Search results for "capsid"

showing 10 items of 248 documents

Genetic lesions associated with Muller's ratchet in an RNA virus

1996

The molecular basis of Muller's ratchet has been investigated using the important animal pathogen foot-and-mouth disease virus (FMDV). Clones from two FMDV populations were subjected to serial plaque transfers (repeated bottleneck events) on host BHK-21 cells. Relative fitness losses were documented in 11 out of 19 clones tested. Small fitness gains were observed in three clones. One viral clone attained an extremely low plating efficiency, suggesting that accumulation of deleterious mutations had driven the virus near extinction. Nucleotide sequence analysis revealed unique genetic lesions in multiply transferred clones that had never been seen in FMDVs isolated in nature or subjected to m…

Mutational hot spotvirusesViral quasispeciesViral Plaque AssayVirusOligoadenylate extensionCell LineExtinction PsychologicalAphthovirusStructural BiologyCricetinaePolyadenylateAnimalsFitness lossMolecular BiologyGeneticsbiologyFoot-and-mouth disease virusNucleic acid sequenceRNA virusMuller's ratchetbiology.organism_classificationVirologyQuasispeciesCapsidMutationNucleic Acid ConformationRNA ViralFoot-and-mouth disease virus
researchProduct

Antiviral Mechanisms of N-Phenyl Benzamides on Coxsackie Virus A9

2023

Enteroviruses are one of the most abundant groups of viruses infecting humans, and yet there are no approved antivirals against them. To find effective antiviral compounds against enterovirus B group viruses, an in-house chemical library was screened. The most effective compounds against Coxsackieviruses B3 (CVB3) and A9 (CVA9) were CL212 and CL213, two N-phenyl benzamides. Both compounds were more effective against CVA9 and CL213 gave a better EC50 value of 1 µM with high a specificity index of 140. Both drugs were most effective when incubated directly with viruses suggesting that they mainly bound to the virions. A real-time uncoating assay showed that the compounds stabilized the virion…

N-phenyl benzamideenteroviruksetviruksetenterovirustartuntatauditenterovirus; antiviral; capsid binder; <i>N</i>-phenyl benzamidePharmaceutical Scienceantiviralcapsid binderkapsidiPharmaceutics; Volume 15; Issue 3; Pages: 1028
researchProduct

A Sliding Window-Based Method to Detect Selective Constraints in Protein-Coding Genes and Its Application to RNA Viruses

2002

Here we present a new sliding window-based method specially designed to detect selective constraints in specific regions of a multiple protein-coding sequence alignment. In contrast to previous window-based procedures, our method is based on a nonarbitrary statistical approach to find the appropriate codon-window size to test deviations of synonymous (d(S)) and nonsynonymous (d(N)) nucleotide substitutions from the expectation. The probabilities of d(N) and d(S) are obtained from simulated data and used to detect significant deviations of d(N) and d(S) in a specific window region of the real sequence alignment. The nonsynonymous-to-synonymous rate ratio (w = d(N)/d(S)) was used to highlight…

Nonsynonymous substitutionGenes ViralSequence alignmentBiologyGenes envEvolution MolecularViral ProteinsSliding window protocolGeneticsRNA VirusesSelection GeneticMolecular BiologyGenePhylogenyEcology Evolution Behavior and SystematicsSelection (genetic algorithm)GeneticsBase SequenceReproducibility of ResultsContrast (statistics)RNAWindow (computing)Genes gagFoot-and-Mouth Disease VirusDNA ViralHIV-1Capsid ProteinsSequence AlignmentAlgorithmJournal of Molecular Evolution
researchProduct

Genetic variability and evolutionary analysis of parietaria mottle virus: role of selection and genetic exchange

2015

[EN] The genetic variability and evolution of parietaria mottle virus (PMoV) of the genus Ilarvirus was studied by analyzing nucleotide sequences of 2b and CP genes from isolates collected in different countries. Phylogenetic analysis showed that PMoV isolates clustered in different clades: one (clade I) composed of only Italian isolates and three clades (clades II-IV) including the Spanish isolates. The Greek isolate GrT-1 used in this study was in clade IV for the CP phylogenetic tree whereas it formed a separate branch in the 2b phylogenetic tree. The nucleotide sequence diversity of both the 2b and CP genes was low (0.062 +/- A 0.006 and 0.063 +/- A 0.006 for 2b and CP, respectively) bu…

Nonsynonymous substitutionRNA virusesPopulation geneticsMovementMolecular Sequence DataPopulation geneticsBiologyIlarvirusTomatoEvolution MolecularPhylogeneticsVirologyRatesGenetic variationMosaic virusSequencePRODUCCION VEGETALGenetic variabilityOriginsCladePhylogenyPlant DiseasesIlarvirusGeneticsCoat proteinPhylogenetic treeparietaria mottle virus genetic exchange evolutionary analysisGenetic VariationSettore AGR/12 - Patologia VegetaleMICROBIOLOGIAGeneral Medicinebiology.organism_classificationVirologyBiological EvolutionRecombinationParietariaCapsid Proteins
researchProduct

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
researchProduct

Chimaeric HBV core particles carrying a defined segment of Puumala hantavirus nucleocapsid protein evoke protective immunity in an animal model

1998

Abstract Hantaviruses are rodent-born agents which are pathogenic in humans causing haemorrhagic fever with renal syndrome or hantavirus pulmonary syndrome. To induce a protective immunity against a European hantavirus (Puumala) we constructed chimaeric hepatitis B virus (HBV) core particles carrying defined fragments of the Puumala virus nucleocapsid protein. After immunisation of bank voles, the natural host of Puumala virus, with core particles possessing an insertion of the N-terminal part of Puumala virus nucleocapsid protein, four of five animals were protected against subsequent virus challenge. The results show that the major protective region of the nucleocapsid protein is located …

OrthohantavirusHantavirus InfectionsRecombinant Fusion Proteinsvirusesmedicine.disease_causeVirusVirus-like particlemedicineAnimalsNucleocapsidHantavirusHepatitis B virusHantavirus pulmonary syndromeGeneral VeterinaryGeneral Immunology and MicrobiologybiologyArvicolinaePublic Health Environmental and Occupational Healthvirus diseasesViral Vaccinesbiology.organism_classificationHepatitis B Core AntigensVirologyInfectious DiseasesHepadnaviridaeMolecular MedicinePuumala virusBunyaviridaeVaccine
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct