Search results for "030102 biochemistry & molecular biology"

showing 10 items of 174 documents

A novel rat CVB1-VP1 monoclonal antibody 3A6 detects a broad range of enteroviruses

2018

AbstractEnteroviruses (EVs) are common RNA viruses that cause diseases ranging from rash to paralytic poliomyelitis. For example, EV-A and EV-C viruses cause hand-foot and mouth disease and EV-B viruses cause encephalitis and myocarditis, which can result in severe morbidity and mortality. While new vaccines and treatments for EVs are under development, methods for studying and diagnosing EV infections are still limited and therefore new diagnostic tools are required. Our aim was to produce and characterize new antibodies that work in multiple applications and detect EVs in tissues and in vitro. Rats were immunized with Coxsackievirus B1 capsid protein VP1 and hybridomas were produced. Hybr…

Models Molecular0301 basic medicineBiolääketieteet - BiomedicineProtein Conformationmedicine.drug_classImmunoelectron microscopylcsh:MedicineEnzyme-Linked Immunosorbent AssayCoxsackievirusmedicine.disease_causeMonoclonal antibodyenterovirusesArticleEpitopeEpitopesMice03 medical and health sciencesProtein DomainsEnterovirus InfectionsmedicineantibodiesAnimalsHumanslcsh:ScienceMultidisciplinary030102 biochemistry & molecular biologybiologyPolioviruslcsh:Rvasta-aineetAntibodies Monoclonalbiology.organism_classificationAntibodies NeutralizingImmunohistochemistryVirologyEnterovirus B HumanRats3. Good healthenterovirukset030104 developmental biologyKasvibiologia mikrobiologia virologia - Plant biology microbiology virologybiology.proteinImmunohistochemistrylcsh:QCapsid ProteinsAntibodyClone (B-cell biology)Protein BindingScientific Reports
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Electrostatic Tuning of the Ligand Binding Mechanism by Glu27 in Nitrophorin 7

2018

AbstractNitrophorins (NP) 1–7 are NO-carrying heme proteins found in the saliva of the blood-sucking insect Rhodnius prolixus. The isoform NP7 displays peculiar properties, such as an abnormally high isoelectric point, the ability to bind negatively charged membranes, and a strong pH sensitivity of NO affinity. A unique trait of NP7 is the presence of Glu in position 27, which is occupied by Val in other NPs. Glu27 appears to be important for tuning the heme properties, but its influence on the pH-dependent NO release mechanism, which is assisted by a conformational change in the AB loop, remains unexplored. Here, in order to gain insight into the functional role of Glu27, we examine the ef…

Models Molecular0301 basic medicineConformational changeProtein ConformationMolecular biologylcsh:MedicineSangCrystallography X-RayLigands01 natural scienceschemistry.chemical_compoundProtein structureModelsZoologiaBloodsucking insectsNitrophorinStatic electricitylcsh:ScienceHemeCell receptorschemistry.chemical_classificationCrystallographyMultidisciplinaryParasitologiaAmino acidBloodRhodniusInsect ProteinsAnimals; Crystallography X-Ray; Glutamic Acid; Heme; Hemeproteins; Insect Proteins; Ligands; Models Molecular; Molecular Dynamics Simulation; Mutation; Protein Conformation; Rhodnius; Salivary Proteins and Peptides; Static ElectricityHemeproteinsHemeproteinStatic ElectricityGlutamic AcidHemeMolecular Dynamics Simulation010402 general chemistryArticle03 medical and health sciencesAnimalsSalivary Proteins and PeptidesBiologia molecularInsectes hematòfags030102 biochemistry & molecular biologylcsh:RMolecular0104 chemical sciencesIsoelectric pointchemistryMutationX-RayBiophysicslcsh:QReceptors cel·lularsParasitologyZoologyScientific Reports
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Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Fumarate dependent protein composition under aerobic and anaerobic growth conditions in Escherichia coli

2020

Abstract In the absence of sugars, C4-dicarboxylates (C4DC) like fumarate represent important substrates for growth of Escherichia coli. Aerobically, C4DCs are oxidized to CO2 whereas anaerobically, C4DCs are used for fumarate respiration. In order to determine the impact of fumarate under aerobic and anaerobic conditions, proteomes of E. coli W3110 grown aerobically or anaerobically with fumarate and/or the non-C4DC substrate glycerol were comparatively profiled by nanoLC-MS/MS. Membrane enrichment allowed sensitive detection of membrane proteins. A total of 1657 proteins of which 646 and 374 were assigned to the cytosol or membrane, respectively, were covered. Presence of fumarate trigger…

Proteomics0301 basic medicineBiophysicsCatabolite repressionmedicine.disease_causeBiochemistryCarbon utilization03 medical and health sciencesFumaratesTandem Mass SpectrometryEscherichia colimedicineDicarboxylic AcidsAnaerobiosisEscherichia coli030102 biochemistry & molecular biologybiologyChemistryEscherichia coli ProteinsGene Expression Regulation BacterialAerobiosisDNA-Binding ProteinsCitric acid cycle030104 developmental biologyRegulonMembrane proteinBiochemistrycAMP receptor proteinbiology.proteinProtein KinasesAnaerobic exerciseTranscription FactorsJournal of Proteomics
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Minimal Information About an Immuno-Peptidomics Experiment (MIAIPE)

