Search results for "Baculoviridae"

showing 10 items of 62 documents

Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding

2003

AbstractIn order to turn the subunit association and biotin binding of avidin into pH-sensitive phenomena, we have replaced individually three amino acid residues in avidin (Met96, Val115 and Ile117) with histidines in the 1–3 interface, and in combination with a histidine conversion in the 1–2 interface (Trp110). The single replacements Met96His and Val115His in the 1–3 interface were found to have a clear effect on the quaternary structure of avidin, since subunit associations of these mutants became pH-dependent. The histidine replacement in the 1–2 interface affected the biotin-binding properties of the mutants, in particular reversibility of binding and protein–ligand complex formation…

Models MolecularBiotin bindingInsectaProtein subunitBiophysicsBiotinBiosensing TechniquesBiochemistryCell LineProtein structureStructural BiologyGeneticsAnimalsHistidinepH dependenceProtein Structure QuaternaryMolecular BiologyHistidinebiologyChemistryCell BiologyProtein engineeringHydrogen-Ion ConcentrationAvidinRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry FluorescenceAmino Acid SubstitutionBiochemistryBiotinylationBiophysicsbiology.proteinProtein quaternary structureProtein engineeringBaculoviridaeProtein BindingAvidinFEBS Letters
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Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells

2004

AbstractA mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protei…

Parvovirus CanineRecombinant Fusion Proteinsanimal diseasesvirusesGreen Fluorescent ProteinsBiophysicsMammalian expressionBiochemistryCell LineGreen fluorescent proteinTransduction (genetics)DogsTransduction GeneticStructural BiologyGeneticsAnimalsBaculovirusCanine parvovirusMolecular BiologyCell NucleusEnhanced green fluorescent proteinbiologyParvovirusCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyCell biologyCapsidCytoplasmCell cultureCatsCapsid ProteinsBaculoviridaeNuclear localization sequenceFEBS Letters
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Enhanced baculovirus-mediated transduction of human cancer cells by tumor-homing peptides.

2006

ABSTRACT Tumor cells and vasculature offer specific targets for the selective delivery of therapeutic genes. To achieve tumor-specific gene transfer, baculovirus tropism was manipulated by viral envelope modification using baculovirus display technology. LyP-1, F3, and CGKRK tumor-homing peptides, originally identified by in vivo screening of phage display libraries, were fused to the transmembrane anchor of vesicular stomatitis virus G protein and displayed on the baculoviral surface. The fusion proteins were successfully incorporated into budded virions, which showed two- to fivefold-improved binding to human breast carcinoma (MDA-MB-435) and hepatocarcinoma (HepG2) cells. The LyP-1 pepti…

Phage displayCarcinoma HepatocellularTransgenevirusesImmunologyBreast NeoplasmsGene deliveryMicrobiologyVesicular stomatitis Indiana virusTransduction (genetics)Gene DeliveryViral envelopePeptide LibraryTransduction GeneticVirologyCell Line TumorHumansGlycoproteinsbiologyGenetic Therapybiology.organism_classificationMolecular biologyFusion proteinNeoplasm ProteinsVesicular stomatitis virusCell cultureInsect ScienceCapsid ProteinsPeptidesBaculoviridaeProtein BindingJournal of virology
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Properties of baculovirus particles displaying GFP analyzed by fluorescence correlation spectroscopy.

2003

Abstract Recombinant baculovirus particles displaying green fluorescent protein (GFP) fused to the major envelope glycoprotein gp64 of the Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) were characterized by fluorescence correlation spectroscopy (FCS). FCS detected Brownian motion of single, intact recombinant baculovirus display particles with a diffusion coefficient (D) of (2.89±0.74)10 8 cm2s 1 and an apparent hydrodynamic radius of 83.35±21.22 nm. In the presence of sodium dodecyl sulfate (SDS), Triton X-100, and octylglucoside, the diffusion time was reduced to the 0.2 ms range (D = 7.5710 7 cm2s 1), showing that the fusion proteins were anchored in the viral envelope…

PhotochemistryvirusesClinical BiochemistryDetergentsGreen Fluorescent ProteinsFluorescence correlation spectroscopySpodopteraBiochemistryGreen fluorescent proteinDiffusionchemistry.chemical_compoundViral envelopeAnimalsSodium dodecyl sulfateMolecular BiologybiologyChemistryViral membranebiology.organism_classificationFluorescenceFusion proteinMolecular biologyMolecular WeightAutographa californicaLuminescent ProteinsSpectrometry FluorescenceElectrophoresis Polyacrylamide GelIndicators and ReagentsBaculoviridaeViral Fusion ProteinsAlgorithmsBiological chemistry
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Production of biologically active recombinant avidin in baculovirus-infected insect cells

1997

Abstract An efficient lepidopteran insect cell system was established for the expression of a recombinant form of chicken egg-white avidin. The gene product was obtained in both secreted and intracellular forms, and biologically active recombinant avidin was isolated using affinity chromatography on an iminobiotin–agarose column. Similar to the known quaternary structure of the native egg-white protein, the purified recombinant protein was glycosylated and assembled mainly into tetramers. Like native avidin, the recombinant tetramer also exhibited a high level of thermostability, and was further stabilized upon binding biotin. The biotin-binding and structural properties of the recombinant …

Protein DenaturationGlycosylationProtein ConformationGenetic VectorsBiotinEnzyme-Linked Immunosorbent AssaySpodopteraChromatography Affinitylaw.inventionchemistry.chemical_compoundAffinity chromatographyBiotinTetramerlawAnimalsbiologySepharoseAvidinFusion proteinRecombinant ProteinsBiochemistrychemistryBiotinylationRecombinant DNAbiology.proteinProtein quaternary structureBaculoviridaeChickensBiotechnologyAvidinProtein Expression and Purification
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Expression and glycosylation studies of human FGF receptor 4

