Search results for " envelope"

showing 10 items of 253 documents

Deletions in the hepatitis B virus small envelope protein: effect on assembly and secretion of surface antigen particles

1992

The small envelope S protein of hepatitis B virus carrying the surface antigen has the unique property of mobilizing cellular lipids into empty envelope particles which are secreted from mammalian cells. We studied the biogenesis of such particles using site-directed mutagenesis. In this study, we describe the effect of deletions in the N-terminal hydrophobic and hydrophilic domains of the S protein. Whereas short overlapping deletions of hydrophilic sequences flanking the first hydrophobic domain were tolerated, larger deletions of the same sequences were not. Conversely, the hydrophilic region preceding the second hydrophobic domain was not permissive for even short deletions. Deletion of…

Hepatitis B virusMolecular Sequence DataImmunologyMutantMutagenesis (molecular biology technique)Biologymedicine.disease_causeMicrobiologyViral Envelope ProteinsViral envelopeVirologymedicineInterleukin 9SecretionCloning MolecularCells CulturedSecretory pathwayMutationHepatitis B Surface AntigensBase SequenceTunicamycinEndoplasmic reticulumPrecipitin TestsMolecular biologyInsect ScienceMutagenesis Site-DirectedChromosome DeletionPlasmidsResearch ArticleJournal of Virology
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Chaperones Involved in Hepatitis B Virus Morphogenesis

1999

Little is known about host cell factors necessary for hepatitis B virus (HBV) assembly which involves envelopment of cytosolic nucleocapsids by the S, M and L transmembrane viral envelope proteins and subsequent budding into intraluminal cisternae. Central to virogenesis is the L protein that mediates hepatocyte receptor binding and envelopment of capsids. To serve these topologically conflicting roles, L protein exhibits an unusual dual membrane topology, disposing its N-terminal preS domain inside and outside of the virion lipid envelope. The mixed topology is achieved by posttranslational preS translocation of about half of the L protein molecules across a post-endoplasmic reticulum memb…

Hepatitis B virusProtein FoldingCalnexinHSC70 Heat-Shock ProteinsClinical BiochemistryBiochemistryViral Matrix ProteinsCytosolViral Envelope ProteinsViral envelopeCalnexinMorphogenesisAnimalsHumansHSP70 Heat-Shock ProteinsProtein PrecursorsMolecular BiologyHepatitis B Surface AntigensViral matrix proteinbiologyChemistryCalcium-Binding ProteinsHSC70 Heat-Shock ProteinsBiological TransportVirologyTransmembrane proteinCell biologyProtein BiosynthesisMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein foldingCarrier ProteinsMolecular ChaperonesBiological Chemistry
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Functional incorporation of green fluorescent protein into hepatitis B virus envelope particles

2004

AbstractThe envelope of hepatitis B virus (HBV), containing the L, M, and S proteins, is essential for virus entry and maturation. For direct visualization of HBV, we determined whether envelope assembly could accommodate the green fluorescent protein (GFP). While the C-terminal addition of GFP to S trans-dominant negatively inhibited empty envelope particle secretion, the N-terminal GFP fusion to S (GFP.S) was co-integrated into the envelope, giving rise to fluorescent particles. Microscopy and topogenesis analyses demonstrated that the proper intracellular distribution and folding of GFP.S, required for particle export were rescued by interprotein interactions with wild-type S. Thereby, a…

Hepatitis B virusRecombinant Fusion ProteinsGreen Fluorescent ProteinsRestriction MappingEnzyme-Linked Immunosorbent AssayBiologyTransfectionmedicine.disease_causeHBsAg particlesArticleViral envelopeGreen fluorescent proteinViral Envelope ProteinsViral envelopeViral entryVirologyChlorocebus aethiopsmedicineAnimalsHumansGreen fluorescent proteinSecretionPromoter Regions GeneticHepatitis B virusCOS cellsfungiTransfectionMolecular biologyCell biologyKineticsCOS CellsMetallothioneinVirus assembly and secretionProtein KinasesIntracellularVirology
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Hepatitis B virus assembly is sensitive to changes in the cytosolic S loop of the envelope proteins.

