Search results for "IGE"

showing 10 items of 17476 documents

Rab33B and its autophagic Atg5/12/16L1 effector assist in hepatitis B virus naked capsid formation and release

2015

Hepatitis B virus morphogenesis is accompanied by the production and release of non-enveloped capsids/nucleocapsids. Capsid particles are formed inside the cell cytosol by multimerization of core protein subunits and ultimately exported in an uncommon coatless state. Here, we investigated potential roles of Rab GTPases in capsid formation and trafficking by using RNA interference and overexpression studies. Naked capsid release does not require functions of the endosome-associated Rab5, Rab7 and Rab27 proteins, but depends on functional Rab33B, a GTPase participating in autophagosome formation via interaction with the Atg5-Atg12/Atg16L1 complex. During capsid formation, Rab33B acts in conju…

virusesATG8ImmunologyATG5Autophagybiochemical phenomena metabolism and nutritionBiologyGroup-specific antigenMicrobiologyVirus ReleaseCell biologyATG12CapsidVirologyRabCellular Microbiology
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Infection-induced chromatin modifications facilitate translocation of herpes simplex virus capsids to the inner nuclear membrane

2021

Herpes simplex virus capsids are assembled and packaged in the nucleus and move by diffusion through the nucleoplasm to the nuclear envelope for egress. Analyzing their motion provides conclusions not only on capsid transport but also on the properties of the nuclear environment during infection. We utilized live-cell imaging and single-particle tracking to characterize capsid motion relative to the host chromatin. The data indicate that as the chromatin was marginalized toward the nuclear envelope it presented a restrictive barrier to the capsids. However, later in infection this barrier became more permissive and the probability of capsids to enter the chromatin increased. Thus, although …

virusesGene ExpressionVirus ReplicationPathology and Laboratory Medicineherpes simplex -virusChlorocebus aethiopsCapsidsMedicine and Health SciencesSimplexvirusBiology (General)Mass DiffusivityStainingChromosome BiologyPhysicsChromatinChemistryMedical MicrobiologyViral PathogensPhysical SciencesVirusesHerpes Simplex Virus-1EpigeneticsCellular Structures and OrganellesPathogenskapsidiResearch ArticleHerpesvirusesNuclear EnvelopeQH301-705.5Biological Transport ActiveViral StructureResearch and Analysis MethodsinfektiotMicrobiologydiffuusio (fysikaaliset ilmiöt)CapsidNuclear MembraneVirologyGeneticsAnimalsherpesviruksetVero CellsMicrobial PathogensCell NucleusChemical PhysicsOrganismsBiology and Life SciencesHerpes SimplexCell Biologybiochemical phenomena metabolism and nutritionRC581-607Viral ReplicationHerpes Simplex VirusNuclear StainingSpecimen Preparation and TreatmentImmunologic diseases. AllergyDNA viruses
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Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B

1999

NS5A of the hepatitis C virus (HCV) is a highly phosphorylated protein involved in resistance against interferon and required most likely for replication of the viral genome. Phosphorylation of this protein is mediated by a cellular kinase(s) generating multiple proteins with different electrophoretic mobilities. In the case of the genotype 1b isolate HCV-J, in addition to the basal phosphorylated NS5A (designated pp56), a hyperphosphorylated form (pp58) was found on coexpression of NS4A (T. Kaneko, Y. Tanji, S. Satoh, M. Hijikata, S. Asabe, K. Kimura, and K. Shimotohno, Biochem. Biophys. Res. Commun. 205:320‐326, 1994). Using a comparative analysis of two full-length genomes of genotype 1b…

virusesHepatitis C virusHepacivirusMolecular Sequence DataImmunologyGene ExpressionReplicationHyperphosphorylationGenome ViralHepacivirusViral Nonstructural Proteinsmedicine.disease_causeMicrobiologyCell LineInterferonCricetinaeVirologymedicineAnimalsHumansPhosphorylationNS5ANS3Base SequencebiologyPestivirusvirus diseasesRNAbiochemical phenomena metabolism and nutritionbiology.organism_classificationVirologyMolecular biologydigestive system diseasesAmino Acid SubstitutionInsect ScienceDNA Viralmedicine.drugJournal of Virology
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Functional properties of a monoclonal antibody inhibiting the hepatitis C virus RNA-dependent RNA polymerase.

