Search results for "Capsid Protein"

showing 10 items of 137 documents

G2 rotavirus infections in an infantile population of the South of Italy: variability of viral strains over time.

2005

Rotavirus positive samples collected in Palermo, Italy, during 2002–2004 did not react with the G2 type-specific RV5:3 monoclonal antibodies (MAbs) and could be identified as G2 only by RT-PCR genotyping. The genetic variation of VP7 and VP4 antigenic proteins was studied in 14 G2 samples including a selection of both those successfully characterized by serotyping and those failing to be serotyped. The phylogenetic analysis performed on partial VP7 sequences showed a temporal clustering of these strains, with those isolated in Palermo in 2003 belonging to the same lineage of G2 MAbs-unreactive strains identified in UK in 1996–1997 and in Bari, Italy, in 2003–2004. A single amino acid substi…

SerotypeRotavirusSettore MED/07 - Microbiologia E Microbiologia ClinicaTime FactorsSettore MED/17 - Malattie InfettivevirusesPopulationReoviridaemedicine.disease_causeVirusRotavirus InfectionsFecesfluids and secretionsVirologyRotavirusGenetic variationmedicineHumansSerotypingeducationGenotypingAntigens ViralPhylogenyGeneticsrotavirus G2 genetic variation phylogenetic analysiseducation.field_of_studybiologyPhylogenetic treeInfant Newbornvirus diseasesInfantbiology.organism_classificationVirologyInfectious DiseasesItalyChild PreschoolCapsid ProteinsJournal of medical virology
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Analysis of early strains of the norovirus pandemic variant GII.4 Sydney 2012 identifies mutations in adaptive sites of the capsid protein.

2014

AbstractGlobal surveillance for norovirus identified in 2012 the emergence of a novel pandemic GII.4 variant, termed Sydney 2012. In Italy, the novel pandemic variant was identified as early as November 2011 but became predominant only in the winter season 2012–2013. Upon sequencing and comparison with strains of global origin, the early Sydney 2012 strains were found to differ from those spreading in 2012–2013 in the capsid (ORF2) putative epitopes B, C and D, segregating into a distinct phylogenetic clade. At least three residues (333, 340 and 393, in epitopes B, C and D, respectively) of the VP1 varied among Sydney 2012 strains of different clades. These findings suggest that the spread …

Settore MED/07 - Microbiologia E Microbiologia ClinicaEvolutionMolecular Sequence DataCapsid protein VP1 epitopes Evolution GII.4 Italy Norovirus Sydney 2012 variantBiologymedicine.disease_causeEpitopeSydney 2012 variantVirologyPandemicmedicineHumansAmino Acid SequenceCladePandemicsPhylogenyPhylogenetic treeNorovirusCapsid protein VP1 epitopesVirologyGastroenteritisCapsidItalyMutationNorovirusCapsid ProteinsSeasonsWinter seasonGII.4Virology
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Epidemiological dynamics of norovirus GII.4 variant New Orleans 2009.

2015

Norovirus (NoV) is one of the major causes of diarrhoeal disease with epidemic, outbreak and sporadic patterns in humans of all ages worldwide. NoVs of genotype GII.4 cause nearly 80–90 % of all NoV infections in humans. Periodically, some GII.4 strains become predominant, generating major pandemic variants. Retrospective analysis of the GII.4 NoV strains detected in Italy between 2007 and 2013 indicated that the pandemic variant New Orleans 2009 emerged in Italy in the late 2009, became predominant in 2010–2011 and continued to circulate in a sporadic fashion until April 2013. Upon phylogenetic analysis based on the small diagnostic regions A and C, the late New Orleans 2009 NoVs circulati…

Settore MED/07 - Microbiologia E Microbiologia ClinicaGenotypeMolecular Sequence DataBiologymedicine.disease_causeGenomeFecesOpen Reading FramesPhylogeneticsVirologyPandemicGenotypemedicineHumansAmino Acid SequencePhylogenyCaliciviridae InfectionsRetrospective StudiesGeneticsnorovirus GII.4 variant New Orleans 2009 epidemiologyPhylogenetic treeNorovirusOutbreakNew OrleansVirologyGastroenteritisCaliciviridae InfectionsItalyNorovirusCapsid ProteinsSequence AlignmentThe Journal of general virology
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The complete genome sequence of Lamium mild mosaic virus, a member of the genus Fabavirus

2013

Springer-Verlag Wien 2013 Abstract Lamium mild mosaic virus (LMMV) is the only one of the five members of the genus Fabavirus for which there are no nucleotide sequence data. In this study, the complete genome sequence of LMMV was determined and compared with the available complete genome sequences of other members of the genus Fabavirus. The genome was the largest of the genus but maintained the typical orga- nization, with RNA 1 of 6080 nucleotides (nt), RNA 2 of 4065 nt, and an unusually long 3 0 untranslated region in RNA 2 of 603 nt. Phylogenetic analysis of the amino acid sequences of the protease-polymerase (Pro-Pol) region and the two coat proteins confirmed that LMMV belongs to a d…