2018

Minimal Information about an Immuno-Peptidomics Experiment (MIAIPE) is an initiative of the members of the Human Immuno-Peptidome Project (HIPP), an international program organized by the Human Proteome Organization (HUPO). The aim of the MIAIPE guidelines is to deliver technical guidelines representing the minimal information required to sufficiently support the evaluation and interpretation of immunopeptidomics experiments. The MIAIPE document has been designed to report essential information about sample preparation, mass spectrometric measurement and associated mass spectrometry (MS)-related bioinformatics aspects that are unique to immunopeptidomics and may not be covered by the genera…

Proteomics0301 basic medicineComputer scienceComputational biologyProteomicsBiochemistrySpecimen Handling03 medical and health sciencesStandardisation & GuidelinesHuman proteome projectHumansantigen processing and presentationDatabases ProteinMolecular Biology030102 biochemistry & molecular biologyHistocompatibility Antigens Class IHistocompatibility Antigens Class IIimmunopeptidomicsComputational BiologyMass spectrometricPeptide Fragmentsmajor histocompatibility complex3. Good health030104 developmental biologyComputational Biology/standards; Databases Protein; Histocompatibility Antigens Class I/analysis; Histocompatibility Antigens Class I/immunology; Histocompatibility Antigens Class I/metabolism; Histocompatibility Antigens Class II/analysis; Histocompatibility Antigens Class II/immunology; Histocompatibility Antigens Class II/metabolism; Humans; Peptide Fragments/analysis; Peptide Fragments/immunology; Peptide Fragments/metabolism; Proteomics/standards; Software; Specimen Handling/standards; antigen processing and presentation; immunopeptidomics; major histocompatibility complexSoftwareantigen processing and presentation; immunopeptidomics; major histocompatibility complex
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Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus

2016

Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, 
 including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemag…

Proteomics0301 basic medicinePhysiologySyconBiochemistry03 medical and health sciencesAffinity chromatographyLectinsAnimalsTrypsinMolecular Biology030102 biochemistry & molecular biologybiologyCalcareous spongeHemagglutinationLectinClathrina clathrusbiology.organism_classificationMolecular biologyCell aggregationPoriferaPorifera ; Clathrina clathrus ; lectin ; N-acetyl-glucosamine ; cell aggregation ; proteomicsSponge030104 developmental biologyBiochemistryConcanavalin AProteolysisbiology.proteinCarbohydrate MetabolismFemaleRabbitsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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Evaluation of FASP, SP3, and iST Protocols for Proteomic Sample Preparation in the Low Microgram Range

2017

Efficient and reproducible sample preparation is a prerequisite for any robust and sensitive quantitative bottom-up proteomics workflow. Here, we performed an independent comparison between single-pot solid-phase-enhanced sample preparation (SP3), filter-aided sample preparation (FASP), and a commercial kit based on the in-StageTip (iST) method. We assessed their performance for the processing of proteomic samples in the low μg range using varying amounts of HeLa cell lysate (1-20 μg of total protein). All three workflows showed similar performances for 20 μg of starting material. When handling sample sizes below 10 μg, the number of identified proteins and peptides as well as the quantitat…

Proteomics0301 basic medicineReproducibilityChromatography030102 biochemistry & molecular biologyChemistryMicrogramReproducibility of ResultsGeneral ChemistryCommercial kitProteomicsBiochemistrySpecimen HandlingWorkflow03 medical and health sciences030104 developmental biologySample SizeProteomeHumansSample preparationBottom-up proteomicsHeLa CellsTotal proteinJournal of Proteome Research
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Proteomic characterization of the mucosal pellicle formed in vitro on a cellular model of oral epithelium

2020

The oral mucosal pellicle is a thin lubricating layer generated by the binding of saliva proteins on epithelial oral cells. The protein composition of this biological structure has been to date studied by targeted analyses of specific salivary proteins. In order to perform a more exhaustive proteome characterization of pellicles, we used TR146 cells expressing or not the transmembrane mucin MUC1 and generated pellicles by incubation with human saliva and washing to remove unbound proteins. A suitable method was established for the in vitro isolation of the mucosal pellicle by "shaving" it from the cells using trypsin. The extracts, the washing solutions and the saliva used to constitute the…

Proteomics0301 basic medicineSalivaTR146/MUC1 cells[SDV]Life Sciences [q-bio]BiophysicsPluncBiochemistryEpithelium03 medical and health sciencesTandem Mass SpectrometrymedicineHumansDental PellicleSalivary Proteins and PeptidesSalivaproteomicMUC1Mucosal pellicle030102 biochemistry & molecular biologyChemistryMucinTrypsinIn vitroTransmembrane proteinCellular model of oral mucosa030104 developmental biologyBiochemistryProteome[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionmedicine.drugJournal of Proteomics
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