Search results for " REPLICATION"

showing 10 items of 406 documents

PML nuclear body-residing proteins sequentially associate with HPV genome after infectious nuclear delivery.

2019

Subnuclear promyelocytic leukemia (PML) nuclear bodies (NBs) are targeted by many DNA viruses after nuclear delivery. PML protein is essential for formation of PML NBs. Sp100 and Small Ubiquitin-Like Modifier (SUMO) are also permanently residing within PML NBs. Often, large DNA viruses disassemble and reorganize PML NBs to counteract their intrinsic antiviral activity and support establishment of infection. However, human papillomavirus (HPV) requires PML protein to retain incoming viral DNA in the nucleus for subsequent efficient transcription. In contrast, Sp100 was identified as a restriction factor for HPV. These findings suggested that PML NBs are important regulators of early stages o…

Viral DiseasesPhysiologyvirusesIntranuclear Inclusion BodiesPromyelocytic Leukemia ProteinVirus ReplicationBiochemistryAutoantigensImmune PhysiologyMedicine and Health SciencesCell Cycle and Cell DivisionNuclear proteinBiology (General)PapillomaviridaeStaining0303 health sciencesViral GenomicsImmune System ProteinsChromosome Biology030302 biochemistry & molecular biologyCell StainingTotal Cell CountingNuclear Proteinsvirus diseasesAntigens NuclearGenomicsCell biologymedicine.anatomical_structureInfectious DiseasesCapsidCell ProcessesViral GenomeCellular Structures and OrganellesIntranuclear SpaceResearch ArticleHuman Papillomavirus InfectionQH301-705.5UrologyImmunologyCell Enumeration TechniquesSUMO-1 ProteinSexually Transmitted DiseasesMitosisMicrobial GenomicsGenome ViralBiologyResearch and Analysis MethodsMicrobiologyVirusAntibodies03 medical and health sciencesPromyelocytic leukemia proteinVirologyNuclear BodiesmedicineGeneticsHumansVesiclesMolecular BiologyMitosisTranscription factor030304 developmental biologyCell NucleusGenitourinary InfectionsTumor Suppressor ProteinsBiology and Life SciencesProteinsCell BiologyRC581-607Cell nucleusViral replicationSpecimen Preparation and Treatmentbiology.proteinParasitologyCapsid ProteinsImmunologic diseases. AllergyTranscription FactorsPLoS Pathogens
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Respiratory syncytial virus inhibits ciliagenesis in differentiated normal human bronchial epithelial cells: effectiveness of N-acetylcysteine.

2012

Persistent respiratory syncytial virus (RSV) infections have been associated with the exacerbation of chronic inflammatory diseases, including chronic obstructive pulmonary disease (COPD). This virus infects the respiratory epithelium, leading to chronic inflammation, and induces the release of mucins and the loss of cilia activity, two factors that determine mucus clearance and the increase in sputum volume. These alterations involve reactive oxygen species-dependent mechanisms. The antioxidant N-acetylcysteine (NAC) has proven useful in the management of COPD, reducing symptoms, exacerbations, and accelerated lung function decline. NAC inhibits RSV infection and mucin release in human A54…

Viral DiseasesPulmonologyChronic Obstructive Pulmonary Diseaseslcsh:MedicineMucin 5ACVirus ReplicationAcetylcysteinePulmonary Disease Chronic ObstructiveTubulinRespiratory systemlcsh:ScienceCells CulturedMultidisciplinaryInterleukin-13Microscopy VideoCell DifferentiationForkhead Transcription FactorsFree Radical Scavengersrespiratory systemHost-Pathogen InteractionLower Respiratory Tract InfectionsInfectious Diseasesmedicine.anatomical_structureInterleukin 13Medicinemedicine.symptomResearch Articlemedicine.drugDrugs and DevicesInflammationBronchiRespiratory Syncytial Virus InfectionsBiologyMicrobiologyAntiviral AgentsUpper Respiratory Tract InfectionsmedicineHumansCiliaBiologyInflammationRespiratory Syncytial Virus InfectionA549 cellMucinlcsh:RImmunityEpithelial CellsAxonemal DyneinsEpitheliumAcetylcysteineGene Expression RegulationRespiratory Syncytial Virus HumanRespiratory InfectionsImmunologyRespiratory epitheliumlcsh:QPLoS ONE
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Replication of hepatitis C virus

