Search results for "Virology"

showing 10 items of 2354 documents

New enveloped dsRNA phage from freshwater habitat.

2015

Cystoviridae is a family of bacteriophages with a tri-segmented dsRNA genome enclosed in a tri-layered virion structure. Here, we present a new putative member of the Cystoviridae family, bacteriophage ϕNN. ϕNN was isolated from a Finnish lake in contrast to the previously identified cystoviruses, which originate from various legume samples collected in the USA. The nucleotide sequence of the virus reveals a strong genetic similarity (~80 % for the L-segments, ~55 % for the M-segments and ~84 % for the S-segments) to Pseudomonas phage ϕ6, the type member of the virus family. However, the relationship between ϕNN and other cystoviruses is more distant. In general, proteins located in the int…

CystoviridaevirusesMolecular Sequence DataFresh Waterfreshwater habitatsGenomeVirusBacteriophage03 medical and health sciencesVirologyPseudomonasSequence Homology Nucleic AcidCluster AnalysisBacteriophagesFinlandPhylogeny030304 developmental biologyGenetics0303 health sciencesbiology030306 microbiologyta1183ta1182Bacteriophage phi 6Nucleic acid sequenceSequence Analysis DNAbiology.organism_classificationVirologyRNA silencingLakesMolecular virologyRNA ViralRecombinationThe Journal of general virology
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Loss of surface fibronectin after infection of cultured cells by HSV-1 and 2

1985

Fibronectin is lost from the surface of HSV infected cells during cell rounding. In order to investigate also the fate of fibronectin during the process of HSV-induced cell-fusion, BHK, Vero as well as primary or secondary rabbit kidney cells were infected with HSV-1 strains producing cell-fusion. By immunofluorescence and immunoelectron microscopy a considerable loss of fibronectin after HSV infection could be demonstrated leaving only irregular clumps of fibronectin containing virus particles on the cell surface. Decrease and disarrangement of fibronectin was similar during cell rounding and cell fusion. Loss of Fibronectin was closely connected with the two types of the cytopathic effect…

Cytochalasin BvirusesImmunoelectron microscopyBiologyKidneyVirus ReplicationCell FusionCell membranechemistry.chemical_compoundCricetinaeVirologymedicineAnimalsSimplexvirusProtease InhibitorsCytochalasin BCells CulturedCytopathic effectCell fusionHerpes SimplexGeneral MedicineActin cytoskeletonVirologyFibronectinsFibronectinActin Cytoskeletonmedicine.anatomical_structurechemistryCell culturebiology.proteinRabbitsArchives of Virology
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Presentation of an Immunodominant Immediate-Early CD8+ T Cell Epitope Resists Human Cytomegalovirus Immunoevasion.

2013

Control of human cytomegalovirus (HCMV) depends on CD8+ T cell responses that are shaped by an individual's repertoire of MHC molecules. MHC class I presentation is modulated by a set of HCMV-encoded proteins. Here we show that HCMV immunoevasins differentially impair T cell recognition of epitopes from the same viral antigen, immediate-early 1 (IE-1), that are presented by different MHC class I allotypes. In the presence of immunoevasins, HLA-A- and HLA-B-restricted T cell clones were ineffective, but HLA-C*0702-restricted T cell clones recognized and killed infected cells. Resistance of HLA-C*0702 to viral immunoevasins US2 and US11 was mediated by the alpha3 domain and C-terminal region …

Cytomegalovirus InfectionMaleViral DiseasesvirusesCytomegalovirusEpitopes T-LymphocyteNK cellsAdaptive ImmunityCD8-Positive T-LymphocytesMajor Histocompatibility ComplexInterleukin 21Viral Envelope ProteinsCytotoxic T celllcsh:QH301-705.5Antigen PresentationbiologyViral Immune EvasionImmune cellsRNA-Binding ProteinsInnate ImmunityKiller Cells Naturalmedicine.anatomical_structureInfectious DiseasesCytomegalovirus InfectionsMedicineFemaleResearch Articlelcsh:Immunologic diseases. AllergyT cellImmunologyCD1T cells610StreptamerMicrobiologyImmediate-Early ProteinsImmunomodulationViral ProteinsVirologyMHC class IGeneticsmedicineHumansAntigen-presenting cellMolecular BiologyBiologyImmune EvasionHistocompatibility Antigens Class IImmunityMHC restrictionVirologyProtein Structure Tertiarylcsh:Biology (General)Immunologybiology.proteinParasitologylcsh:RC581-607
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DNA binding of L1 is required for human papillomavirus morphogenesis in vivo.