2001

The hepatitis C virus (HCV) RNA-dependent RNA polymerase (RdRp), represented by nonstructural protein 5B (NS5B), has recently emerged as a promising target for antiviral intervention. Here, we describe the isolation, functional characterization, and molecular cloning of a monoclonal antibody (mAb) inhibiting the HCV RdRp. This mAb, designated 5B-12B7, binds with high affinity to a conformational epitope in the palm subdomain of the HCV RdRp and recognizes native NS5B expressed in the context of the entire HCV polyprotein or subgenomic replicons. Complete inhibition of RdRp activity in vitro was observed at equimolar concentrations of NS5B and mAb 5B-12B7, whereas RdRp activities of classica…

virusesHepatitis C virusMolecular Sequence DataBiologyViral Nonstructural Proteinsmedicine.disease_causeBiochemistryAntiviral AgentsViruschemistry.chemical_compoundMiceRNA polymerasemedicineAnimalsAmino Acid SequenceMolecular BiologyNS5BImmunoglobulin FragmentsPolymeraseSubgenomic mRNAMice Inbred BALB CBase Sequencevirus diseasesRNAAntibodies MonoclonalCell BiologyVirologyMolecular biologydigestive system diseasesEpitope mappingchemistrybiology.proteinFemaleEpitope MappingThe Journal of biological chemistry
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Replication of herpes simplex virus type 1 and 2 in the medulla of the adrenal gland after vaginal infection of mice.

1996

After vaginal infections of mice with neuroinvasive strains of herpes simplex virus type 1 and 2 (HSV-1, HSV-2) virus replicates in the epithelium of the vagina, in the paravaginal ganglia, in the spinal cord and finally in the brain and in the adrenal glands. However, viral antigens could be demonstrated only in the medulla of the adrenal glands but not in the cortex, as assessed by immunohistochemistry (IHC). HSV could not be isolated from liver, spleen, uterus, and ovaries. This contrasts to the intraperitoneal (i.p) route of infection with replication in different visceral organs including the adrenal gland's cortex.

virusesHerpesvirus 2 HumanUterusSpleenHerpesvirus 1 HumanBiologymedicine.disease_causeVirus ReplicationHerpesviridaeVirusMiceVirologyChlorocebus aethiopsmedicineAnimalsHumansAntigens ViralVero CellsMedullaCerebral CortexMice Inbred BALB CAdrenal glandGeneral MedicineVirologymedicine.anatomical_structureHerpes simplex virusSpinal CordAdrenal MedullaVaginaVaginaFemaleArchives of virology
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Generation and neutralization of pseudovirions of human papillomavirus type 33

1997

Since human papillomaviruses (HPV) cannot be propagated in cell culture, the generation of infectious virions in vitro is a highly desirable goal. Here we report that pseudovirions can be generated by the assembly of virus-like particles (VLPs) in COS-7 cells containing multiple copies of a marker plasmid. Using recombinant vaccinia viruses, we have obtained spherical VLPs of HPV type 33 (HPV-33) which fractionate into heavy and light VLPs in cesium chloride density gradients. VLPs in the heavy fraction (1.31 g/cm3) carry the plasmid in DNase-resistant form and are capable of transferring the genetic marker located on the plasmid to COS-7 cells in a DNase-resistant way (pseudoinfection). Th…

virusesImmunologyBiologyAntibodies Viralcomplex mixturesMicrobiologyNeutralizationlaw.inventionchemistry.chemical_compoundCapsidPlasmidNeutralization TestslawVirologyAnimalsDeoxyribonuclease IHumansAntigens ViralPapillomaviridaeAntiserumVirus AssemblyVirionvirus diseasesOncogene Proteins ViralVirologyMolecular biologyIn vitroTiterchemistryCapsidInsect ScienceCOS CellsDNA ViralRecombinant DNACapsid ProteinsDNAResearch ArticleJournal of Virology
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Translocation of the nuclear autoantigen La to the cell surface of herpes simplex virus type 1 infected cells.

1992

Recently we developed a procedure to translocalize one of the extractable nuclear antigens (ENAs), the La protein, to the cell surface of CV-1 cells. Here we report that herpes simplex virus type 1 infection can also induce a translocation of the autoantigen to the cell surface. On the cell surface we detected La protein assembled with large protrusions. Within these protrusions La protein colocalized with virus particles. These protrusions are known to be released from the cell after virus infections. Such complexes consisting of self and virus could provide helper determinants for an anti-self response, and therefore be important in generation of autoimmunity.

virusesImmunologyCellmedicine.disease_causeAutoantigensVirusHerpesviridaeSingle-stranded binding proteinAntigenAlphaherpesvirinaeCricetinaemedicineImmunology and AllergyAnimalsNuclear proteinCells CulturedCell NucleusbiologyAntibodies MonoclonalBiological TransportHerpes Simplexbiology.organism_classificationBlood Physiological PhenomenaVirologymedicine.anatomical_structureHerpes simplex virusRibonucleoproteinsbiology.proteinAutoimmunity
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The human autoantigen La/SS-B accelerates herpes simplex virus type 1 replication in transfected mouse 3T3 cells.