2000

Viral pathogenesisHepatitis C virusVirus AssemblyViral transformationHepatitis CHepacivirusBiologymedicine.diseasemedicine.disease_causeTransfectionVirus ReplicationMicrobiologyVirologyPathogenesisViral ProteinsViral replicationReplication (statistics)medicineAnimalsRNA ViralOncovirusCells Cultured
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The evolution of collective infectious units in viruses

2019

Viruses frequently spread among cells or hosts in groups, with multiple viral genomes inside the same infectious unit. These collective infectious units can consist of multiple viral genomes inside the same virion, or multiple virions inside a larger structure such as a vesicle. Collective infectious units deliver multiple viral genomes to the same cell simultaneously, which can have important implications for viral pathogenesis, antiviral resistance, and social evolution. However, little is known about why some viruses transmit in collective infectious units, whereas others do not. We used a simple evolutionary approach to model the potential costs and benefits of transmitting in a collect…

Viral pathogenesisviruseseducationGenome ViralBiologyVirus ReplicationGenomebehavioral disciplines and activitiesArticleEvolution Molecular03 medical and health sciences0302 clinical medicine030304 developmental biology0303 health sciencesVirus AssemblyAntiviral resistanceVirionDefective VirusesModels TheoreticalVirologyViral replicationViral genomesVirus Diseasespopulation characteristicsRNA Viral030217 neurology & neurosurgery
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Cordycepin analogues of 2',5'-oligoadenylate inhibit human immunodeficiency virus infection via inhibition of reverse transcriptase.

1991

Analogues of 2',5'-oligoadenylates (2-5A), the cordycepin (3'-deoxyadenosine) core trimer (Co3) and its 5'-monophosphate derivative (pCo3), were shown to display pronounced anti-human immunodeficiency virus type 1 (HIV-1) activity in vitro. Treatment of HIV-1 infected H9 cells with 1 microM Co3 or pCo3 resulted in an almost 100% inhibition of virus production. The compounds were encapsulated in liposomes targeted by antibodies specific for the T-cell receptor molecule CD3. Substitution of one or two cordycepin units in Co3 or pCo3 decreased the antiviral activity of the compounds. pCo3 did not stimulate 2-5A-dependent ribonuclease L activity and displayed no effect on the amount of cellular…

Virus ReplicationBiochemistryAntiviral AgentsVirusCell Linechemistry.chemical_compoundStructure-Activity RelationshipDeoxyadenosineHumansPolymeraseNucleic Acid Synthesis InhibitorsOligoribonucleotidesbiologyCordycepinDeoxyadenosines2'-5'-OligoadenylateAdenine NucleotidesRNAMolecular biologyReverse transcriptaseBiochemistrychemistryRNA RibosomalLiposomesbiology.proteinHIV-1RNA Transfer LysReverse Transcriptase InhibitorsRibonuclease LBiochemistry
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Adenovirus E1A/E1B Transformed Amniotic Fluid Cells Support Human Cytomegalovirus Replication.

2015

The human cytomegalovirus (HCMV) replicates to high titers in primary human fibroblast cell cultures. A variety of primary human cells and some tumor-derived cell lines do also support permissive HCMV replication, yet at low levels. Cell lines established by transfection of the transforming functions of adenoviruses have been notoriously resistant to HCMV replication and progeny production. Here, we provide first-time evidence that a permanent cell line immortalized by adenovirus type 5 E1A and E1B (CAP) is supporting the full HCMV replication cycle and is releasing infectious progeny. The CAP cell line had previously been established from amniotic fluid cells which were likely derived from…

adenovirus E1A/E1BvirusesAdenoviruses Human610 Medizinlcsh:QR1-502Cytomegalovirusamniotic fluid cellsCell Transformation ViralVirus ReplicationCAPlcsh:MicrobiologyArticleCevec’s aminocyte production cell lineAdenovirus Infections Human610 Medical sciencesCytomegalovirus InfectionsHumansAdenovirus E1A ProteinsAdenovirus E1B ProteinsViruses
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Cytoplasmic Parvovirus Capsids Recruit Importin Beta for Nuclear Delivery

2019

Parvoviruses are an important platform for gene and cancer therapy. Their cell entry and the following steps, including nuclear import, are inefficient, limiting their use in therapeutic applications. Two models exist on parvoviral nuclear entry: the classical import of the viral capsid using nuclear transport receptors of the importin (karyopherin) family or the direct attachment of the capsid to the nuclear pore complex leading to the local disintegration of the nuclear envelope. Here, by laser scanning confocal microscopy and in situ proximity ligation analyses combined with coimmunoprecipitation, we show that infection requires importin β-mediated access to the nuclear pore complex and …

alpha KaryopherinsCytoplasmNuclear EnvelopevirusesImmunologyActive Transport Cell NucleusImportinKaryopherinsBiologyVirus ReplicationMicrobiologyCell LineParvoviridae InfectionsParvovirus03 medical and health sciencesCapsidCytosolViral entryVirologyAnimalsNuclear pore030304 developmental biologyKaryopherinCell Nucleuschemistry.chemical_classification0303 health sciencesNucleoplasm030302 biochemistry & molecular biologyVirus Internalizationbeta KaryopherinsVirus-Cell InteractionsCell biologychemistryCytoplasmInsect ScienceNuclear PoreCapsid ProteinsNucleoporinNuclear transportJournal of Virology
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The Putative Metal Coordination Motif in the Endonuclease Domain of Human Parvovirus B19 NS1 Is Critical for NS1 Induced S Phase Arrest and DNA Damage

2011

The non-structural proteins (NS) of the parvovirus family are highly conserved multi-functional molecules that have been extensively characterized and shown to be integral to viral replication. Along with NTP-dependent helicase activity, these proteins carry within their sequences domains that allow them to bind DNA and act as nucleases in order to resolve the concatameric intermediates developed during viral replication. The parvovirus B19 NS1 protein contains sequence domains highly similar to those previously implicated in the above-described functions of NS proteins from adeno-associated virus (AAV), minute virus of mice (MVM) and other non-human parvoviruses. Previous studies have show…

apoptotic cell deathDNA repairDNA damagevirusesAmino Acid MotifsDNA Mutational AnalysisApoptosisSpodopteraViral Nonstructural ProteinsVirus ReplicationApplied Microbiology and Biotechnology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineControl of chromosome duplicationparvoviral infectionParvovirus B19 HumanAnimalsHumansMolecular BiologyEcology Evolution Behavior and SystematicsS phase030304 developmental biology0303 health sciencesbiologyParvovirushost cell DNA damagevirus diseasesHep G2 CellsCell BiologyEndonucleasesbiology.organism_classificationMolecular biology3. Good healthchemistryViral replicationS Phase Cell Cycle CheckpointsMutagenesis Site-Directed030211 gastroenterology & hepatologyDNAMinute virus of miceResearch PaperDNA DamageDevelopmental BiologyInternational Journal of Biological Sciences
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Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1.

2015

AbstractBacteriophage PRD1, which has been studied intensively at the structural and functional levels, still has some gene products with unknown functions and certain aspects of the PRD1 assembly process have remained unsolved. In this study, we demonstrate that the phage-encoded non-structural proteins P17 and P33, either individually or together, complement the defect in a temperature-sensitive GroES mutant of Escherichia coli for host growth and PRD1 propagation. Confocal microscopy of fluorescent fusion proteins revealed co-localisation between P33 and P17 as well as between P33 and the host chaperonin GroEL. A fluorescence recovery after photobleaching assay demonstrated that the diff…

assemblychaperoninvirusesMutantfluorescence recovery after photobleachingViral Nonstructural Proteinsmedicine.disease_causeVirus ReplicationChaperoninHost-Parasite InteractionsBacteriophagebacteriophageVirologymedicineEscherichia colifluorescent proteinBacteriophage PRD1Escherichia colimembrane virusMicroscopy Confocalbiologyprotein localisationVirus Assemblyta1182Fluorescence recovery after photobleachingGroESChaperonin 60biology.organism_classificationFusion proteinGroEL3. Good healthCell biologyVirology
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Endoreduplication induced in cultured Chinese hamster cells by different anti-topoisomerase II chemicals

2005

With the ultimate purpose of testing the hypothesis that, as shown in yeast mutants, any malfunction of DNA topoisomerase II might result in aberrant mitosis due to defective chromosome segregation, we have chosen three chemicals of different nature, recently reported to catalytically inhibit the enzyme. The endpoint selected to assess any negative effect on the ability of topoisomerase II to properly carry out decatenation of fully replicated chromosomes in the G2/M phase of the cell cycle was the presence of metaphases showing diplochromosomes as a result of endoreduplication, i.e. two successive rounds of DNA replication without intervening mitosis. The anti-topoisomerase drugs selected …

biologyHealth Toxicology and MutagenesisTopoisomeraseDNA replicationCell cycleMolecular biologyCell biologyChromosome segregationchemistry.chemical_compoundchemistryGeneticsbiology.proteinEndoreduplicationTopoisomerase-II InhibitorMitosisDNAMutation Research/Genetic Toxicology and Environmental Mutagenesis
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