2002

AbstractThe role of putative DNA-binding domains of human papillomavirus (HPV) capsid proteins for DNA encapsidation in vivo is still unknown. We have now analyzed mutants of the major capsid protein L1 of HPV type 33, which are defective for DNA binding, for their ability to encapsidate DNA using an in vivo packaging approach. Since the DNA-binding domain and the nuclear localization signal (NLS) of L1 overlap, both a carboxy-terminal deletion mutant (L1-1/470) and a substitution mutant (L1-1/477M9) were analyzed. L1-1/477M9 has the classical NLS replaced by a noncanonical NLS taken from the human hnRNP protein A1. The mutant proteins were defective for DNA binding in contrast to wild-type…

CytoplasmHMG-boxMutantBiologyKidneypapillomavirusCell Linechemistry.chemical_compoundCapsidVirologyHumansPoint MutationDNA bindingPapillomaviridaeInfectivityCell NucleusVirus AssemblypseudovirionsL1DNA encapsidationMolecular biologyChromatinDNA-Binding ProteinschemistryCapsidCytoplasmDNA ViralchromatinDNANuclear localization sequenceVirology
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Intracellular distribution of the La antigen in CV-1 cells after herpes simplex virus type 1 infection compared with the localization of U small nucl…

1989

The La antigen is known to associate, at least transiently, with a series of small nuclear and cytoplasmic ribonucleoprotein particles (snRNPs and scRNPs), e.g. U1 and U6 snRNPs. In CV-1 cells a monoclonal antibody (MAb), directed against the La protein (La1B5), immunostained intranuclear speckles. These speckles were found to co-localize with speckles that were stained by MAbs directed against either all U snRNPs or only against U1 snRNPs. Two h after infection of CV-1 cells with herpes simplex virus type 1 (HSV-1) (strain HFEM) the staining of nuclear speckles with the anti-La MAb disappeared and the La protein was found quantitatively in the cytoplasm. In contrast nuclear speckles remain…

CytoplasmImmunoblottingFluorescent Antibody TechniqueBiologymedicine.disease_causeenvironment and public healthAutoantigensImmediate early proteinCell LineAntigenVirologymedicineHumansSimplexvirussnRNPRibonucleoproteinCell NucleusAntibodies MonoclonalRibonucleoproteins Small NuclearVirologyMolecular biologyCell nucleusHerpes simplex virusmedicine.anatomical_structureRibonucleoproteinsCytoplasmMutationSmall nuclear ribonucleoproteinTranscription FactorsThe Journal of general virology
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Intracellular route of canine parvovirus entry.

1998

ABSTRACT The present study was designed to investigate the endocytic pathway involved in canine parvovirus (CPV) infection. Reduced temperature (18°C) or the microtubule-depolymerizing drug nocodazole was found to inhibit productive infection of canine A72 cells by CPV and caused CPV to be retained in cytoplasmic vesicles as indicated by immunofluorescence microscopy. Consistent with previously published results, these data indicate that CPV enters a host cell via an endocytic route and further suggest that microtubule-dependent delivery of CPV to late endosomes is required for productive infection. Cytoplasmic microinjection of CPV particles was used to circumvent the endocytosis and membr…

CytoplasmMicroinjectionsParvovirus CanineEndosomeanimal diseasesvirusesImmunologyEndocytic cycleBiologyVirus ReplicationEndocytosisMicrotubulesMicrobiologyCell LineDogsVirologyAnimalsMicroinjectionParvovirusNocodazoleTemperatureCanine parvovirusLipid bilayer fusionbiology.organism_classificationVirologyEndocytosisVirus-Cell InteractionsMicroscopy FluorescenceViral replicationInsect Science
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Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.

