Search results for "Capsid"

showing 8 items of 248 documents

DNA-induced structural changes in the papillomavirus capsid.

2001

ABSTRACT Human papillomavirus capsid assembly requires intercapsomeric disulfide bonds between molecules of the major capsid protein L1. Virions isolated from naturally occurring lesions have a higher degree of cross-linking than virus-like particles (VLPs), which have been generated in eukaryotic expression systems. Here we show that DNA encapsidation into VLPs leads to increased cross-linking between L1 molecules comparable to that seen in virions. A higher trypsin resistance, indicating a tighter association of capsomeres through DNA interaction, accompanies this structural change.

virusesImmunologyDna interactionBiologyMicrobiologychemistry.chemical_compoundVirologymedicineProkaryotic expressionHumansPapillomaviridaePapillomaviridaeVirus AssemblyStructure and AssemblyCapsomereDisulfide bondVirionbiochemical phenomena metabolism and nutritionTrypsinbiology.organism_classificationMolecular biologyCapsidchemistryInsect ScienceDNA ViralBiophysicsDNAmedicine.drugJournal of virology
researchProduct

Baculovirus-mediated immediate-early gene expression and nuclear reorganization in human cells

2007

Baculovirus, Autographa californica multiple nucleopolyhedrovirus (AcMNPV), has the ability to transduce mammalian cell lines without replication. The general objective of this study was to detect the transcription and expression of viral immediate-early genes in human cells and to examine the interactions between viral components and subnuclear structures. Viral capsids were seen in large, discrete foci in nuclei of both dividing and non-dividing human cells. Concurrently, the transcription of viral immediate-early transregulator genes (ie-1, ie-2) and translation of IE-2 protein were detected. Quantitative microscopy imaging and analysis showed that virus transduction altered the size of …

virusesImmunologyGene ExpressionAnthraquinonesMicrobiologyCell LineHistonesMiceViral ProteinsTransduction (genetics)CapsidViral entryTranscription (biology)VirologyAnimalsHumansInsect virusGenes Immediate-EarlyGeneCell NucleusMicroscopy ConfocalbiologyChromatin Assembly and DisassemblyMolecular biologyNucleopolyhedrovirusesChromatinHistoneMicroscopy Fluorescencebiology.proteinImmediate early geneCellular Microbiology
researchProduct

The closest relatives of icosahedral viruses of thermophilic bacteria are among viruses and plasmids of the halophilic archaea.

2009

We have sequenced the genome and identified the structural proteins and lipids of the novel membranecontaining, icosahedral virus P23-77 of Thermus thermophilus. P23-77 has an 17-kb circular double-stranded DNA genome, which was annotated to contain 37 putative genes. Virions were subjected to dissociation analysis, and five protein species were shown to associate with the internal viral membrane, while three were constituents of the protein capsid. Analysis of the bacteriophage genome revealed it to be evolutionarily related to another Thermus phage (IN93), archaeal Halobacterium plasmid (pHH205), a genetic element integrated into Haloarcula genome (designated here as IHP for integrated Ha…

virusesImmunologyMicrobiologyGenomeVirusBacteriophage03 medical and health sciencesBacterial ProteinsVirologyGeneVirus classificationPhylogeny030304 developmental biologyGeneticsAdenosine Triphosphatases0303 health sciencesbiologyBase Sequence030306 microbiologyThermus thermophilusMembrane ProteinsViral membraneProvirusbiology.organism_classificationLipidsGenetic Diversity and EvolutionVirion assemblyGenes BacterialInsect ScienceCapsid ProteinsGenome BacterialJournal of virology
researchProduct

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
researchProduct

Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.

