Search results for "Virus-Cell Interactions"

showing 10 items of 50 documents

Tetraspanin CD151 Mediates Papillomavirus Type 16 Endocytosis

2013

ABSTRACT Human papillomavirus type 16 (HPV16) is the primary etiologic agent for cervical cancer. The infectious entry of HPV16 into cells occurs via a so-far poorly characterized clathrin- and caveolin-independent endocytic pathway, which involves tetraspanin proteins and actin. In this study, we investigated the specific role of the tetraspanin CD151 in the early steps of HPV16 infection. We show that surface-bound HPV16 moves together with CD151 within the plane of the membrane before they cointernalize into endosomes. Depletion of endogenous CD151 did not affect binding of viral particles to cells but resulted in reduction of HPV16 endocytosis. HPV16 uptake is dependent on the C-termina…

Small interfering RNAEndosomevirusesmedia_common.quotation_subjectDNA Mutational AnalysisImmunologyEndocytic cycleIntegrinTetraspanin 24EndocytosisMicrobiologyClathrinCell LineTetraspaninVirologyHumansInternalizationmedia_commonHuman papillomavirus 16integumentary systembiologyvirus diseasesVirus InternalizationMolecular biologyEndocytosisfemale genital diseases and pregnancy complicationsVirus-Cell InteractionsCell biologyGene Knockdown TechniquesInsect Sciencebiology.proteinMutant ProteinsJournal of Virology
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Internalization of coxsackievirus A9 is mediated by {beta}2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin.

2010

ABSTRACT Coxsackievirus A9 (CAV9) is a member of the human enterovirus B species within the Enterovirus genus of the family Picornaviridae . It has been shown to utilize αV integrins, particularly αVβ6, as its receptors. The endocytic pathway by which CAV9 enters human cells after the initial attachment to the cell surface has so far been unknown. Here, we present a systematic study concerning the internalization mechanism of CAV9 to A549 human lung carcinoma cells. The small interfering RNA (siRNA) silencing of integrin β6 subunit inhibited virus proliferation, confirming that αVβ6 mediates the CAV9 infection. However, siRNAs against integrin-linked signaling molecules, such as Src, Fyn, R…

Small interfering RNAmedia_common.quotation_subjectImmunologyEndocytic cycleIntegrinCaveolin 1CoxsackievirusEndocytosisCaveolaeMicrobiologyClathrinAmilorideDynamin IIVirologyCell Line TumorHumansRNA Small InterferingInternalizationmedia_commonDynaminbiologyADP-Ribosylation FactorsVirus Internalizationbiology.organism_classificationMolecular biologyClathrinEndocytosisCell biologyEnterovirus B HumanVirus-Cell InteractionsADP-Ribosylation Factor 6Insect Sciencebiology.proteinPinocytosisbeta 2-MicroglobulinJournal of virology
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CD8 T Cells Control Cytomegalovirus Latency by Epitope-Specific Sensing of Transcriptional Reactivation

2006

ABSTRACT During murine cytomegalovirus (mCMV) latency in the lungs, most of the viral genomes are transcriptionally silent at the major immediate-early locus, but rare and stochastic episodes of desilencing lead to the expression of IE1 transcripts. This low-frequency but perpetual expression is accompanied by an activation of lung-resident effector-memory CD8 T cells specific for the antigenic peptide 168-YPHFMPTNL-176, which is derivedfrom the IE1 protein. These molecular and immunological findings were combined in the “silencing/desilencing and immune sensing hypothesis” of cytomegalovirus latency and reactivation. This hypothesis proposes that IE1 gene expression proceeds to cell surfac…

