Search results for "Virus-Cell Interactions"

showing 10 items of 50 documents

Extracellular Albumin and Endosomal Ions Prime Enterovirus Particles for Uncoating That Can Be Prevented by Fatty Acid Saturation

2019

ABSTRACT There is limited information about the molecular triggers leading to the uncoating of enteroviruses under physiological conditions. Using real-time spectroscopy and sucrose gradients with radioactively labeled virus, we show at 37°C, the formation of albumin-triggered, metastable uncoating intermediate of echovirus 1 without receptor engagement. This conversion was blocked by saturating the albumin with fatty acids. High potassium but low sodium and calcium concentrations, mimicking the endosomal environment, also induced the formation of a metastable uncoating intermediate of echovirus 1. Together, these factors boosted the formation of the uncoating intermediate, and the infectiv…

Models MolecularEchovirusHot TemperatureEndosomevirusesImmunologycryoEM structurerasvahapotEndosomesBiologymedicine.disease_causeMicrobiologyDivalentCell Line03 medical and health sciencesVirologyAlbuminsChlorocebus aethiopsExtracellularmedicineAnimalsalbumin030304 developmental biologychemistry.chemical_classificationalbumiinit0303 health sciencesbiokemiaionitenterovirus030302 biochemistry & molecular biologyCryoelectron MicroscopyFatty AcidsFatty acidRNAVirus-Cell InteractionsEnterovirus B HumanenteroviruksetchemistryCapsidvirologia13. Climate actionInsect ScienceBiophysicsCapsid ProteinsuncoatingLow sodium
researchProduct

Membrane Integration of Poliovirus 2B Viroporin

2011

Virus infections can result in a variety of cellular injuries, and these often involve the permeabilization of host membranes by viral proteins of the viroporin family. Prototypical viroporin 2B is responsible for the alterations in host cell membrane permeability that take place in enterovirus-infected cells. 2B protein can be localized at the endoplasmic reticulum (ER) and the Golgi complex, inducing membrane remodeling and the blockade of glycoprotein trafficking. These findings suggest that 2B has the potential to integrate into the ER membrane, but specific information regarding its biogenesis and mechanism of membrane insertion is lacking. Here, we report experimental results of in vi…

Models MolecularFarmacologiaVesicle-associated membrane protein 8MedicinaMolecular Sequence DataImmunologyPorinsViral Nonstructural ProteinsEndoplasmic ReticulumModels BiologicalMicrobiologyAmino acid sequencesymbols.namesakeMolecular sequence dataCricetinaeVirologyAnimalsAmino Acid SequenceIntegral membrane proteinCells CulturedSequence DeletionHost cell membranebiologyMembrane transport proteinEndoplasmic reticulumGolgi apparatusBiología y Biomedicina / BiologíaVirusVirus-Cell InteractionsCell biologyPoliovirusMembraneBiochemistryCytoplasmInsect Sciencesymbolsbiology.proteinJournal of Virology
researchProduct

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
researchProduct

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
researchProduct

Reorganization of Nuclear Pore Complexes and the Lamina in Late-Stage Parvovirus Infection

2015

Article

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
researchProduct

Exploitation of Microtubule Cytoskeleton and Dynein during Parvoviral Traffic toward the Nucleus

2003

ABSTRACT Canine parvovirus (CPV), a model virus for the study of parvoviral entry, enters host cells by receptor-mediated endocytosis, escapes from endosomal vesicles to the cytosol, and then replicates in the nucleus. We examined the role of the microtubule (MT)-mediated cytoplasmic trafficking of viral particles toward the nucleus. Immunofluorescence and immunoelectron microscopy showed that capsids were transported through the cytoplasm into the nucleus after cytoplasmic microinjection but that in the presence of MT-depolymerizing agents, viral capsids were unable to reach the nucleus. The nuclear accumulation of capsids was also reduced by microinjection of an anti-dynein antibody. More…

Parvovirus CaninevirusesImmunoelectron microscopyImmunologyDyneinActive Transport Cell Nucleusmacromolecular substancesMicrotubulesMicrobiologyMotor proteinCapsidCytosolMicrotubuleVirologymedicineAnimalsCytoskeletonCytoskeletonCell NucleusbiologyDyneinsbiochemical phenomena metabolism and nutritionVirus-Cell InteractionsCell biologyMicroscopy ElectronTubulinmedicine.anatomical_structureCytoplasmInsect ScienceCatsbiology.proteinNucleusJournal of Virology
researchProduct

