. P. lividus coelomocytes mediate immune response through phagocytosis and encapsulation of non-self particles, in addition to the production of antimicrobial molecules. Despite this understanding, details of exactly how these processes occur and the mechanisms which drive them are still in need of clarification. In this study, we show how the bacterial lipopolysaccharides (LPS) is able to induce a stress response which increases the levels of the heat shock proteins HSP70 and HSP90 only a few hours after treatment. This study also shows that LPS treatment increases the expressi…

0301 basic medicineLipopolysaccharidesPhagocytosisAntimicrobial peptidesAquatic ScienceParacentrotus lividusAntimicrobical peptide03 medical and health sciencesImmune systemStress PhysiologicalHeat shock proteinbiology.animalEnvironmental ChemistryHSP90AnimalsSea urchinHSP70Heat-Shock ProteinsbiologyEchinoderm04 agricultural and veterinary sciencesGeneral Medicinebiology.organism_classificationHsp90Immunity InnateHsp70Cell biologyThymosin030104 developmental biologyImmune System040102 fisheriesbiology.proteinParacentrotus0401 agriculture forestry and fisheriesCoelomocyteParacentrotus lividuFishshellfish immunology
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Identification of New Antimicrobial Peptides from Mediterranean Medical Plant Charybdis pancration (Steinh.) Speta

2020

The present work was designed to identify and characterize novel antimicrobial peptides (AMPs) from Charybdis pancration (Steinh.) Speta, previously named Urginea maritima, is a Mediterranean plant, well-known for its biological properties in traditional medicine. Polypeptide-enriched extracts from different parts of the plant (roots, leaves and bulb), never studied before, were tested against two relevant pathogens, Staphylococcus aureus and Pseudomonas aeruginosa. With the aim of identifying novel natural AMPs, peptide fraction displaying antimicrobial activity (the bulb) that showed minimum inhibitory concentration (MICs) equal to 30 &micro

0301 basic medicineMicrobiology (medical)Charybdis030106 microbiologyAntimicrobial peptides) SpetaSettore BIO/05 - ZoologiatemporinPeptidemedicine.disease_causeSettore BIO/19 - Microbiologia GeneraleBiochemistryMicrobiologyMicrobiologyantibiotic resistant strains03 medical and health sciencesMinimum inhibitory concentrationAntibiotic resistancemedicinePharmacology (medical)high-resolution mass spectrometryGeneral Pharmacology Toxicology and Pharmaceuticsplant defensinschemistry.chemical_classificationbiologyPseudomonas aeruginosaantimicrobial peptides from plantCharybdis pancration (Steinh.) SpetaSettore BIO/02 - Botanica Sistematicalcsh:RM1-950temporinsbiology.organism_classificationAntimicrobialplant defensinmolecular dynamicslcsh:Therapeutics. Pharmacology030104 developmental biologyInfectious DiseaseschemistryStaphylococcus aureusCharybdis pancration (Steinhantimicrobial peptides from plants<i>Charybdis pancration</i> (Steinh.) Spetaantibiotic resistant strainAntibiotics
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The LuxR Regulators PcoR and RfiA Co-regulate Antimicrobial Peptide and Alginate Production in Pseudomonas corrugata

2018

Cyclic lipopeptides (CLPs) are considered as some of the most important secondary metabolites in different plant-associated bacteria, thanks to their antimicrobial, cytotoxic, and surfactant properties. In this study, our aim was to investigate the role of the Quorum Sensing (QS) system, PcoI/PcoR, and the LuxR-type transcriptional regulator RfiA in CLP production in the phytopatogenic bacterium, Pseudomonas corrugata based on our previous work where we reported that the pcoR and rfiA mutants were devoid of the CLPs cormycin and corpeptin production. Due to the close genetic link between the QS system and the RfiA (rfiA is co-transcribed with pcoI), it was difficult to ascertain the specifi…

0301 basic medicineMicrobiology (medical)transcriptional analysiscyclic lipopeptides RNA-seq non-ribosomal peptides transcriptional analysis exopolysaccarides030106 microbiologyAntimicrobial peptidesMutantexopolysaccarideslcsh:QR1-502exopolysaccarideMicrobiologylcsh:Microbiology03 medical and health sciencescyclic lipopeptideGene expressionnon-ribosomal peptideTranscriptional regulationGenebiologyChemistrySettore AGR/12 - Patologia Vegetalebiology.organism_classificationQuorum sensingPseudomonas corrugatacyclic lipopeptidesRegulonBiochemistrynon-ribosomal peptidesRNA-seqFrontiers in Microbiology
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Antimicrobial and Antibiofilm Activity of a Recombinant Fragment of β-Thymosin of Sea Urchin Paracentrotus lividus

