Search results for "Parvovirus"

showing 10 items of 98 documents

Persistence of Human Bocavirus 1 in Tonsillar Germinal Centers and Antibody-Dependent Enhancement of Infection

2021

Human bocavirus 1 (HBoV1), a common pediatric respiratory pathogen, can persist in airway secretions for months hampering diagnosis. It also persists in tonsils, providing potential reservoirs for airway shedding, with the exact location, host cell types, and virus activity unknown.

NASOPHARYNXviruksetPalatine TonsilFc receptorCHILDRENvirus persistenceMonocytesHuman bocavirusCONGENITAL INSENSITIVITYBokavirusChildviruspersistenssi11832 Microbiology and virology0303 health sciencesB-LymphocytesbiologyHuman bocavirusvasta-aineetDENGUE-VIRUS-INFECTIONrespiratory systemMiddle AgedQR1-5023. Good healthLymphatic systemB-CELLSChild PreschoolAntibodyCELL-LINE U937HUMAN PARVOVIRUSResearch ArticleAdultAdolescentEndosomesMicrobiologyinfektiotVirusHost-Microbe BiologyParvoviridae Infections03 medical and health sciencesYoung AdultImmune systemnielurisaVirologytonsilsHumansAntibody-dependent enhancementRESPIRATORY VIRUSESparvovirukset030304 developmental biologyAgedRECEPTOR030306 microbiologyparvovirusInfant NewbornGerminal centerInfantbiology.organism_classificationGerminal CenterAntibody-Dependent Enhancementrespiratory tract diseasesgerminal centerImmunologyDNA Viralbiology.protein1182 Biochemistry cell and molecular biology3111 Biomedicinein situ hybridizationADEB-soluTRACTmBio
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Influence of the oncolytic parvovirus H-1, CTLA-4 antibody tremelimumab and cytostatic drugs on the human immune system in a human in vitro model of …

2013

Bernd Heinrich,* Katrin Goepfert,* Maike Delic, Peter R Galle, Markus MoehlerUniversity Medical Center of the Johannes Gutenberg University Mainz, 1st Department of Internal Medicine, Langenbeckstrasse, Mainz, Germany *These authors contributed equally to this workIntroduction: Tumor-directed and immune-system-stimulating therapies are of special interest in cancer treatment. Here, we demonstrate the potential of parvovirus H-1 (H-1PV) to efficiently kill colorectal cancer cells and induce immunogenicity of colorectal tumors by inducing maturation of dendritic cells (DCs) alone and also in combination with cytostatic drugs in vitro. Using our cell culture model, we have additionally investi…

Parvovirus H-1business.industrymedicine.medical_treatmentOncoTargets and TherapyOncolytic virusImmune systemCytokineOncologyAntigenCTLA-4ImmunologyCancer researchmedicineSW480Cytotoxic T cellPharmacology (medical)dendritic cellsbusinessTremelimumabmedicine.drugOriginal ResearchOncoTargets and Therapy
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Distribution and dynamics of transcription-associated proteins during parvovirus infection.

2012

Canine parvovirus (CPV) infection leads to reorganization of nuclear proteinaceous subcompartments. Our studies showed that virus infection causes a time-dependent increase in the amount of viral nonstructural protein NS1 mRNA. Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein (TBP), transcription factor IIB (TFIIB), and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins. peerReviewed

Parvovirus transkriptioproteiinitvirusesdynamiikka
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Desipramine induces disorder in cholesterol-rich membranes:implications for viral trafficking

2009

In this study, the effect of desipramine (DMI) on phospholipid bilayers and parvoviral entry was elucidated. In atomistic molecular dynamics simulations, DMI was found to introduce disorder in cholesterol-rich phospholipid bilayers. This was manifested by a decrease in the deuterium order parameter S(CD) as well as an increase in the membrane area. Disordering of the membrane suggested DMI to destabilize cholesterol-rich membrane domains (rafts) in cellular conditions. To relate the raft disrupting ability of DMI with novel biological relevance, we studied the intracellular effect of DMI using canine parvovirus (CPV), a virus known to interact with endosomal membranes and sphingomyelin, as …

Parvovirus CanineEndosomeBiophysicsPhospholipidBiologyAntidepressive Agents Tricyclicchemistry.chemical_compoundDogsStructural BiologyDesipraminemedicineAnimalsComputer SimulationMolecular BiologyCells CulturedMolecular StructureVesicleCell MembraneDesipramineCell BiologyRaftDisease Models AnimalMembraneCholesterolchemistryBiochemistryBiophysicslipids (amino acids peptides and proteins)Sphingomyelinhuman activitiesIntracellularmedicine.drug
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Role of Recycling Endosomes and Lysosomes in Dynein-Dependent Entry of Canine Parvovirus

2002

ABSTRACT Canine parvovirus (CPV) is a nonenveloped virus with a 5-kb single-stranded DNA genome. Lysosomotropic agents and low temperature are known to prevent CPV infection, indicating that the virus enters its host cells by endocytosis and requires an acidic intracellular compartment for penetration into the cytoplasm. After escape from the endocytotic vesicles, CPV is transported to the nucleus for replication. In the present study the intracellular entry pathway of the canine parvovirus in NLFK (Nordisk Laboratory feline kidney) cells was studied. After clustering in clathrin-coated pits and being taken up in coated vesicles, CPV colocalized with coendocytosed transferrin in endosomes r…

Parvovirus CanineEndosomeanimal diseasesvirusesImmunologyDyneinCoated vesicleEndosomesBiologyEndocytosisMicrobiologyMicrotubulesCell LineDogsMicrotubuleVirologyAnimalsMicroscopy ImmunoelectronIn Situ Hybridization FluorescenceMicroscopy ConfocalVesicleEndoplasmic reticulumDyneinsEndocytosisCell biologyVirus-Cell InteractionsCytoplasmInsect ScienceLysosomes
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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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Assembly of fluorescent chimeric virus-like particles of canine parvovirus in insect cells

2004

Canine parvovirus (CPV) is a small non-enveloped ssDNA virus composed of the viral proteins VP1, VP2, and VP3 with a T=1 icosahedral symmetry. VP2 is nested in VP1 and the two proteins are produced by differential splicing of a primary transcript of the right ORF of the viral genome. The VP2 protein can be further proteolytically cleaved to form VP3. Previous studies have shown that VP1 and VP3 are unnecessary for capsid formation and consequently, that VP2 alone is sufficient for assembly. We have hypothesized that insertion of the enhanced green fluorescent protein (EGFP) at the N-terminus of VP2 could be carried out without altering assembly. To investigate the possibility to develop flu…

Parvovirus CanineRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsHeterologousFluorescence correlation spectroscopySpodopteraBiochemistryVirusCell LineInclusion Bodies ViralGreen fluorescent proteinAnimalsAmino Acid SequenceMolecular BiologyMicroscopy ConfocalBase SequencebiologyChimeraVirus AssemblyCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFusion proteinLuminescent ProteinsMicroscopy ElectronCapsidRNA splicingCapsid ProteinsPlasmidsBiochemical and Biophysical Research Communications
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Distribution and Dynamics of Transcription-Associated Proteins during Parvovirus Infection

2012

ABSTRACT Canine parvovirus (CPV) infection leads to reorganization of nuclear proteinaceous subcompartments. Our studies showed that virus infection causes a time-dependent increase in the amount of viral nonstructural protein NS1 mRNA. Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein (TBP), transcription factor IIB (TFIIB), and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins.

Parvovirus CanineViral nonstructural proteinvirusesImmunologyMicrobiologyParvoviridae Infections03 medical and health sciencesVirologyAnimalsTranscription factor030304 developmental biology0303 health sciencesbiologyParvovirusBinding protein030302 biochemistry & molecular biologyCanine parvovirusFluorescence recovery after photobleachingbiology.organism_classificationMolecular biology3. Good healthVirus-Cell InteractionsCell CompartmentationInsect Sciencebiology.proteinTATA-binding proteinTranscription factor II BSubcellular FractionsTranscription Factors
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Detection of canine parvovirus antigens with antibodies to synthetic peptides

1996

Antibodies produced in rabbits against an 18-amino acid peptide (peptide 1, NSLPQSEGATNFGDIGVP) of capsid protein VP2/residues 292-309 of canine parvovirus (CPV) or against an 18-amino acid peptide (peptide 2, GKRNTVLFHGPASTKGKS) of nonstructural protein NS1/residues 391-409 of CPV identified, in immunofluorescence analysis, viral antigens in canine A 72 cells infected with CPV. Antibodies to peptide 2 also identified viral antigens in bovine cells infected with bovine parvovirus. In western blot analysis, antibodies to peptide 1 and peptide 2 also detected viral antigens derived from blue fox parvovirus, feline parvovirus, mink enteritis virus and raccoon dog parvovirus. The peptide antibo…

Parvovirus Canineanimal diseasesvirusesBlotting WesternMolecular Sequence DataFoxesEnzyme-Linked Immunosorbent AssayAntibodies ViralVirusParvovirusCapsidDogsAntigenVirologyAnimalsAmino Acid SequenceFluorescent Antibody Technique IndirectAntigens ViralPeptide sequenceParvoviridaebiologyParvovirusCanine parvovirusvirus diseasesGeneral MedicineBovine parvovirusbiology.organism_classificationVirologyMink enteritis virusMinkCatsCapsid ProteinsCattleRaccoonsRabbitsFeline Panleukopenia VirusArchives of Virology
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Reorganization of Nuclear Pore Complexes and the Lamina in Late-Stage Parvovirus Infection

2015

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Parvovirus Canineanimal diseasesvirusesnuclear pore complexesImmunologyMicrobiologyParvoviridae InfectionsCapsidDogsVirologymedicineotorhinolaryngologic diseasesAnimalsDog DiseasesNuclear poreparvovovirusCell NucleusNuclear LaminaLamin Type BbiologyParvovirusParvovirus infectionCanine parvovirusLamin Type Abiology.organism_classificationmedicine.diseaseVirologyVirus-Cell InteractionsCell biologyNuclear Pore Complex ProteinsCell nucleusstomatognathic diseasesmedicine.anatomical_structureInsect ScienceNuclear PoreNuclear laminaNucleusLamin
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