Search results for "Virus Assembly"

showing 10 items of 29 documents

Half a Century of Research on Membrane-Containing Bacteriophages: Bringing New Concepts to Modern Virology

2019

Half a century of research on membrane-containing phages has had a major impact on virology, providing new insights into virus diversity, evolution and ecological importance. The recent revolutionary technical advances in imaging, sequencing and lipid analysis have significantly boosted the depth and volume of knowledge on these viruses. This has resulted in new concepts of virus assembly, understanding of virion stability and dynamics, and the description of novel processes for viral genome packaging and membrane-driven genome delivery to the host. The detailed analyses of such processes have given novel insights into DNA transport across the protein-rich lipid bilayer and the transformati…

0301 basic medicineArchaeal VirusesModels Molecularcorticoviridaeviruksetviruses030106 microbiologyPopulationlcsh:QR1-502lipid-containing bacteriophagevirus–host interactionReviewGenomeViruslcsh:MicrobiologybakteriofagitEvolution Molecular03 medical and health sciencesViral genome packagingplasmaviridaetectiviridaeVirologyBacteriophage PRD1Bacteriophageseducationvirus evolutioneducation.field_of_studyMembranesbiologyvirus-host interactionVirus Assemblyta1183Virionta1182Archaeal Virusescystoviridaebiology.organism_classificationVirology030104 developmental biologyInfectious DiseasesPlasmaviridaeCapsidViral evolutionDNA ViralCapsid ProteinsViruses
researchProduct

ICTV Virus Taxonomy Profile: Dicistroviridae

2017

Dicistroviridae is a family of small non-enveloped viruses with monopartite, linear, positive-sense RNA genomes of approximately 8–10 kb. Viruses of all classified species infect arthropod hosts, with some having devastating economic consequences, such as acute bee paralysis virus in domesticated honeybees and taura syndrome virus in shrimp farming. Conversely, the host specificity and other desirable traits exhibited by several members of this group make them potential natural enemies for intentional use against arthropod pests, such as triatoma virus against triatomine bugs that vector Chagas disease. This is a summary of the International Committee on Taxonomy of Viruses (ICTV) Report on…

0301 basic medicineChagas diseasevirusesInsect VirusesGenome ViralDisease VectorsVirus ReplicationGenome03 medical and health sciencestaxonomyVirologymedicineICTV ReportAnimalsNatural enemiesTriatomaVirus classificationEconomic consequencesDicistroviridaebiologyVirus AssemblyfungiVirionBeesbiology.organism_classificationmedicine.diseaseVirology3. Good healthICTV Virus Taxonomy Profiles030104 developmental biologyDicistroviridaeRNATaxonomy (biology)ArthropodThe Journal of General Virology
researchProduct

Rab33B Controls Hepatitis B Virus Assembly by Regulating Core Membrane Association and Nucleocapsid Processing

2017

Many viruses take advantage of cellular trafficking machineries to assemble and release new infectious particles. Using RNA interference (RNAi), we demonstrate that the Golgi/autophagosome-associated Rab33B is required for hepatitis B virus (HBV) propagation in hepatoma cell lines. While Rab33B is dispensable for the secretion of HBV subviral envelope particles, its knockdown reduced the virus yield to 20% and inhibited nucleocapsid (NC) formation and/or NC trafficking. The overexpression of a GDP-restricted Rab33B mutant phenocopied the effect of deficit Rab33B, indicating that Rab33B-specific effector proteins may be involved. Moreover, we found that HBV replication enhanced Rab33B expres…

0301 basic medicineHepatitis B virusBiologymedicine.disease_causeVirusArticleCell LineCell membraneRab33B03 medical and health sciencesnucleocapsid assemblyTranscription (biology)RNA interferenceVirologymedicineHumansSecretionNucleocapsidcore/capsid membrane associationHepatitis B virus030102 biochemistry & molecular biologyEffectorVirus AssemblyCell MembraneVirologyHepatitis B Core Antigenshepatitis B virus; Rab GTPase; Rab33B; core/capsid membrane association; nucleocapsid assembly; virus traffickingTransport proteinProtein Transport030104 developmental biologyInfectious Diseasesmedicine.anatomical_structurevirus traffickingrab GTP-Binding ProteinsHost-Pathogen InteractionsHepatocytesRab GTPaseViruses; Volume 9; Issue 6; Pages: 157
researchProduct

Host Cell Rab GTPases in Hepatitis B Virus Infection

2018

Hepatitis B virus (HBV) is a leading cause of liver disease and is presently estimated to infect more than 250 million humans. The extremely successful spread of this virus among the human population is explained by its effective transmission strategies and its manifold particle types, including virions, empty envelopes and naked capsids. Due to its tiny genome, HBV depends on cellular machineries to thrive in infected hepatocytes. To enter, traverse and exit the cell, HBV exploits host membrane trafficking pathways, including intracellular highways directed by Rab GTPases. Here, we review recent discoveries focused on how HBV co-opts and perturbs host Rab GTPase functions with an emphasis …

0301 basic medicineautophagyPopulationvirus assemblyReviewGTPaseBiologymedicine.disease_causeVirusRab33BCell and Developmental Biology03 medical and health sciencesViral life cyclemedicineHBVeducationlcsh:QH301-705.5Hepatitis B viruseducation.field_of_studyRab effector030102 biochemistry & molecular biologyEffectorCell BiologyRab7ARab GAPCell biology030104 developmental biologyRAB7Avirus traffickinglcsh:Biology (General)RabDevelopmental BiologyFrontiers in Cell and Developmental Biology
researchProduct

Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins

2004

For functional diversity, the large (L) envelope protein of hepatitis B virus (HBV) acquires a dual transmembrane topology via co-translational membrane integration of the S region and partial post-translational translocation of the preS subdomain. Because each process requires the second transmembrane segment (TM2), we explored the action of this determinant by using protease protection analysis of mutant L proteins. We demonstrated that neither the disruption of a leucine zipper-like motif by multiple alanine substitutions nor the flanking charges of TM2 affected the topological reorientation of L. The dispensability of both putative subunit interaction modules argues against a link betwe…

AlanineHepatitis B virusHepatitis B virusVirus AssemblyAmino Acid MotifsMolecular Sequence DataProtein domainPhenotype mixingBiological TransportBiologyEndoplasmic Reticulummedicine.disease_causeVirologyTransmembrane domainDual topologyAmino Acid SubstitutionViral Envelope ProteinsVirologyMembrane topologymedicineHepadnavirusAmino Acid SequenceProtein Processing Post-TranslationalJournal of General Virology
researchProduct

Mosaic Qβ coats as a new presentation model

1998

The new protein carrier was developed on the basis of recombinant RNA phage Qbeta capsid. C-terminal UGA extension of the short form of Qbeta coat, so-called A1 extension, served as a target for presentation of foreign peptides on the outer surface of mosaic Qbeta particles. In conditions of enhanced UGA suppression, the proportion of A1-extended to short coats in mosaic particles dropped from 48% to 14%, with an increase of the length of A1 extension. A model insertion, short preS1 epitope 31-DPAFR-35 of hepatitis B surface antigen, demonstrated superficial location on the mosaic Qbeta particles and ensured specific antigenicity and immunogenicity.

AntigenicityRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHepatitis b surface antigenBiochemistryEpitopelaw.inventionCapsid assemblyMiceCapsidPhage QβPeptide LibraryStructural BiologylawGeneticsAnimalsHepatitis B virus preS1Cloning MolecularMolecular BiologyAllolevivirusMice Inbred BALB CCoat protein UGA suppressionVirus AssemblyImmunogenicityA1 extensionRNACell BiologyImmunogenicityVirologyMolecular biologyCapsidCarrier proteinCodon TerminatorRecombinant DNACapsid ProteinsFEBS Letters
researchProduct

Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

2014

Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their …

Cancer ResearchViral proteinvirusesIntracellular SpaceBiologymedicine.disease_causeBacterial cell structureProtein–protein interactionViral Proteins03 medical and health sciencesVirologyEscherichia colimedicineBacteriophage PRD1Escherichia coli030304 developmental biology0303 health sciencesBacteria030302 biochemistry & molecular biologyDNA replicationta1182Protein interactionsFusion proteinVirus assemblyCell biologyConfocal microscopyProtein TransportInfectious DiseasesMembrane proteinVirion assemblyMembrane virusVirus Research
researchProduct

Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

2014

Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their …

Confocal microscopykonfokaalimikroskopiabakteeriMembrane virusvirusesproteiinien vuorovaikutuksetKalvollinen virusProtein interactionsVirus assemblybakteerit
researchProduct

Something old, something new : exploring membrane-containing bacteriophages

2016

Cystoviridaesaperonitrakenneviruksetvirus assemblymembrane-containing virusbakteriofagitfluoresenssimikroskopiassDNA phagevirologiaperimäkalvotchaperonin complexproteiinitbacteriophage PRD1fluorescent fusion proteinkapsidi
researchProduct

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
researchProduct