Entry of Human Parechovirus 1

2001

ABSTRACT Human parechovirus 1 (HPEV-1) is a prototype member of parechoviruses, a recently established picornavirus genus. Although there is preliminary evidence that HPEV-1 recognizes α V integrins as cellular receptors, our understanding of early events during HPEV-1 infection is still very limited. The aim of this study was to clarify the entry mechanisms of HPEV-1, including the attachment of the virus onto the host cell surface and subsequent internalization. In blocking experiments with monoclonal antibodies against different receptor candidates, antibodies against α V and β 3 integrin subunits, in particular in combination, appeared to be the most efficient ones in preventing the HPE…

PicornavirusEndosomeImmunologyEndocytic cycleGolgi ApparatusHuman parechovirus 1EndosomesPicornaviridaePlatelet Membrane GlycoproteinsEndoplasmic ReticulumVirus ReplicationCaveolinsMicrobiologyClathrinEEA103 medical and health sciencessymbols.namesakeCapsidAntigens CDVirologyTumor Cells CulturedHumans030304 developmental biologyHost cell surface0303 health sciencesbiology030302 biochemistry & molecular biologyIntegrin beta3Clathrin-Coated VesiclesIntegrin alphaVGolgi apparatusbiology.organism_classificationVirologyClathrinEndocytosisVirus-Cell Interactions3. Good healthCell biologyInsect Sciencesymbolsbiology.proteinReceptors VirusJournal of Virology
researchProduct

Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1▿

2007

ABSTRACT Calpains are calcium-dependent cysteine proteases that degrade cytoskeletal and cytoplasmic proteins. We have studied the role of calpains in the life cycle of human echovirus 1 (EV1). The calpain inhibitors, including calpeptin, calpain inhibitor 1, and calpain inhibitor 2 as well as calpain 1 and calpain 2 short interfering RNAs, completely blocked EV1 infection in the host cells. The effect of the inhibitors was not specific for EV1, because they also inhibited infection by other picornaviruses, namely, human parechovirus 1 and coxsackievirus B3. The importance of the calpains in EV1 infection also was supported by the fact that EV1 increased calpain activity 3 h postinfection. …

ProteasesImmunoelectron microscopyImmunologyParechovirusVirus ReplicationMicrobiologyCell LineViral entryVirologyHumansGene SilencingEnzyme InhibitorsMicroscopy ImmunoelectronMicroscopy ConfocalbiologyCalpainCytoplasmic VesiclesRNACalpainMolecular biologyCell biologyVirus-Cell InteractionsEnterovirus B HumanViral replicationCell cultureInsect ScienceCalpain-2biology.proteinRNA Viral
researchProduct

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
researchProduct

The Abundant Tegument Protein pUL25 of Human Cytomegalovirus Prevents Proteasomal Degradation of pUL26 and Supports Its Suppression of ISGylation

2018

The tegument of human cytomegalovirus (HCMV) virions contains proteins that interfere with both the intrinsic and the innate immunity. One protein with a thus far unknown function is pUL25. The deletion of pUL25 in a viral mutant (Towne-ΔUL25) had no impact on the release of virions and subviral dense bodies or on virion morphogenesis. Proteomic analyses showed few alterations in the overall protein composition of extracellular particles. A surprising result, however, was the almost complete absence of pUL26 in virions and dense bodies of Towne-ΔUL25 and a reduction of the large isoform pUL26-p27 in mutant virus-infected cells. pUL26 had been shown to inhibit protein conjugation with the in…

Proteomics0301 basic medicineIntrinsic immunityHuman cytomegalovirusImmunoprecipitationvirusesImmunologyMutantCytomegalovirusBiologyVirus ReplicationMicrobiologyViral Matrix ProteinsViral Proteins03 medical and health sciencesInterferonVirologymedicineHumansUbiquitinsCells CulturedInnate immune systemvirus diseasesViral tegumentFibroblastsbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseISG15Immunity InnateVirus-Cell InteractionsCell biology030104 developmental biologyInsect ScienceMutationProteolysisCytokinesmedicine.drugJournal of Virology
researchProduct