Search results for "Capsid Protein"

showing 10 items of 137 documents

Synthesis and assembly of virus-like particles of human papillomaviruses type 6 and type 16 in fission yeast Schizosaccharomyces pombe.

1995

AbstractWe have synthesized capsid proteins of human papillomavirus types 6 (HPV 6) and 16 (HPV 16) in fission yeast Schizosaccharomyces pombe and produced virus-like particles (VLP). The capsid proteins were localized in the nucleus by indirect immunofluorescence and cell fractionation analyses. The VLP were produced in both yeast clones synthesizing L1 alone and L1/L2 and purified by sulfato-cellulofine chromatography. Electron microscopic examination showed that these VLP were similar in structure to native HPV particles. Two HPV 16 L1 variants (16 B27L1 and 16 T3L1), isolated from benign cervical samples, produced many more (68- and 14-fold) VLP than the prototype L1 (16 PL1) derived fr…

Oncogene ProteinsImmunoprecipitationvirusesMolecular Sequence DataBiologyVirusSepharoseViral ProteinsCapsidVirologySchizosaccharomycesCloning MolecularPapillomaviridaeDNA PrimersBase SequenceVirionvirus diseasesOncogene Proteins Viralbiology.organism_classificationMolecular biologyYeastRecombinant ProteinsMicroscopy ElectronCapsidSchizosaccharomyces pombeCapsid ProteinsCell fractionationVirology
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An amino-terminal segment of hantavirus nucleocapsid protein presented on hepatitis B virus core particles induces a strong and highly cross-reactive…

2004

AbstractPreviously, we have demonstrated that hepatitis B virus (HBV) core particles tolerate the insertion of the amino-terminal 120 amino acids (aa) of the Puumala hantavirus nucleocapsid (N) protein. Here, we demonstrate that the insertion of 120 amino-terminal aa of N proteins from highly virulent Dobrava and Hantaan hantaviruses allows the formation of chimeric core particles. These particles expose the inserted foreign protein segments, at least in part, on their surface. Analysis by electron cryomicroscopy of chimeric particles harbouring the Puumala virus (PUUV) N segment revealed 90% T = 3 and 10% T = 4 shells. A map computed from T = 3 shells shows additional density splaying out …

OrthohantavirusHepatitis B virusCryo-electron microscopyHantavirus InfectionsRecombinant Fusion ProteinsVirulenceCross Reactions030312 virologyAntibodies Viralmedicine.disease_causeCore antigenMice03 medical and health sciencesVirologymedicineAnimals030304 developmental biologyHantavirusNucleocapsid proteinchemistry.chemical_classificationHepatitis B virusMice Inbred BALB C0303 health sciencesbiologyCryoelectron MicroscopyViral VaccinesNucleocapsid ProteinsVirus-like particlesbiology.organism_classificationHepatitis B Core AntigensVirology3. Good healthAmino acidMice Inbred C57BLchemistrybiology.proteinFemalePuumala virusAntibodyHantavirus InfectionHantavirusVirology
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A hantavirus nucleocapsid protein segment exposed on hepatitis B virus core particles is highly immunogenic in mice when applied without adjuvants or…

2005

Hepatitis B virus (HBV) core particles carrying the amino-terminal 120 amino acids (aa) of the nucleocapsid (N) protein of the hantaviruses Dobrava, Hantaan or Puumala have been demonstrated to be highly immunogenic in mice when complexed with adjuvants. Here we demonstrate that even without adjuvant, these chimeric particles induced high-titered, and strongly cross-reactive N-specific antibody responses in BALB/c and C57BL/6 mice. The induced N-specific antibodies represented all IgG subclasses. Pre-existing core-specific antibodies did not abrogate the induction of an N-specific immune response by a hantavirus N insert presented on core particles. Therefore, chimeric core particles should…

Orthohantavirusmedicine.medical_treatmentEnzyme-Linked Immunosorbent AssaySaccharomyces cerevisiaeCross Reactionsmedicine.disease_causeAntibodies ViralVirusMiceOrthohepadnavirusAdjuvants ImmunologicmedicineEscherichia coliAnimalsImmunization ScheduleHantavirusHepatitis B virusMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologybiologyImmunogenicityPublic Health Environmental and Occupational Healthvirus diseasesNucleocapsid Proteinsbiology.organism_classificationVirologyHepatitis B Core AntigensMice Inbred C57BLInfectious DiseasesHepadnaviridaeImmunoglobulin Gbiology.proteinMolecular MedicineFemaleAntibodyCarrier ProteinsAdjuvantPlasmidsVaccine
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Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells

2004

AbstractA mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protei…

Parvovirus CanineRecombinant Fusion Proteinsanimal diseasesvirusesGreen Fluorescent ProteinsBiophysicsMammalian expressionBiochemistryCell LineGreen fluorescent proteinTransduction (genetics)DogsTransduction GeneticStructural BiologyGeneticsAnimalsBaculovirusCanine parvovirusMolecular BiologyCell NucleusEnhanced green fluorescent proteinbiologyParvovirusCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyCell biologyCapsidCytoplasmCell cultureCatsCapsid ProteinsBaculoviridaeNuclear localization sequenceFEBS Letters
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Assembly of fluorescent chimeric virus-like particles of canine parvovirus in insect cells

2004

Canine parvovirus (CPV) is a small non-enveloped ssDNA virus composed of the viral proteins VP1, VP2, and VP3 with a T=1 icosahedral symmetry. VP2 is nested in VP1 and the two proteins are produced by differential splicing of a primary transcript of the right ORF of the viral genome. The VP2 protein can be further proteolytically cleaved to form VP3. Previous studies have shown that VP1 and VP3 are unnecessary for capsid formation and consequently, that VP2 alone is sufficient for assembly. We have hypothesized that insertion of the enhanced green fluorescent protein (EGFP) at the N-terminus of VP2 could be carried out without altering assembly. To investigate the possibility to develop flu…

Parvovirus CanineRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsHeterologousFluorescence correlation spectroscopySpodopteraBiochemistryVirusCell LineInclusion Bodies ViralGreen fluorescent proteinAnimalsAmino Acid SequenceMolecular BiologyMicroscopy ConfocalBase SequencebiologyChimeraVirus AssemblyCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFusion proteinLuminescent ProteinsMicroscopy ElectronCapsidRNA splicingCapsid ProteinsPlasmidsBiochemical and Biophysical Research Communications
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Detection of canine parvovirus antigens with antibodies to synthetic peptides

1996

Antibodies produced in rabbits against an 18-amino acid peptide (peptide 1, NSLPQSEGATNFGDIGVP) of capsid protein VP2/residues 292-309 of canine parvovirus (CPV) or against an 18-amino acid peptide (peptide 2, GKRNTVLFHGPASTKGKS) of nonstructural protein NS1/residues 391-409 of CPV identified, in immunofluorescence analysis, viral antigens in canine A 72 cells infected with CPV. Antibodies to peptide 2 also identified viral antigens in bovine cells infected with bovine parvovirus. In western blot analysis, antibodies to peptide 1 and peptide 2 also detected viral antigens derived from blue fox parvovirus, feline parvovirus, mink enteritis virus and raccoon dog parvovirus. The peptide antibo…

Parvovirus Canineanimal diseasesvirusesBlotting WesternMolecular Sequence DataFoxesEnzyme-Linked Immunosorbent AssayAntibodies ViralVirusParvovirusCapsidDogsAntigenVirologyAnimalsAmino Acid SequenceFluorescent Antibody Technique IndirectAntigens ViralPeptide sequenceParvoviridaebiologyParvovirusCanine parvovirusvirus diseasesGeneral MedicineBovine parvovirusbiology.organism_classificationVirologyMink enteritis virusMinkCatsCapsid ProteinsCattleRaccoonsRabbitsFeline Panleukopenia VirusArchives of Virology
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Enhanced baculovirus-mediated transduction of human cancer cells by tumor-homing peptides.

2006

ABSTRACT Tumor cells and vasculature offer specific targets for the selective delivery of therapeutic genes. To achieve tumor-specific gene transfer, baculovirus tropism was manipulated by viral envelope modification using baculovirus display technology. LyP-1, F3, and CGKRK tumor-homing peptides, originally identified by in vivo screening of phage display libraries, were fused to the transmembrane anchor of vesicular stomatitis virus G protein and displayed on the baculoviral surface. The fusion proteins were successfully incorporated into budded virions, which showed two- to fivefold-improved binding to human breast carcinoma (MDA-MB-435) and hepatocarcinoma (HepG2) cells. The LyP-1 pepti…

Phage displayCarcinoma HepatocellularTransgenevirusesImmunologyBreast NeoplasmsGene deliveryMicrobiologyVesicular stomatitis Indiana virusTransduction (genetics)Gene DeliveryViral envelopePeptide LibraryTransduction GeneticVirologyCell Line TumorHumansGlycoproteinsbiologyGenetic Therapybiology.organism_classificationMolecular biologyFusion proteinNeoplasm ProteinsVesicular stomatitis virusCell cultureInsect ScienceCapsid ProteinsPeptidesBaculoviridaeProtein BindingJournal of virology
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Synthesis of recombinant atrial natriuretic peptide (rANP) using hybrid fusion protein-phage fr coat/ANP (CP/ANP).