2018

With the aim to obtain new antimicrobials against important pathogens such as Staphylococcus aureus and Pseudomonas aeruginosa, we focused on antimicrobial peptides (AMPs) from Echinoderms. An example of such peptides is Paracentrin 1 (SP1), a chemically synthesised peptide fragment of a sea urchin thymosin. In the present paper, we report on the biological activity of a Paracentrin 1 derivative obtained by recombination. The recombinant paracentrin RP1, in comparison to the synthetic SP1, is 22 amino acids longer and it was considerably more active against the planktonic forms of S. aureus ATCC 25923 and P. aeruginosa ATCC 15442 at concentrations of 50 &micro

0301 basic medicineSettore BIO/05 - ZoologiaPharmaceutical Science<i>Staphylococcus aureus</i>Peptide<i>Paracentrotus lividus</i>Settore BIO/19 - Microbiologia Generalemedicine.disease_causebiofilmDrug DiscoveryPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5chemistry.chemical_classificationbiologyMicrobial Sensitivity TestChemistrymolecular dynamicBiological activityRecombinant ProteinAntimicrobialRecombinant ProteinsAnti-Bacterial AgentsBiochemistrySettore CHIM/03 - Chimica Generale E InorganicaStaphylococcus aureusPeptidePseudomonas aeruginosaStaphylococcus aureuParacentrotusAntibacterial activityAMP (antimicrobial peptides)Staphylococcus aureusSea UrchinAntimicrobial peptidesMicrobial Sensitivity TestsParacentrotus lividusArticle03 medical and health sciencesAnti-Bacterial AgentmedicineAnimalsAMP (antimicrobial peptides); Paracentrotus lividus; Pseudomonas aeruginosa; Staphylococcus aureus; biofilm; molecular dynamics; thymosinAnimalBiofilmthymosinbiology.organism_classificationmolecular dynamics<i>Pseudomonas aeruginosa</i>030104 developmental biologylcsh:Biology (General)Paracentrotus lividusBiofilmsSea UrchinsParacentrotuPeptidesParacentrotus lividuMarine Drugs
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Food quality affects the expression of antimicrobial peptide genes upon simulated parasite attack in the larvae of greater wax moth

2017

Predator‐prey interactions are an important evolutionary force affecting the immunity of the prey. Parasitoids and mites pierce the cuticle of their prey, which respond by activating their immune system against predatory attacks. Immunity is a costly function for the organism, as it often competes with other life‐history traits for limited nutrients. We tested whether the expression of antimicrobial peptides (AMP) of the larvae of the greater wax moth Galleria mellonella (L.) (Lepidoptera: Pyralidae) changes as a consequence of insertion of a nylon monofilament, which acts like a synthetic parasite. The treatment was done for larvae grown on a high‐quality vs. a low‐quality diet. The expres…

0301 basic medicineanimal structuresInnate immune systembiologyCuticlefungiAntimicrobial peptidesZoologybiochemical phenomena metabolism and nutritionbiology.organism_classificationPredationLepidoptera genitaliaGalleria mellonella03 medical and health sciences030104 developmental biologyInsect ScienceParasite hostingta1181Ecology Evolution Behavior and SystematicsPyralidaeEntomologia Experimentalis et Applicata
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Annelid Coelomic Fluid Proteins

2020

The coelomic cavity is part of the main body plan of annelids. This fluid filled space takes up a considerable volume of the body and serves as an important site of exchange of both metabolites and proteins. In addition to low molecular substances such as amino acids and glucose and lactate, the coelomic fluid contains different proteins that can arise through release from adjacent tissues (intestine) or from secretion by coelomic cells. In this chapter, we will review the current knowledge about the proteins in the annelid coelomic fluid. Given the number of more than 20,000 extant annelid species, existing studies are confined to a relatively few species. Most studies on the oligochaetes …

0301 basic medicinechemistry.chemical_classificationSipunculaEchiuraAnnelid030102 biochemistry & molecular biologybiologyAntimicrobial peptidesbiology.organism_classificationAmino acid03 medical and health sciencesVitellogenin030104 developmental biologychemistryBiochemistrybiology.proteinCoelomVitellogenesis
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Antimicrobial peptide–metal ion interactions – a potential way of activity enhancement

2018

Increasing bacterial and fungal drug resistance requires novel, effective antimicrobial treatments to be actively sought. Because of a general lack of resistance towards antimicrobial peptides (AMPs), they are being relied on as a novel class of therapeutics aiming to conquer drug-resistant bacteria and fungi. There are numerous ways in which AMPs might interact with pathogens, such as membrane disruption, production of ROS, inhibition of cell wall, nucleic acid and protein synthesis or by the withdrawal of essential metal ions. Biologically indispensable metal ions have a dual effect on the activity of antimicrobial peptides: (i) AMPs bind them, so that microbes cannot get enough metals es…

0301 basic medicinechemistry.chemical_classificationbiologyChemistryMetal ions in aqueous solutionAntimicrobial peptidesPeptideGeneral ChemistryDrug resistanceAntimicrobialbiology.organism_classificationCatalysis03 medical and health sciences030104 developmental biologyBiochemistryMaterials ChemistryNucleic acidMode of actionBacteriaNew Journal of Chemistry
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Hidden complexity in membrane permeabilization behavior of antimicrobial polycations.

2021

A promising alternative to classical antibiotics are antimicrobial peptides and their synthetic mimics (smAMPs) that supposedly act directly on membranes. For a more successful design of smAMPs, we need to know how the type of interaction with the membrane determines the type of membrane perturbation. How this, in turn, transfers into selectivity and microbial killing activity is largely unknown. Here, we characterize the action of two smAMPs: MM:CO (a copolymer of hydrophobic cyclooctyl subunits and charged β-monomethyl-α-aminomethyl subunits) and the highly charged poly-NM (a homopolymer of α-aminomethyl subunits). By thorough characterization of vesicle leakage experiments, we elucidate …

0303 health sciencesMembrane permeabilizationChemistryVesicleKineticsAntimicrobial peptidesStatic ElectricityGeneral Physics and Astronomy010402 general chemistryAntimicrobialFluoresceins01 natural sciencesPermeability0104 chemical sciences03 medical and health sciencesMembraneGlycerophosphatesBiophysicsPhysical and Theoretical ChemistryHydrophobic and Hydrophilic InteractionsUnilamellar Liposomes030304 developmental biologyLeakage (electronics)Antimicrobial Cationic PeptidesProtein BindingPhysical chemistry chemical physics : PCCP
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Stability of Asymmetric Lipid Bilayers Assessed by Molecular Dynamics Simulations

2009

The asymmetric insertion of amphiphiles into biological membranes compromises the balance between the inner and outer monolayers. As a result, area expansion of the receiving leaflet and curvature strain may lead to membrane permeation, shape changes, or membrane fusion events. We have conducted both atomistic and coarse-grained molecular dynamics simulations of dipalmitoyl-phosphatidylcholine (DPPC) bilayers to study the effect of an asymmetric distribution of lipids between the two monolayers on membrane stability. Highly asymmetric lipid bilayers were found to be surprisingly stable within the submicrosecond time span of the simulations. Even the limiting case of a monolayer immersed in …

12-DipalmitoylphosphatidylcholineLipid BilayersBiochemistryCatalysisColloid and Surface ChemistryCOARSE-GRAINED MODELSHAPE TRANSFORMATIONSMonolayerComputer SimulationLipid bilayer phase behaviorLipid bilayerChemistryBilayerLipid bilayer fusionBiological membraneGeneral ChemistryLipid bilayer mechanicsANTIMICROBIAL PEPTIDESCrystallographyMembraneTRANSMEMBRANE DISTRIBUTIONEGG PHOSPHATIDYLCHOLINEPhosphatidylcholinesPORE FORMATIONBiophysicsPRESSURE PROFILESMECHANOSENSITIVE CHANNELlipids (amino acids peptides and proteins)OCTYL GLUCOSIDEPHOSPHOLIPID-BILAYERSJournal of the American Chemical Society
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Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Moll…

2011

Since sponges, as typical filter-feeders, are exposed to a high load of attacking prokaryotic and eukaryotic organisms, they are armed with a wide arsenal of antimicrobial/cytostatic low-molecular-weight, non-proteinaceous bioactive compounds. Here we present the first sponge agent belonging to the group of ASABF-type antimicrobial peptides. The ASABF gene was identified and cloned from the demospongeSuberites domuncula. The mature peptide, with a length of 64 aa residues has a predicted pI of 9.24, and comprises the characteristic CSαβ structural motif. Consequently, the S. domuncula ASABF shares high similarity with the nematode ASABFs ; it is distantly related to the defensins. The recom…

ASABFAntimicrobial peptidesGastropodaMolecular Sequence DataPharmaceutical SciencePeptideMicrobial Sensitivity TestsGram-Positive BacteriaReal-Time Polymerase Chain ReactionArticleMicrobiology03 medical and health sciencesantimicrobial peptidesAnti-Infective AgentsSequence Analysis ProteinDrug DiscoveryAnimalsBittium sp.Structural motiflcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)spongesPhylogeny030304 developmental biologychemistry.chemical_classification0303 health sciencesbiology030306 microbiologyEffectorHemolytic AgentsapoptosisGeologyBittium spsponges; <em>Suberites domuncula</em>; ASABF; antimicrobial peptides; apoptosis; <em>Bittium</em> sp.biology.organism_classificationSuberites domunculasponges ; Suberites domuncula ; ASABF ; antimicrobial peptides ; apoptosis ; Bittium sp.Recombinant ProteinsSuberites domunculaSpongeEnzymelcsh:Biology (General)chemistryMolluscaSuberitesSuberitesAntimicrobial Cationic PeptidesMarine Drugs
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