1998

SUMMARY Permanently transfected mouse cell lines which expressed different levels of the human autoantigen La/SS-B were infected with different strains of herpes simplex virus type 1, including the strains ANG, HSZP, 17syn+ and HFEM. During infection the localization of the human La protein was followed using an anti-La MoAb, which recognized only the human La protein but did not cross-react with either the endogenous mouse La protein or any viral encoded protein. After infection La protein was transported from the nucleus to the cytoplasm. The time course of translocation was dependent on the amount of human La protein expressed in the respective cell line. Moreover, acceleration of viral …

virusesImmunologyHerpesvirus 1 Humanmedicine.disease_causeTransfectionVirus ReplicationAutoantigensVirus3T3 cellsSingle-stranded binding proteinMicemedicineImmunology and AllergyAnimalsHumansbiologyTransfection3T3 CellsOriginal ArticlesHerpes simplex virusmedicine.anatomical_structureViral replicationGene Expression RegulationRibonucleoproteinsCytoplasmCell cultureImmunologybiology.proteinClinical and experimental immunology
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Rapid and sensitive detection of metapneumovirus in clinical specimens by indirect fluorescence assay using a monoclonal antibody.

2008

Human metapneumovirus, with two known genotypes named A and B, is associated with mild respiratory symptoms to severe LRTI in children, high-risk adults and the elderly. Rapid and reliable methods of hMPV detection in clinical samples are essential to implement appropriate care, to better understand the pathology of hMPV and to determine its epidemiology. Respiratory samples from 1,386 patients collected during 2 consecutive years were screened for hMPV using indirect immunofluorescence (IFA) assay with a monoclonal antibody. Forty-three patients tested positive for hMPV by the IFA method. In parallel, the samples were examined with RT-PCR on the F gene. Of these, 41 specimens were RT-PCR p…

virusesMESH : AgedMESH : Respiratory Tract InfectionsMESH : Fluorescent Antibody Technique IndirectFusion geneMiceMESH : ChildGenotypeMetapneumovirusRespiratory systemChildFluorescent Antibody Technique IndirectAntigens ViralRespiratory Tract InfectionsCells CulturedComputingMilieux_MISCELLANEOUS[SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/VirologyMice Inbred BALB CParamyxoviridae Infectionsmedicine.diagnostic_testbiologyAntibodies Monoclonalvirus diseasesMESH : AdultInfectious DiseasesMESH : Antibodies MonoclonalMESH : Sensitivity and SpecificityAdultmedicine.drug_classMonoclonal antibodyImmunofluorescenceSensitivity and Specificity[ SDV.MP.VIR ] Life Sciences [q-bio]/Microbiology and Parasitology/VirologyVirusHuman metapneumovirusVirologyMESH : MiceMESH : Cells CulturedmedicineAnimalsHumansMESH : Mice Inbred BALB CAgedMESH : HumansMESH : Antigens ViralMESH : Paramyxoviridae Infectionsbiology.organism_classificationVirologyrespiratory tract diseasesMESH : MetapneumovirusMetapneumovirusMESH : Animals
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In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

1996

AbstractProteolytic processing of the nonstructural proteins of the hepatitis C virus (HCV) is mediated by two viral proteinases: the NS2-3 proteinase cleaving at the NS2/3 junction and the NS3 serine-type proteinase responsible for processing at the NS3/4A, NS4A/B, NS4B/5A, and NS5A/B sites. Activity of the NS3 proteinase is modulated by NS4A. In the absence of this cofactor processing at the NS3-dependent sites does not occur or, in the case of the NS5A/B junction, is poor but increased when NS4A is present. Although recent studies demonstrated that proteinase activation requires direct interaction between NS3 and NS4A, the mechanism by which NS4A exerts the activation function is not kno…

virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsCell LineEnzyme activatorProteinase 3VirologyCricetinaeMicrosomesAnimalsHumansAmino Acid SequenceBinding siteNS5APeptide sequenceSequence Deletionchemistry.chemical_classificationNS3Binding SitesBase Sequencevirus diseasesIntracellular Membranesbiochemical phenomena metabolism and nutritionMolecular biologyIn vitrodigestive system diseasesAmino acidEnzyme ActivationBiochemistrychemistryDNA ViralPeptidesHeLa CellsVirology
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