2000

Among the three related L, M, and S envelope proteins of the hepatitis B virus (HBV), the L and S polypeptides are required for virion production. Whereas the pivotal function of the pre-S region of L in nucleocapsid envelopment has been established, the contribution of its S domain and the S protein is less clear. In this study, we evaluated the role of the cytosolic S loop, common to L and S, in HBV assembly by performing mutagenesis experiments. To distinguish between the effect of the mutations on either envelope or virion formation, we investigated the ability of the mutants to assemble into secretable subviral empty envelopes and to replace the wild-type proteins in virion maturation,…

Hepatitis B virusRecombination GeneticMutationHepatitis B virusvirusesVirus AssemblyMutantMolecular Sequence DataMorphogenesisMutagenesis (molecular biology technique)Biologymedicine.disease_causeVirologyCell biologyLoop (topology)CytosolCytosolViral Envelope ProteinsSequence Analysis ProteinVirologymedicineMutagenesis Site-DirectedHumansAmino Acid SequenceFunction (biology)Virology
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Hepatitis B Virus Large Envelope Protein Interacts with γ2-Adaptin, a Clathrin Adaptor-Related Protein

2001

ABSTRACT For the outcome of a hepatitis B virus (HBV) infection, the viral L envelope protein with its pre-S domain performs pivotal functions by mediating attachment of HBV to liver cells, envelopment of viral capsids, release of (sub)viral particles, regulation of supercoiled DNA amplification, and transcriptional transactivation. To assess its multiple functions and host-protein assistance involved, we initiated a two-hybrid screen using the L-specific pre-S1 domain as bait. With this approach, we have identified γ2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein. Evidence for a physic…

Hepatitis B virusVesicle-associated membrane protein 8ImmunoprecipitationImmunologyGolgi ApparatusTransfectionmedicine.disease_causeMicrobiologyClathrinChromatography AffinityCytosolViral Envelope ProteinsMutant proteinYeastsVirologyProtein targetingmedicineAnimalsBinding siteAdaptor Protein Complex gamma SubunitsBinding SitesbiologyMembrane ProteinsPrecipitin TestsClathrinTransmembrane proteinVirus-Cell InteractionsCell biologyInsect ScienceCOS CellsMutationbiology.proteinClathrin adaptor proteinsProtein BindingJournal of Virology
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Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.

2008

AbstractThe hepatitis B virus L protein forms a dual topology in the endoplasmic reticulum (ER) via a process involving cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain. Here, we show that preS posttranslocation depends on the action of the ER chaperone BiP. To modulate the in vivo BiP activity, we designed an approach based on overexpressing its positive and negative regulators, ER-localized DnaJ-domain containing protein 4 (ERdj4) and BiP-associated protein (BAP), respectively. The feasibility of this approach was confirmed by demonstrating that BAP, but not ERdj4, destabilizes the L/BiP complex. Overexpressing BAP or ERdj4 inhibits…

Hepatitis B virusgenetic structuresBiPBiophysicsHemagglutinin (influenza)Chromosomal translocationmacromolecular substancesmedicine.disease_causeEndoplasmic ReticulumBiochemistryCell LineAdenosine TriphosphateViral Envelope ProteinsStructural BiologyIn vivoCalnexinHBVGeneticsmedicineHumansMolecular BiologyEndoplasmic Reticulum Chaperone BiPTranslocational regulationHeat-Shock ProteinsHepatitis B virusbiologyEndoplasmic reticulumMembrane ProteinsCell BiologyHSP40 Heat-Shock ProteinsMolecular biologyProtein Structure TertiaryProtein TransportDual topologyMembrane topologyProtein BiosynthesisMembrane topologybiology.proteinPosttranslational translocationMolecular ChaperonesFEBS letters
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Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins

1991

The envelope of hepatitis B virus contains three related proteins, one of which is myristylated. The nonmyristylated small and middle protein are assembled into empty envelope particles which are secreted from cells, whereas the myristylated large envelope protein is mainly found in complete virions and is not secreted in the absence of the nucleocapsid. The block to secretion can be partially overcome by mutation or deletion of the myristylation site. Creation of a myristyl attachment site in the small protein impairs the secretion of empty envelope particles but not their intracellular assembly. Myristylation may therefore play a crucial role in hepatitis B virus replication by channeling…

Hepatitis B virusvirusesDNA Mutational AnalysisImmunologyIn Vitro TechniquesBiologyVirus Replicationmedicine.disease_causeMyristic AcidMicrobiologyVirusStructure-Activity RelationshipCapsidViral Envelope ProteinsViral envelopeVirologymedicineHumansSecretionProtein PrecursorsHepatitis B virusMutationHepatitis B Surface Antigensbiology.organism_classificationVirologyCell CompartmentationMolecular WeightCapsidHepadnaviridaeViral replicationInsect ScienceMyristic AcidsProtein Processing Post-TranslationalResearch ArticleJournal of Virology
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Refined analysis of genetic variability parameters in hepatitis C virus and the ability to predict antiviral treatment response.