SubfamilyLMMVMolecular Sequence DataGenome ViralGenomeFabaviruBroad bean wilt virusViral ProteinsSpecies SpecificityGenusMosaic VirusesVirologySecoviridaeTobaccoComovirinaePhylogenyPlant DiseasesGeneticsWhole genome sequencingLamiaceaebiologyBase SequenceNucleic acid sequenceSettore AGR/12 - Patologia Vegetalefood and beveragesGeneral MedicineDNA-Directed RNA PolymerasesSequence Analysis DNAClassificationbiology.organism_classificationVirologyFabavirusRNA ViralCapsid ProteinsPeptide Hydrolases
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Surface-exposed Amino Acid Residues of HPV16 L1 Protein Mediating Interaction with Cell Surface Heparan Sulfate

2007

Efficient infection of cells by human papillomaviruses (HPVs) and pseudovirions requires primary interaction with cell surface proteoglycans with apparent preference for species carrying heparan sulfate (HS) side chains. To identify residues contributing to virus/cell interaction, we performed point mutational analysis of the HPV16 major capsid protein, L1, targeting surface-exposed amino acid residues. Replacement of lysine residues 278, 356, or 361 for alanine reduced cell binding and infectivity of pseudovirions. Various combinations of these amino acid exchanges further decreased cell attachment and infectivity with residual infectivity of less than 5% for the triple mutant, suggesting …

Surface PropertiesLysinePlasma protein bindingBiochemistryAntibodieschemistry.chemical_compoundCapsidChlorocebus aethiopsAnimalsHumansComputer SimulationMolecular Biologychemistry.chemical_classificationAlanineInfectivityHeparinLysineCell MembraneCapsomereOncogene Proteins ViralCell BiologyHeparan sulfateAmino acidchemistryBiochemistryCapsidMutagenesisCOS CellsCapsid ProteinsHeparitin SulfateProtein BindingJournal of Biological Chemistry
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Seroepidemiology of porcine enteric sapovirus in pig farms in Venezuela

2010

Porcine enteric sapovirus (PES) has been shown to cause diarrhea under experimental conditions in gnotobiotic piglets. However, the role of PES as enteric pathogens in porcine farms remains unclear. To further understand the PES-host interactions under field conditions, a serological survey was carried out. To this end the capsid gene of a PES isolate was cloned in the baculovirus expression system and an ELISA was developed based on virus-like particles from the baculovirus-expressed PES capsid protein. A total of 85 serum samples collected from pigs ranging from 8 weeks to over 54 weeks of age were analyzed. An overall seroprevalence to PESs of 62% was found, with significant differences …

SwinevirusesImmunologyAntibodies ViralSapovirusSerologyBlood serumSeroepidemiologic StudiesmedicineAnimalsSeroprevalencePig farmingGeneral VeterinarybiologyAge FactorsVirionSapovirusbiology.organism_classificationVirologyRecombinant Proteinsbody regionsDiarrheaCapsidbiology.proteinCapsid Proteinsmedicine.symptomAntibodyBaculoviridaehuman activitiesVeterinary Immunology and Immunopathology
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Dendritic cell aggresome-like-induced structure formation and delayed antigen presentation coincide in influenza virus-infected dendritic cells.

2005

Abstract Influenza virus infection induces maturation of murine dendritic cells (DCs), which is most important for the initiation of an immune response. However, in contrast to EL-4 and MC57 cells, DCs present viral CTL epitopes with a delay of up to 10 h. This delay in Ag presentation coincides with the up-regulation of MHC class I molecules as well as costimulatory molecules on the cell surface and the accumulation of newly synthesized ubiquitinated proteins in large cytosolic structures, called DC aggresome-like-induced structures (DALIS). These structures were observed previously after LPS-induced maturation of DCs, and it was speculated that they play a role in the regulation of MHC cl…

Time FactorsImmunologyAntigen presentationCellAntigen-Presenting CellsEpitopes T-Lymphocytechemical and pharmacologic phenomenaBone Marrow CellsVirusCell LineMiceImmune systemCell Line TumorMHC class ImedicineImmunology and AllergyAnimalsHumansReceptors ImmunologicCells CulturedAntigen PresentationMice Inbred C3HbiologyUbiquitinViral Core ProteinsRNA-Binding ProteinsCell DifferentiationDendritic cellDendritic CellsNucleocapsid ProteinsVirologyToll-Like Receptor 2Cell biologyNucleoproteinMice Inbred C57BLToll-Like Receptor 4Aggresomemedicine.anatomical_structureNucleoproteinsInfluenza A virusbiology.proteinCytoplasmic StructuresT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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The Transcription Factors TBX2 and TBX3 Interact with Human Papillomavirus 16 (HPV16) L2 and Repress the Long Control Region of HPVs

