Search results for "Thymosin"

showing 7 items of 7 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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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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A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa

2016

Conventional antibiotics might fail in the treatment of biofilm-associated infections causing infection recurrence and chronicity. The search for antimicrobial peptides has been performed with the aim to discover novel anti-infective agents active on pathogens in both planktonic and biofilm associated forms. The fragment 9-19 of human thymosin β4 was studied through 1 μs MD simulation. Two main conformations of the peptide were detected, both constituted by a central hydrophobic core and by the presence of peripheral charged residues suggesting a possible mechanism of interaction with two models of biological membranes, related to eukaryotic or bacterial membrane respectively. In addition, …

Models Molecular0301 basic medicineStaphylococcus aureusPhysiology030106 microbiologyAntimicrobial peptidesSettore BIO/05 - ZoologiaPeptideMicrobial Sensitivity TestsMolecular Dynamics SimulationBiologymedicine.disease_causeSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and BiotechnologyMicrobiologyStructure-Activity Relationship03 medical and health sciencesAnti-Infective AgentsmedicineHumansAmino Acid SequencePeptide sequencechemistry.chemical_classificationPseudomonas aeruginosaAntimicrobial peptides Molecular dynamics Staphylococcal biofilms ThymosinBiofilmThymosinGeneral MedicineAntimicrobialSettore CHIM/08 - Chimica FarmaceuticaThymosin030104 developmental biologychemistryBiochemistrySettore CHIM/03 - Chimica Generale E InorganicaBiofilmsPseudomonas aeruginosaPeptidesAntibacterial activityBiotechnology
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ANTIMICROBIAL AND ANTISTAPHYLOCOCCAL BIOFILM ACTIVITY FROM THE SEA URCHIN PARACENTROTUS LIVIDUS

2009

Aims: Staphylococcal biofilm-associated infections are resistant to conventional antibiotics. Consequently, new agents are needed to treat them. With this aim, we focused on the effector cells (coelomocytes) of the sea urchin Paracentrotus lividus immune system. Methods and Results: We tested the activity of the 5-kDa peptide fraction of the cytosol from coelomocytes (5-CC) against a group of Gram-positive, Gram-negative bacteria and fungi. We determined minimal inhibitory concentrations (MICs) ranging from 253.7 to 15.8 mg ml(-1). We observed an inhibitory activity and antibiofilm properties of 5-CC against staphylococcal biofilms of reference strains Staphylococcus epidermidis DSM 3269 an…

Staphylococcus aureusMicrobial ViabilityMicroscopy ConfocalStaining and LabelingMicrobial Sensitivity TestsStaphylococcal InfectionsCell FractionationSettore BIO/19 - Microbiologia GeneraleThymosinCytosolAnti-Infective AgentsBiofilmsParacentrotusStaphylococcus epidermidisAnimalsPeptidesantimicrobial antimicrobial peptides biofilminnate immunity staphylococci
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Fragments of β-thymosin from the sea urchin Paracentrotus lividus as potential antimicrobial peptides against staphylococcal biofilms.

2012

The immune mediators in echinoderms can be a potential source of novel antimicrobial peptides (AMPs) applied toward controlling pathogenic staphylococcal biofilms that are intrinsically resistant to conventional antibiotics. The peptide fraction5 kDa from the cytosol of coelomocytes of the sea urchin Paracentrotus lividus (5-CC) was tested against a group of Gram-positive and Gram-negative pathogen reference strains. The 5-CC of P. lividus was active against all planktonic-tested strains but also showed antibiofilm properties against staphylococcal strains. Additionally, we demonstrated the presence of three small peptides in the 5-CC belonging to segment 9-41 of a P. lividusβ-thymosin. The…

ThymosinAnti-Infective AgentsBiofilmsSea UrchinsStaphylococcusantibiofilm agents; antimicrobial peptides (AMPs); staphylococcal biofilmsstaphylococcal biofilmsAnimalsMicrobial Sensitivity TestsSettore BIO/19 - Microbiologia Generaleantibiofilm agentantimicrobial peptides (AMPs)Annals of the New York Academy of Sciences
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The comparison of beta-thymosin homologues among metazoa supports an arthropod-nematode clade.

2000

The definition of an Ecdysozoa clade among the protostomians, including all phyla with a regularly molted alpha-chitin-rich cuticle, has been one of the most provocative hypotheses to arise from recent investigations on animal phylogeny. Here we present evidence in favor of an arthropod-nematode clade, from the comparison of beta-thymosin homologues among the Metazoa. Arthropods and nematodes share the absence of the highly conserved beta-thymosin form found in all other documented bilaterian phyla as well as sponges, and the possession of a very unusual, internally triplicated homologue of the beta-thymosin protein, unknown in other phyla. We argue that such discrete molecular character is…

biologyNematodaSequence Homology Amino AcidPhylumMolecular Sequence DataZoologybiology.organism_classificationCladisticsThymosinMonophylyNematodeDrosophila melanogasterPhylogeneticsGeneticsAnimalsArthropodAmino Acid SequenceCladeCaenorhabditis elegansMolecular BiologyEcdysozoaArthropodshormones hormone substitutes and hormone antagonistsEcology Evolution Behavior and SystematicsPhylogenyJournal of molecular evolution
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Fragments of β-thymosin from the sea urchinParacentrotus lividusas potential antimicrobial peptides against staphylococcal biofilms

2012

The immune mediators in echinoderms can be a potential source of novel antimicrobial peptides (AMPs) applied toward controlling pathogenic staphylococcal biofilms that are intrinsically resistant to conventional antibiotics. The peptide fraction <5 kDa from the cytosol of coelomocytes of the sea urchin Paracentrotus lividus (5-CC) was tested against a group of Gram-positive and Gram-negative pathogen reference strains. The 5-CC of P. lividus was active against all planktonic-tested strains but also showed antibiofilm properties against staphylococcal strains. Additionally, we demonstrated the presence of three small peptides in the 5-CC belonging to segment 9-41 of a P. lividusβ-thymosin. T…

chemistry.chemical_classificationbiologymedicine.drug_classGeneral NeuroscienceAntimicrobial peptidesAntibioticsThymosinBiofilmPeptidebiology.organism_classificationGeneral Biochemistry Genetics and Molecular BiologyParacentrotus lividusMicrobiologyHistory and Philosophy of Sciencechemistrybiology.animalmedicineSea urchinPathogenAnnals of the New York Academy of Sciences
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