1997

Abstract Baumanis, V., I. Jansone, A. Skangals, I. Mandrika and V. Berzins. Synthesis of recombinant atrial natriuretic peptide (rANP) using hybrid fusion protein-phage fr coat/ANP (CP/ANP). Peptides 18(8) 1229–1235, 1997.—Recombinant atrial natriuretic peptide (rANP) was expressed in and isolated from E. coli. rANP was purified using HPLC. Amino acid analysis, partial sequencing, and molecular mass were determined. Fused protein was used to rise polyclonal antibodies and to develop of immunoenzymatic assays of rANP and CP/ANP. Experiments were designed to study rANP effects on isolated rabbit aortic strips and to examine hypotensive, diuretic, and natriuretic activity, as well as renal cre…

PhysiologyMuscle RelaxationRecombinant Fusion ProteinsRenal functionEnzyme-Linked Immunosorbent AssayIn Vitro TechniquesBiochemistryMuscle Smooth Vascularlaw.inventionCellular and Molecular NeuroscienceEndocrinologyCapsidAtrial natriuretic peptideIn vivolawEscherichia coliAnimalsAntihypertensive AgentsAortaChromatography High Pressure LiquidbiologyMolecular massChemistryMetalloendopeptidasesFusion proteinNPR2DiuresisRatsBiochemistryPolyclonal antibodiescardiovascular systembiology.proteinRecombinant DNACapsid ProteinsRabbitshormones hormone substitutes and hormone antagonistsAtrial Natriuretic Factorcirculatory and respiratory physiologyGlomerular Filtration RatePeptides
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Globally defining the effects of mutations in a picornavirus capsid

2021

The capsids of non-enveloped viruses are highly multimeric and multifunctional protein assemblies that play key roles in viral biology and pathogenesis. Despite their importance, a comprehensive understanding of how mutations affect viral fitness across different structural and functional attributes of the capsid is lacking. To address this limitation, we globally define the effects of mutations across the capsid of a human picornavirus. Using this resource, we identify structural and sequence determinants that accurately predict mutational fitness effects, refine evolutionary analyses, and define the sequence specificity of key capsid-encoded motifs. Furthermore, capitalizing on the derive…

PicornavirusViral proteinQH301-705.5Sciencevirusesmedicine.medical_treatmentPicornaviridaeComputational biologymedicine.disease_causeGenomeGeneral Biochemistry Genetics and Molecular BiologyVirusImmune systemcapsidmedicineSingle amino acidBiology (General)GeneTropismHost proteinGeneticsEvolutionary BiologyMicrobiology and Infectious DiseaseMutationmutational fitness effectsProteaseGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceQRviral proteaseGeneral Medicinebiochemical phenomena metabolism and nutritionbiology.organism_classificationViruspicornavirusViral proteaseCapsidMutationMedicineCapsid ProteinsHuman genomeDeep mutational scanningResearch ArticleHuman
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Apoptosis: a relevant tool for anticancer therapy.

2006

Apoptosis is a form of cell death that permits the removal of damaged, senescent or unwanted cells in multicellular organisms, without damage to the cellular microenvironment. Defective apoptosis represents a major causative factor in the development and progression of cancer. The majority of chemotherapeutic agents, as well as radiation, utilize the apoptotic pathway to induce cancer cell death. Resistance to standard chemotherapeutic strategies also seems to be due to alterations in the apoptotic pathway of cancer cells. Recent knowledge on apoptosis has provided the basis for novel targeted therapies that exploit apoptosis to treat cancer. These new target include those acting in the ext…

Programmed cell deathSettore MED/06 - Oncologia MedicaSurvivinAntineoplastic AgentsApoptosisLigandsInhibitor of Apoptosis ProteinsBortezomibTNF-Related Apoptosis-Inducing Ligandchemistry.chemical_compoundSulindacExisulindNeoplasmsSurvivinmedicineAnimalsHumansbusiness.industryBortezomibapoptosis TRAIL/Apo2L apoptin/VP3 ONYX015 Bortezomib exisulind survivinCancerReceptors Death DomainHematologymedicine.diseaseBoronic AcidsNeoplasm ProteinsOncologyProteasomechemistryApoptosisPyrazinesCancer cellCancer researchCapsid ProteinsbusinessMicrotubule-Associated Proteinsmedicine.drug
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