2003

The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted with recombinant NS5A protein. Subsequent mass spectrometry identified the adaptor protein amphiphysin II as a novel interaction partner of NS5A. Mutational analysis revealed that complex formation is primarily mediated by a proline-rich region in the C-terminal part of NS5A, which interacts with the amphiphysin II Src homology 3 domain. Importantly, we could further demonstrate specific co-precipitation and cellular co-localization of endogenous a…

CytoplasmProlinevirusesImmunoblottingNerve Tissue ProteinsHepacivirusBiologyProtein Serine-Threonine KinasesViral Nonstructural ProteinsVirus ReplicationSH3 domainVirologyTumor Cells CulturedHumansRepliconNS5AFluorescent Antibody Technique IndirectSubgenomic mRNALeucine ZippersKinasevirus diseasesSignal transducing adaptor proteinbiochemical phenomena metabolism and nutritionMAP Kinase Kinase KinasesRNA-Dependent RNA PolymeraseVirologyMolecular biologydigestive system diseasesRecombinant ProteinsViral replicationMutationPhosphorylationRepliconProtein BindingThe Journal of general virology
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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Cutting edge: priming of CTL by transcutaneous peptide immunization with imiquimod.

2005

Abstract CTL are important in combating cancer and viruses. Therefore, triggering the complete potential of CTL effector functions by new vaccination strategies will not only improve prophylaxis of tumor or virus-related diseases, but also open opportunities for effective therapeutic immunizations. Using transcutaneous immunization, we show that epicutaneous (e.c.)4 application of an ointment containing a CTL epitope and the TLR7 ligand imiquimod is highly effective in activating T cells in mice using TCR-transgenic CTL or in wild-type mice. Transcutaneous immunization-activated CTL mount a full-blown immune response against the target epitope characterized by proliferation, cytolytic activ…

Cytotoxicity ImmunologicAdoptive cell transferImmunologyReceptors Antigen T-CellPriming (immunology)Epitopes T-Lymphocytechemical and pharmacologic phenomenaImiquimodMice TransgenicAdministration CutaneousLymphocyte ActivationResting Phase Cell CycleEpitopeMiceImmune systemmedicineImmunology and AllergyAnimalsCells CulturedMice KnockoutImiquimodbusiness.industryTLR7VirologyAdoptive TransferVaccinationMice Inbred C57BLCTL*Protein TransportImmunologyVaccines SubunitAminoquinolinesLymph NodesbusinessSpleenmedicine.drugT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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H-2-linked murine cytotoxic T cell responses specific for sendai virus-infected cells

1978

CBA (H-2k) mouse-derived lymphochoriomeningitis virus and herpes simplex virus-specific cytotoxic T lymphocytes lyse virus-infected target cells compatible on either the H-2k or H-2D region. In contrast, CBA, C3H and AKR (H-2k) mouse-derived sendai virus-specific cytotoxic T lymphocytes (CTL) fail to lyse H-2D-compatible virus-infected cells. A similar lack of H-2D region-associated lytic activity was found with C57BL/6 and C57BL/10 (H-2b) mice as well as with the recombinants B10.A (2R) [Kb-Db] and B10.A (4R) [Kk-Db]. On the other hand, BALB/c (H-2d) mice and A/J (H-2a) mice do generate H-2Dd-associated sendai virus-specific CTL. These results are in contrast to those obtained with (CBA X …

Cytotoxicity ImmunologicGenotypeT-LymphocytesvirusesImmunologychemical and pharmacologic phenomenaVirusMajor Histocompatibility ComplexEpitopesMiceGenotypeAnimalsLymphocytic choriomeningitis virusSimplexvirusImmunology and AllergyCytotoxic T cellGeneMice Inbred BALB CParamyxoviridae InfectionsbiologyHerpes Simplexbiology.organism_classificationVirologySendai virusParainfluenza Virus 1 HumanMice Inbred C57BLCTL*RickettsiaLytic cycleMice Inbred CBAEuropean Journal of Immunology
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