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Generation and neutralization of pseudovirions of human papillomavirus type 33

1997

Since human papillomaviruses (HPV) cannot be propagated in cell culture, the generation of infectious virions in vitro is a highly desirable goal. Here we report that pseudovirions can be generated by the assembly of virus-like particles (VLPs) in COS-7 cells containing multiple copies of a marker plasmid. Using recombinant vaccinia viruses, we have obtained spherical VLPs of HPV type 33 (HPV-33) which fractionate into heavy and light VLPs in cesium chloride density gradients. VLPs in the heavy fraction (1.31 g/cm3) carry the plasmid in DNase-resistant form and are capable of transferring the genetic marker located on the plasmid to COS-7 cells in a DNase-resistant way (pseudoinfection). Th…

virusesImmunologyBiologyAntibodies Viralcomplex mixturesMicrobiologyNeutralizationlaw.inventionchemistry.chemical_compoundCapsidPlasmidNeutralization TestslawVirologyAnimalsDeoxyribonuclease IHumansAntigens ViralPapillomaviridaeAntiserumVirus AssemblyVirionvirus diseasesOncogene Proteins ViralVirologyMolecular biologyIn vitroTiterchemistryCapsidInsect ScienceCOS CellsDNA ViralRecombinant DNACapsid ProteinsDNAResearch ArticleJournal of Virology
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The human autoantigen La/SS-B accelerates herpes simplex virus type 1 replication in transfected mouse 3T3 cells.

1998

SUMMARY Permanently transfected mouse cell lines which expressed different levels of the human autoantigen La/SS-B were infected with different strains of herpes simplex virus type 1, including the strains ANG, HSZP, 17syn+ and HFEM. During infection the localization of the human La protein was followed using an anti-La MoAb, which recognized only the human La protein but did not cross-react with either the endogenous mouse La protein or any viral encoded protein. After infection La protein was transported from the nucleus to the cytoplasm. The time course of translocation was dependent on the amount of human La protein expressed in the respective cell line. Moreover, acceleration of viral …

virusesImmunologyHerpesvirus 1 Humanmedicine.disease_causeTransfectionVirus ReplicationAutoantigensVirus3T3 cellsSingle-stranded binding proteinMicemedicineImmunology and AllergyAnimalsHumansbiologyTransfection3T3 CellsOriginal ArticlesHerpes simplex virusmedicine.anatomical_structureViral replicationGene Expression RegulationRibonucleoproteinsCytoplasmCell cultureImmunologybiology.proteinClinical and experimental immunology
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Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymati…

1997

The NS5B protein of the hepatitis C virus (HCV) is an RNA-dependent RNA polymerase (RdRp) (S.-E. Behrens, L. Tomei, and R. De Francesco, EMBO J. 15:12-22, 1996) that is assumed to be required for replication of the viral genome. To further study the biochemical and structural properties of this enzyme, an NS5B-hexahistidine fusion protein was expressed with recombinant baculoviruses in insect cells and purified to near homogeneity. The enzyme was found to have a primer-dependent RdRp activity that was able to copy a complete in vitro-transcribed HCV genome in the absence of additional viral or cellular factors. Filter binding assays and competition experiments showed that the purified enzym…

virusesImmunologyMolecular Sequence DataRNA-dependent RNA polymeraseSequence alignmentRNA-binding proteinHepacivirusViral Nonstructural ProteinsMicrobiologychemistry.chemical_compoundStructure-Activity RelationshipVirologyRNA polymeraseNS5BPeptide sequencePolymerasebiologyBase SequenceSequence Homology Amino AcidRNARNA-Binding ProteinsTemplates GeneticRNA-Dependent RNA PolymeraseMolecular biologyRecombinant ProteinschemistryAmino Acid SubstitutionInsect Sciencebiology.proteinRNA ViralSequence AlignmentResearch Article
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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
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Oncolytic targeting of renal cell carcinoma via encephalomyocarditis virus

2010

Apoptosis is a fundamental host defence mechanism against invading microbes. Inactivation of NF-kappaB attenuates encephalomyocarditis virus (EMCV) virulence by triggering rapid apoptosis of infected cells, thereby pre-emptively limiting viral replication. Recent evidence has shown that hypoxia-inducible factor (HIF) increases NF-kappaB-mediated anti-apoptotic response in clear-cell renal cell carcinoma (CCRCC) that commonly exhibit hyperactivation of HIF due to the loss of its principal negative regulator, von Hippel-Lindau (VHL) tumour suppressor protein. Here, we show that EMCV challenge induces a strong NF-kappaB-dependent gene expression profile concomitant with a lack of interferon-me…

virusesTransplantation HeterologousApoptosisMice SCIDBiologyNF-κBMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA interferenceCell Line TumorVHLEMCVBasic Helix-Loop-Helix Transcription FactorsAnimalsHIFEncephalomyocarditis virusRNA Small InterferingCarcinoma Renal CellResearch Articles030304 developmental biology0303 health sciencesNF-kappa BNF-κBNFKB1RCCVirologyKidney Neoplasms3. Good healthOncolytic virusOncolytic VirusesViral replicationchemistryVon Hippel-Lindau Tumor Suppressor ProteinApoptosisCell culture030220 oncology & carcinogenesisCancer researchMolecular MedicineRNA InterferenceSignal transductionSignal TransductionEMBO Molecular Medicine
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Why viruses sometimes disperse in groups?

2019

AbstractMany organisms disperse in groups, yet this process is understudied in viruses. Recent work, however, has uncovered different types of collective infectious units, all of which lead to the joint delivery of multiple viral genome copies to target cells, favoring co-infections. Collective spread of viruses can occur through widely different mechanisms, including virion aggregation driven by specific extracellular components, cloaking inside lipid vesicles, encasement in protein matrices, or binding to cell surfaces. Cell-to-cell viral spread, which allows the transmission of individual virions in a confined environment, is yet another mode of clustered virus dissemination. Nevertheles…

viruses[SDV]Life Sciences [q-bio]Viral transmissionReview ArticleBiologyGenomeMicrobiologyVirus03 medical and health sciencesMultiplicity of infectionviral spreadVirologydispersal030304 developmental biology0303 health sciencesTransmission (medicine)collective infectious unit030306 microbiologyviral transmissionMutation AccumulationGeographyEvolutionary biologyBiological dispersalmultiplicity of infectionViral spreadCorrigendumVirus Evolution
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SARS-CoV-2 envelope protein topology in eukaryotic membranes

2020

Coronavirus E protein is a small membrane protein found in the virus envelope. Different coronavirus E proteins share striking biochemical and functional similarities, but sequence conservation is limited. In this report, we studied the E protein topology from the new SARS-CoV-2 virus both in microsomal membranes and in mammalian cells. Experimental data reveal that E protein is a single-spanning membrane protein with the N-terminus being translocated across the membrane, while the C-terminus is exposed to the cytoplasmic side (Nt lum /Ct cyt ). The defined membrane protein topology of SARS-CoV-2 E protein may provide a useful framework to understand its interaction with other viral and ho…

virusescoronavirusmedicine.disease_causeViral Envelope Proteinsmembrane insertionPeptide sequencelcsh:QH301-705.5Topology (chemistry)PhylogenyCoronavirusMutationChemistryGeneral NeuroscienceProteïnes de membranaEukaryotavirus diseases129Recombinant ProteinsCell biologysars-cov-2MembraneProtein topologyCoronavirus InfectionsResearch Article1001topologyPneumonia ViralImmunologySequence alignmentBiologyTopologiaVirusGeneral Biochemistry Genetics and Molecular BiologyBetacoronavirusCoronavirus Envelope ProteinsViral envelopeMicrosomesmedicineHumansAmino Acid SequencePandemicsResearchCell MembraneCOVID-1915envelope proteinMembrane proteinlcsh:Biology (General)CytoplasmMutationSequence AlignmentOpen Biology
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Characterization of the autoantigen La (SS-B) as a dsRNA unwinding enzyme