2013

ABSTRACT The minor capsid protein L2 of human papillomaviruses (HPVs) has multiple functions during the viral life cycle. Although L2 is required for effective invasion and morphogenesis, only a few cellular interaction partners are known so far. Using yeast two-hybrid screening, we identified the transcription factor TBX2 as a novel interaction partner of HPV type 16 (HPV16) L2. Coimmunoprecipitations and immunofluorescence analyses confirmed the L2-TBX2 interaction and revealed that L2 also interacts with TBX3, another member of the T-box family. Transcription of the early genes during HPV infection is under the control of an upstream enhancer and early promoter region, the long control r…

Transcription GeneticImmunologyBiologyCervical intraepithelial neoplasiaVirus ReplicationMicrobiologyViral life cycleTranscription (biology)VirologyTwo-Hybrid System TechniquesGene expressionProtein Interaction MappingmedicineHumansImmunoprecipitationGeneTranscription factorGeneticsHuman papillomavirus 16virus diseasesPromoterOncogene Proteins Viralmedicine.diseasefemale genital diseases and pregnancy complicationsGenome Replication and Regulation of Viral Gene ExpressionMicroscopy FluorescenceInsect ScienceHost-Pathogen InteractionsCapsid ProteinsT-Box Domain ProteinsChromatin immunoprecipitationHeLa Cells
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Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection.

2009

In this novel study, we have for the first time identified evolutionarily conserved capsid residues in an individual chronically infected with norovirus (GGII.3). From 2000 to 2003, a total of 147 P1-1 and P2 capsid sequences were sequenced and investigated for evolutionarily conserved and functionally important residues by the evolutionary trace (ET) algorithm. The ET algorithm revealed more absolutely conserved residues (ACR) in the P1-1 domain (47/53, 88 %) as compared with the P2 domain (86/133, 64 %). The capsid P1-1 and P2 domains evolved in time-dependent manner, with a distinct break point observed between autumn/winter of year 2000 (isolates P1, P3 and P5) and spring to autumn of y…

Trisaccharide bindingMolecular Sequence DataViral quasispeciesBiologymedicine.disease_causeEvolution MolecularFecesMolecular evolutionVirologymedicineHumansAmino Acid SequenceCloning MolecularReceptorConserved SequencePhylogenyCaliciviridae InfectionsDNA PrimersImmunosuppression TherapyBinding SitesStrain (chemistry)Reverse Transcriptase Polymerase Chain ReactionNorovirusVirologyChronic infectionCapsidNorovirusBlood Group AntigensRNA ViralCapsid ProteinsSeasonsAlgorithmsThe Journal of general virology
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PML nuclear body-residing proteins sequentially associate with HPV genome after infectious nuclear delivery.

2019

Subnuclear promyelocytic leukemia (PML) nuclear bodies (NBs) are targeted by many DNA viruses after nuclear delivery. PML protein is essential for formation of PML NBs. Sp100 and Small Ubiquitin-Like Modifier (SUMO) are also permanently residing within PML NBs. Often, large DNA viruses disassemble and reorganize PML NBs to counteract their intrinsic antiviral activity and support establishment of infection. However, human papillomavirus (HPV) requires PML protein to retain incoming viral DNA in the nucleus for subsequent efficient transcription. In contrast, Sp100 was identified as a restriction factor for HPV. These findings suggested that PML NBs are important regulators of early stages o…

Viral DiseasesPhysiologyvirusesIntranuclear Inclusion BodiesPromyelocytic Leukemia ProteinVirus ReplicationBiochemistryAutoantigensImmune PhysiologyMedicine and Health SciencesCell Cycle and Cell DivisionNuclear proteinBiology (General)PapillomaviridaeStaining0303 health sciencesViral GenomicsImmune System ProteinsChromosome Biology030302 biochemistry & molecular biologyCell StainingTotal Cell CountingNuclear Proteinsvirus diseasesAntigens NuclearGenomicsCell biologymedicine.anatomical_structureInfectious DiseasesCapsidCell ProcessesViral GenomeCellular Structures and OrganellesIntranuclear SpaceResearch ArticleHuman Papillomavirus InfectionQH301-705.5UrologyImmunologyCell Enumeration TechniquesSUMO-1 ProteinSexually Transmitted DiseasesMitosisMicrobial GenomicsGenome ViralBiologyResearch and Analysis MethodsMicrobiologyVirusAntibodies03 medical and health sciencesPromyelocytic leukemia proteinVirologyNuclear BodiesmedicineGeneticsHumansVesiclesMolecular BiologyMitosisTranscription factor030304 developmental biologyCell NucleusGenitourinary InfectionsTumor Suppressor ProteinsBiology and Life SciencesProteinsCell BiologyRC581-607Cell nucleusViral replicationSpecimen Preparation and Treatmentbiology.proteinParasitologyCapsid ProteinsImmunologic diseases. AllergyTranscription FactorsPLoS Pathogens
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