1998

ABSTRACT We have used viruslike particles (VLPs) of human papillomaviruses to study the structure and assembly of the viral capsid. We demonstrate that mutation of either of two highly conserved cysteines of the major capsid protein L1 to serine completely prevents the assembly of VLPs but not of capsomers, whereas mutation of all other cysteines leaves VLP assembly unaffected. These two cysteines form intercapsomeric disulfides yielding an L1 trimer. Trimerization comprises about half of the L1 molecules in VLPs but all L1 molecules in complete virions. We suggest that trimerization of L1 is indispensable for the stabilization of intercapsomeric contacts in papillomavirus capsids.

virusesImmunologyTrimerBiologymedicine.disease_causeMicrobiologycomplex mixturesSerineCapsidVirologyAnimal VirusesmedicineCysteineDisulfidesPapillomaviridaeMutationVirus AssemblyCapsomereVirionvirus diseasesbiochemical phenomena metabolism and nutritionMolecular biologyCapsidInsect ScienceMutationBiophysicsCysteineJournal of virology
researchProduct

Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix

2019

Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…

virusesLipid BilayersBiophysicsProtein Structure Secondary03 medical and health sciencessymbols.namesake0302 clinical medicineimmune system diseasesAmino Acid Sequence030304 developmental biology0303 health sciencesChemistryEndoplasmic reticulumVesicleCholesterol bindingvirus diseasesArticlesCOPIGolgi apparatusLipidsTransmembrane proteinSphingomyelinsTransmembrane domainCholesterolsymbolsBiophysicsCapsid Proteinslipids (amino acids peptides and proteins)SphingomyelinDimerization030217 neurology & neurosurgeryBiophysical Journal
researchProduct

Evaluation of HBs, HBc, and frCP virus-like particles for expression of human papillomavirus 16 E7 oncoprotein epitopes.

2002

<i>Objectives:</i> In an attempt to develop virus-like particles (VLPs) as experimental vaccine against human papilloma virus (HPV)-induced tumours, the HPV16 E7 oncoprotein epitopes spanning amino acid (aa) residues 35–98 were expressed on three proteins capable of VLP formation: hepatitis B virus (HBV) surface (HBs) and core (HBc) antigens, and RNA phage fr coats (frCP). <i>Methods:</i> The profile of immunoglobulin isotypes induced in Balb/C mice after immunization with purified chimeric proteins was studied. <i>Results:</i> The HBs*-E7(35–54) protein expressing E7 residues 35–54 between residues 139 and 142 of the HBs carrier formed HBs-like particles…

virusesPapillomavirus E7 ProteinsRecombinant Fusion ProteinsMolecular Sequence DataRNA PhagesAntibodies ViralEpitopeVirusEpitopesMiceHpv16 e7Immune systemCapsidPapillomavirus E7 ProteinsVirologyAnimalsHumansAmino Acid SequenceHuman papillomavirusneoplasmsMice Inbred BALB CHepatitis B Surface AntigensbiologyVirionvirus diseasesOncogene Proteins ViralVirologyHepatitis B Core Antigensfemale genital diseases and pregnancy complicationsImmunoglobulin IsotypesInfectious DiseasesImmunizationbiology.proteinFemaleImmunizationAntibodyIntervirology
researchProduct

Pseudovirions as Specific Tools for Investigation of Virus Interactions With Cells

2004

This chapter outlines the generation and application of human papillomavirus type 33 (HPV33) pseudovirions. The method describes (1) the construction of vaccinia viruses recombinant for the major and minor HPV capsid proteins, L1 and L2, respectively; (2) the transfection of Cos7 cells with a marker plasmid replicating to high copy numbers; (3) the expression of L1 and L2 using the vaccinia virus expression system; (4) the extraction, purification, and analysis of HPV33 pseudovirions; and (5) their use in pseudoinfection assays. These pseudovirions are structurally indistinguishable from native virions and are therefore valuable tools for the study of papillomavirus-cell interactions. The m…

virusesTransfectionBiologyVirologyViruslaw.inventionchemistry.chemical_compoundPlasmidchemistryCapsidlawRecombinant DNAVacciniaVaccinia virusesDNA
researchProduct