Transcriptional ActivationMuromegalovirusvirusesImmunologyAntigen presentationCD8-Positive T-LymphocytesVirus ReplicationMajor histocompatibility complexModels BiologicalMicrobiologyEpitopeImmediate-Early ProteinsEpitopesImmunocompromised HostMiceAntigenVirologyMHC class IVirus latencymedicineAnimalsGene silencingCytotoxic T cellAmino Acid SequenceAntigens ViralLungBone Marrow TransplantationMice Inbred BALB CBase Sequencebiologyvirus diseasesHerpesviridae Infectionsbiochemical phenomena metabolism and nutritionmedicine.diseaseVirologyMolecular biologyVirus LatencyVirus-Cell InteractionsPhenotypeAmino Acid SubstitutionInsect ScienceDNA ViralMutagenesis Site-DirectedTrans-Activatorsbiology.proteinFemaleJournal of Virology
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Coxsackievirus B3-Induced Cellular Protrusions: Structural Characteristics and Functional Competence▿†

2011

ABSTRACT Virus-induced alterations in cell morphology play important roles in the viral life cycle. To examine the intracellular events of coxsackievirus B3 (CVB3) infection, green monkey kidney (GMK) cells were either inoculated with the virus or transfected with the viral RNA. Various microscopic and flow cytometric approaches demonstrated the emergence of CVB3 capsid proteins at 8 h posttransfection, followed by morphological transformation of the cells. The morphological changes included formation of membranous protrusions containing viral capsids, together with microtubules and actin. Translocation of viral capsids into these protrusions was sensitive to cytochalasin D, suggesting the …

Viral proteinvirusesImmunologyCellBiologymedicine.disease_causeKidneyMicrobiologyVirusCell Linechemistry.chemical_compoundViral ProteinsImaging Three-DimensionalViral entryVirologymedicineEnterovirus InfectionsAnimalsHumansActinCytochalasin DTransfectionMolecular biologyCell biologyVirus-Cell InteractionsEnterovirus B HumanMicroscopy Electronmedicine.anatomical_structurechemistryInsect ScienceCapsid ProteinsIntracellular
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Membrane Insertion and Biogenesis of the Turnip Crinkle Virus p9 Movement Protein

2010

ABSTRACT Plant viral infection and spread depends on the successful introduction of a virus into a cell of a compatible host, followed by replication and cell-to-cell transport. The movement proteins (MPs) p8 and p9 of Turnip crinkle virus are required for cell-to-cell movement of the virus. We have examined the membrane association of p9 and found that it is an integral membrane protein with a defined topology in the endoplasmic reticulum (ER) membrane. Furthermore, we have used a site-specific photo-cross-linking strategy to study the membrane integration of the protein at the initial stages of its biosynthetic process. This process is cotranslational and proceeds through the signal recog…

VirologiavirusesImmunologyEndoplasmic ReticulumMicrobiologyVirusMembranes (Biologia)VirologyMovement proteinIntegral membrane proteinSignal recognition particlebiologyTurnip crinkle virusEndoplasmic reticulumProteïnes de membranaMembrane Proteinsbiology.organism_classificationVirus-Cell InteractionsVirusCell biologyPlant Viral Movement ProteinsMembrane proteinBiochemistryInsect ScienceBiosynthetic processCarmovirusSignal Recognition ParticleJournal of Virology
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Epigenetic Status of an Adenovirus Type 12 Transgenome upon Long-Term Cultivation in Hamster Cells

2007

ABSTRACT The epigenetic status of integrated adenovirus type 12 (Ad12) DNA in hamster cells cultivated for about 4 decades has been investigated. Cell line TR12, a fibroblastic revertant of the Ad12-transformed epitheloid hamster cell line T637 with 15 copies of integrated Ad12 DNA, carries one Ad12 DNA copy plus a 3.9-kbp fragment from a second copy. The cellular insertion site for the Ad12 integrate, identical in both cell lines, is a >5.2-kbp inverted DNA repeat. The Ad12 transgenome is packaged around nucleosomes. The cellular junction is more sensitive to micrococcal nuclease at Ad12-occupied sites than at unoccupied sites. Bisulfite sequencing reveals complete de novo methylation i…

Virus CultivationTranscription GeneticVirus IntegrationvirusesImmunologyBisulfite sequencingHamsterMicrobiologyAdenoviridaeCell LineEpigenesis GeneticHistoneschemistry.chemical_compoundEpigenetics of physical exerciseProvirusesCricetinaeVirologyAnimalsMicrococcal NucleaseNucleosomeMethylated DNA immunoprecipitationEpigeneticsCell Line TransformedbiologyAcetylationDNADNA Methylationbiochemical phenomena metabolism and nutritionMolecular biologyVirus-Cell InteractionsNucleosomesstomatognathic diseaseschemistryInsect ScienceDNA Viralbiology.proteinDNAMicrococcal nucleaseJournal of Virology
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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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Human Enterovirus Group B Viruses Rely on Vimentin Dynamics for Efficient Processing of Viral Nonstructural Proteins.