2001

Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large am…

Protein FoldingGlycosylationGlycosylationBlotting WesternImmunoblottingMolecular Sequence DataProtein RenaturationBiologyFibroblast growth factorMass SpectrometryInclusion bodiesCell Line03 medical and health scienceschemistry.chemical_compoundSDG 3 - Good Health and Well-beingEscherichia coliAnimalsHumansReceptor Fibroblast Growth Factor Type 4TrypsinAmino Acid SequenceDisulfidesReceptorChromatography High Pressure Liquid030304 developmental biologyInclusion Bodies0303 health sciencesHeparin030302 biochemistry & molecular biologyFibroblast growth factor receptor 4Fibroblast growth factor receptor 3Receptors Fibroblast Growth FactorMolecular biologyRecombinant Proteins3. Good healthchemistryFibroblast growth factor receptorMutationRNA splicing/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingBaculoviridaeBiotechnology
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Cell Susceptibility to Baculovirus Transduction and Echovirus Infection Is Modified by Protein Kinase C Phosphorylation and Vimentin Organization

2013

ABSTRACT Some cell types are more susceptible to viral gene transfer or virus infection than others, irrespective of the number of viral receptors or virus binding efficacy on their surfaces. In order to characterize the cell-line-specific features contributing to efficient virus entry, we studied two cell lines (Ea.hy926 and MG-63) that are nearly nonpermissive to insect-specific baculovirus (BV) and the human enterovirus echovirus 1 (EV1) and compared their characteristics with those of a highly permissive (HepG2) cell line. All the cell lines contained high levels of viral receptors on their surfaces, and virus binding was shown to be efficient. However, in nonpermissive cells, BV and it…

Protein Kinase C-alphaImmunologyVimentinProtein Kinase C-epsilonBiologyModels BiologicalMicrobiologyFilamentous actinCell LineSyndecan 1MiceTransduction (genetics)Transduction GeneticViral entryVirologyAnimalsHumansVimentinPhosphorylationProtein kinase CVirulenceHEK 293 cellsHep G2 CellsVirus InternalizationMolecular biologyvirologyCulture MediaEnterovirus B HumanVirus-Cell InteractionsHEK293 CellsvirologiaCell cultureInsect ScienceHost-Pathogen Interactionsbiology.proteinReceptors VirusSyndecan-1Integrin alpha2beta1BaculoviridaeJournal of Virology
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Expression and trafficking of fluorescent viral membrane proteins in baculovirus-transduced BHK cells

2004

Baculovirus vectors show promise as a novel tool for gene delivery into mammalian cells and gene transfer with wild-type baculovirus has been demonstrated both in vitro and in vivo. To study expression and intracellular trafficking of foreign viral membrane proteins in baculovirus-transduced mammalian cells, the envelope proteins, E1 and E2, of rubella virus (RV) were chosen as a model. The enhanced green fluorescent protein (EGFP) and a red fluorescent protein (RFP) were fused to the C-terminus of E1 and E2, respectively. The proteins were cloned under a cytomegalovirus (CMV) promoter and expressed as fluorescent fusion proteins in baculovirus-transduced baby hamster kidney (BHK) cells. Ex…

Recombinant Fusion ProteinsvirusesGenetic VectorsBioengineeringBiologyGene deliveryKidneyTransfectionApplied Microbiology and BiotechnologyCell LineGreen fluorescent proteinTransduction (genetics)Viral Envelope ProteinsCricetinaeBaby hamster kidney cellProtein biosynthesisAnimalsGene Expression ProfilingEndoplasmic reticulumGeneral MedicineMolecular biologyFusion proteinIn vitroCell biologyProtein TransportGene Expression RegulationMicroscopy FluorescenceBaculoviridaeBiotechnologyJournal of Biotechnology
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Specific Binding of Baculoviruses Displaying gp64 Fusion Proteins to Mammalian Cells

2001

Viral vectors displaying specific ligand binding moieties have raised an increasing interest in the area of targeted gene therapy. In this report, we describe baculovirus vectors displaying either a functional single chain antibody fragment (scFv) specific for the carcinoembryonic antigen (CEA) or the synthetic IgG binding domains (ZZ) derived from protein A of Staphylococcus aureus. In addition, the vectors were engineered to incorporate a reporter gene encoding the enhanced green fluorescent protein (EGFP) under the transcriptional regulation of the cytomegalovirus (CMV) IE promoter. Display of the targeting moieties on the viral surface was achieved through fusion to the N-terminus of gp…

Recombinant Fusion ProteinsvirusesGenetic VectorsGreen Fluorescent ProteinsImmunoglobulin Variable RegionBiophysicsSpodopteraTransfectionBiochemistryCell LineGreen fluorescent proteinViral vector03 medical and health sciencesGenes ReporterTransduction GeneticCricetinaeTumor Cells CulturedAnimalsStaphylococcal Protein AMolecular Biology030304 developmental biology0303 health sciencesReporter genebiology030302 biochemistry & molecular biologyAntibodies MonoclonalGenetic TherapyCell BiologyTransfectionFusion proteinMolecular biologyCarcinoembryonic Antigen3. Good healthLuminescent ProteinsMicroscopy FluorescenceIgG bindingbiology.proteinAntibodyProtein ABaculoviridaeViral Fusion ProteinsBiochemical and Biophysical Research Communications
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