1997

During the analysis of the La (SS-B) autoantigen for catalytic activities an ATP-dependent double-stranded RNA unwinding activity was detected. Both native and recombinant La proteins from different species displayed this activity, which could be inhibited by monospecific anti-La antibodies. La protein was able to melt dsRNA substrates with either two 3'-overhangs or a single 3'- and a 5'-overhang. Double-stranded RNAs with two 5'-overhangs were not unwound, indicating that at least one 3'-overhang is required for unwinding. Sequence elements of the La protein that might be involved in dsRNA unwinding, such as an evolutionarily conserved putative ATP-binding motif and an element that is hom…

virusesgenetic processesGene ExpressionRNA-binding proteinBiologyAutoantigensAntibodiesSubstrate SpecificitySingle-stranded binding proteinlaw.inventionMiceAdenosine TriphosphatelawGene expressionEscherichia coliGeneticsAnimalsHumansGeneralLiterature_REFERENCE(e.g.dictionariesencyclopediasglossaries)Cells CulturedRNA Double-StrandedRibonucleoproteinRNARNA NucleotidyltransferasesProtein kinase RMolecular biologyRecombinant ProteinsRatsenzymes and coenzymes (carbohydrates)RNA silencingLiverRibonucleoproteinsbiology.proteinRecombinant DNAElectrophoresis Polyacrylamide GelRNA HelicasesResearch Article
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Clathrin- and Caveolin-Independent Entry of Human Papillomavirus Type 16—Involvement of Tetraspanin-Enriched Microdomains (TEMs)

2008

BACKGROUND: Infectious entry of human papillomaviruses into their host cells is an important step in the viral life cycle. For cell binding these viruses use proteoglycans as initial attachment sites. Subsequent transfer to a secondary receptor molecule seems to be involved in virus uptake. Depending on the papillomavirus subtype, it has been reported that entry occurs by clathrin- or caveolin-mediated mechanisms. Regarding human papillomavirus type 16 (HPV16), the primary etiologic agent for development of cervical cancer, clathrin-mediated endocytosis was described as infectious entry pathway. METHODOLOGY/PRINCIPAL FINDINGS: Using immunofluorescence and infection studies we show in contra…

viruseslcsh:MedicinePlatelet Membrane GlycoproteinsTetraspanin 24CaveolaeKidneyEndocytosisClathrinVirusCell LineMembrane MicrodomainsViral life cycleTetraspaninAntigens CDCaveolaeInfectious Diseases/Viral InfectionsCaveolinInfectious Diseases/Sexually Transmitted DiseasesHumanslcsh:ScienceHuman papillomavirus 16MultidisciplinarybiologyTetraspanin 30lcsh:RVirionMembrane Proteinsvirus diseasesCell BiologyVirus InternalizationVirology/Host Invasion and Cell EntryVirologyClathrinEndocytosisCell biologyCell culturebiology.proteinFemalelcsh:QMicrobiology/Cellular Microbiology and PathogenesisHeLa CellsResearch ArticlePLoS ONE
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Quantitative microscopy reveals stepwise alteration of chromatin structure during herpesvirus infection

2019

During lytic herpes simplex virus 1 (HSV-1) infection, the expansion of the viral replication compartments leads to an enrichment of the host chromatin in the peripheral nucleoplasm. We have shown previously that HSV-1 infection induces the formation of channels through the compacted peripheral chromatin. Here, we used three-dimensional confocal and expansion microscopy, soft X-ray tomography, electron microscopy, and random walk simulations to analyze the kinetics of host chromatin redistribution and capsid localization relative to their egress site at the nuclear envelope. Our data demonstrated a gradual increase in chromatin marginalization, and the kinetics of chromatin smoothening arou…

viruseslcsh:QR1-502Herpesvirus 1 HumanmikroskopiaVirus ReplicationinfektiotElectronMicrobiologylcsh:MicrobiologyArticleFluorescenceCell LineBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biologyherpes simplex -virustumaChlorocebus aethiopsAnimalsHumansherpesviruksetVero CellsTomographyVirus ReleaseCell NucleusMicroscopyTomography X-RayHerpesvirus 1nuclear egressHerpesviridae InfectionsHSV-1ChromatinMicroscopy ElectronInfectious DiseasesMicroscopy FluorescencetumaegressKasvibiologia mikrobiologia virologia - Plant biology microbiology virologyX-RaykromatiiniSexually Transmitted InfectionschromatinInfectionHuman
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