2019

A virus needs the host cell in order to replicate and produce new progeny viruses. For this, the virus takes over the host cell and modifies it to become a factory for viral proteins. Irrespective of the specific virus family, these proteins can be divided into structural and nonstructural proteins. Structural proteins are the building blocks for the new progeny virions, whereas the nonstructural proteins orchestrate the takeover of the host cell and its functions. Here, we have shown a mechanism that viruses exploit in order to regulate the host cell. We show that viral protein synthesis induces vimentin cages, which promote production of specific viral proteins that eventually control apo…

enterovirusvirusesDNA Helicasesapoptosispolyprotein processingViral Nonstructural ProteinsEnterovirus B HumanVirus-Cell InteractionsRNA Recognition Motif ProteinsvimentinA549 CellsProtein BiosynthesisHumansproteasesHSP90 Heat-Shock ProteinsPoly-ADP-Ribose Binding ProteinsRNA HelicasesHeLa CellsJournal of virology
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Human Papillomavirus Types 16, 18, and 31 Share Similar Endocytic Requirements for Entry

2013

ABSTRACT Human papillomavirus type 18 (HPV18), one of the HPVs with malignant potential, enters cells by an unknown endocytic mechanism. The key cellular requirements for HPV18 endocytosis were tested in comparison to those for HPV16 and -31 endocytoses. HPV18 (like HPV16 and -31) entry was independent of clathrin, caveolin, dynamin, and lipid rafts but required actin polymerization and tetraspanin CD151, and the viruses were routed to the same LAMP-1-positive compartment. Hence, the viruses shared similar cellular requirements for endocytic entry.

virusesImmunologyEndocytic cycleTetraspanin 24EndocytosisMicrobiologyClathrinDynamin IIPolymerizationDynamin IIMembrane MicrodomainsTetraspaninVirologyCaveolinHumansHuman papillomavirus 31Lipid raftDynaminHuman papillomavirus 16Microscopy ConfocalHuman papillomavirus 18biologyvirus diseasesLysosome-Associated Membrane GlycoproteinsVirus InternalizationVirologyActinsEndocytosisVirus-Cell InteractionsCell biologyMicroscopy ElectronMicroscopy FluorescenceInsect Sciencebiology.proteinElectrophoresis Polyacrylamide GelHeLa CellsJournal of Virology
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Impact of VP1-Specific Protein Sequence Motifs on Adeno-Associated Virus Type 2 Intracellular Trafficking and Nuclear Entry

2012

ABSTRACT Adeno-associated virus type 2 (AAV2) has gained much interest as a gene delivery vector. A hallmark of AAV2-mediated gene transfer is an intracellular conformational change of the virus capsid, leading to the exposure of infection-relevant protein domains. These protein domains, which are located on the N-terminal portion of the structural proteins VP1 and VP2, include a catalytic phospholipase A 2 domain and three clusters of basic amino acids. We have identified additional protein sequence motifs located on the VP1/2 N terminus that also proved to be obligatory for virus infectivity. These motifs include signals that are known to be involved in protein interaction, endosomal sort…

virusesImmunologyProtein domainAmino Acid MotifsMolecular Sequence DataSequence alignmentBiologyMicrobiologyVirusCell LineParvoviridae InfectionsVirologyHumansAmino Acid SequenceAdeno-Associated Virus Type 2Peptide sequenceCell NucleusDependovirusMolecular biologyTransport proteinCell biologyVirus-Cell InteractionsProtein TransportCapsidInsect ScienceCapsid ProteinsSequence motifSequence Alignment
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