2008

Summary.  Hepatitis C virus (HCV) infects approximately 3% of the world population. The chronicity of hepatitis C seems to depend on the level of genetic variability. We have recently (Torres-Puente et al., J Viral Hepat, 2008; 15: 188) reported genetic variability estimates from a large-scale sequence analysis of 67 patients infected with HCV subtypes 1a (23 patients) and 1b (44 patients) and related them to response, or lack of, to alpha-interferon plus ribavirin treatment.. Two HCV genome regions were analysed in samples prior to antiviral therapy, one compressing the three hypervariable regions of the E2 glycoprotein and another one including the interferon sensitive determining region …

Hepatitis C virusMutation MissenseAlpha interferonHepacivirusBiologyViral Nonstructural Proteinsmedicine.disease_causeAntiviral AgentsNucleotide diversityViral Envelope ProteinsVirologyDrug Resistance ViralRibavirinmedicineHumansGenetic variabilityNS5AGeneticsHepatologyHaplotypeGenetic VariationHepatitis CHepatitis C Chronicmedicine.diseaseVirologyHypervariable regionInfectious DiseasesTreatment OutcomeHaplotypesInterferonsJournal of viral hepatitis
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Correlated optical/X-ray variability in the high-mass X-ray binary SAX J2103.5+4545

2009

SAX J2103.5+4545 is the Be/X-ray binary with the shortest orbital period. It shows extended bright and faint X-ray states that last for a few hundred days. The main objective of this work is to investigate the relationship between the X-ray and optical variability and to characterise the spectral and timing properties of the bright and faint states. We have found a correlation between the spectral and temporal parameters that fit the energy and power spectra. Softer energy spectra correspond to softer power spectra. That is to say, when the energy spectrum is soft the power at high frequencies is suppressed. We also present the results of our monitoring of the Halpha line of the optical cou…

High Energy Astrophysical Phenomena (astro-ph.HE)Physics010308 nuclear & particles physicsAstrophysics::High Energy Astrophysical PhenomenaX-rayX-ray binaryFOS: Physical sciencesBinary numberAstronomy and AstrophysicsAstrophysics::Cosmology and Extragalactic AstrophysicsCircumstellar envelopeAstrophysicsOrbital period01 natural sciencesSpectral lineNeutron starSpace and Planetary Science0103 physical sciencesAstrophysics::Solar and Stellar AstrophysicsAstrophysics - High Energy Astrophysical Phenomena010303 astronomy & astrophysicsAstrophysics::Galaxy AstrophysicsLine (formation)Monthly Notices of the Royal Astronomical Society
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Numerical models of blackbody-dominated gamma-ray bursts – I. Hydrodynamics and the origin of the thermal emission

2014

GRB 101225A is a prototype of the class of blackbody-dominated (BBD) gamma-ray bursts (GRBs). It has been suggested that BBD-GRBs result from the merger of a binary system formed by a neutron star and the helium core of an evolved star. We have modelled the propagation of ultrarelativistic jets through the environment left behind the merger by means of relativistic hydrodynamic simulations. In this paper, the output of our numerical models is post-processed to obtain the (thermal) radiative signature of the resulting outflow. We outline the most relevant dynamical details of the jet propagation and connect them to the generation of thermal radiation in GRB events akin to that of GRB 101225A…

High Energy Astrophysical Phenomena (astro-ph.HE)PhysicsJet (fluid)010308 nuclear & particles physicsAstrophysics::High Energy Astrophysical PhenomenaFOS: Physical sciencesAstronomyAstronomy and AstrophysicsAstrophysics::Cosmology and Extragalactic AstrophysicsAstrophysicsLight curve01 natural sciencesAfterglowNeutron starCommon envelopeSpace and Planetary ScienceThermal radiation0103 physical sciencesRadiative transferAstrophysics::Solar and Stellar AstrophysicsAstrophysics - High Energy Astrophysical PhenomenaGamma-ray burst010303 astronomy & astrophysicsAstrophysics::Galaxy AstrophysicsMonthly Notices of the Royal Astronomical Society
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