Search results for "Microbio"

showing 10 items of 8741 documents

Single-chain antibodies against a plant viral RNA-dependent RNA polymerase confer virus resistance.

2004

Crop loss due to viral diseases is still a major problem for agriculture today. We present a strategy to achieve virus resistance based on the expression of single-chain Fv fragments (scFvs) against a conserved domain in a plant viral RNA-dependent RNA polymerase (RdRp), a key enzyme in virus replication. The selected scFvs inhibited complementary RNA synthesis of different plant virus RdRps in vitro and virus replication in planta. Moreover, the scFvs also bound to the RdRp of the distantly related hepatitis C virus. T(1) and T(2) progeny of transgenic lines of Nicotiana benthamiana expressing different scFvs either in the cytosol or in the endoplasmic reticulum showed varying degrees of r…

virusesHepatitis C virusAmino Acid MotifsBiomedical EngineeringNicotiana benthamianaBioengineeringmedicine.disease_causeAntibodies ViralVirus ReplicationApplied Microbiology and BiotechnologyVirusPlant VirusesTombusviruschemistry.chemical_compoundRNA polymerasePlant virusTobaccomedicinePlant DiseasesGeneticsbiologyfungifood and beveragesbiology.organism_classificationPlants Genetically ModifiedRNA-Dependent RNA PolymeraseVirologyTombusviridaechemistryViral replicationMolecular MedicineSingle-Chain AntibodiesBiotechnologyNature biotechnology
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Modulation of Hepatitis C Virus NS5A Hyperphosphorylation by Nonstructural Proteins NS3, NS4A, and NS4B

1999

NS5A of the hepatitis C virus (HCV) is a highly phosphorylated protein involved in resistance against interferon and required most likely for replication of the viral genome. Phosphorylation of this protein is mediated by a cellular kinase(s) generating multiple proteins with different electrophoretic mobilities. In the case of the genotype 1b isolate HCV-J, in addition to the basal phosphorylated NS5A (designated pp56), a hyperphosphorylated form (pp58) was found on coexpression of NS4A (T. Kaneko, Y. Tanji, S. Satoh, M. Hijikata, S. Asabe, K. Kimura, and K. Shimotohno, Biochem. Biophys. Res. Commun. 205:320‐326, 1994). Using a comparative analysis of two full-length genomes of genotype 1b…

virusesHepatitis C virusHepacivirusMolecular Sequence DataImmunologyGene ExpressionReplicationHyperphosphorylationGenome ViralHepacivirusViral Nonstructural Proteinsmedicine.disease_causeMicrobiologyCell LineInterferonCricetinaeVirologymedicineAnimalsHumansPhosphorylationNS5ANS3Base SequencebiologyPestivirusvirus diseasesRNAbiochemical phenomena metabolism and nutritionbiology.organism_classificationVirologyMolecular biologydigestive system diseasesAmino Acid SubstitutionInsect ScienceDNA Viralmedicine.drugJournal of Virology
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Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells

1995

Infection of cells by human papillomaviruses (HPVs) associated with malignant genital lesions has not been studied because of the lack of an in vitro system and the unavailability of virions. We have now used virus-like particles (VLPs) of HPV type 33 to analyze the initial events in the interaction of the HPV capsid with cell lines. Binding of VLPs to HeLa cells was observed in biochemical assays and by immunofluorescence. VLP binding was inhibited by antisera raised against VLPs but not by monoclonal antibodies recognizing either L1 or L2 epitopes accessible on VLPs. Under saturating conditions, approximately 2 x 10(4) VLPs were bound per cell, with a dissociation constant of about 100 pM…

virusesImmunoelectron microscopyImmunologyBiologyAntibodies ViralMembrane Fusioncomplex mixturesMicrobiologyVirusEpitopeCell LineMiceVirologyAnimalsHumansMicroscopy ImmunoelectronPapillomaviridaeCapsomereVirionMembrane Proteinsvirus diseasesLipid bilayer fusionbiochemical phenomena metabolism and nutritionMolecular biologyEndocytosisEndocytic vesicleCapsidCell cultureInsect ScienceResearch ArticleJournal of Virology
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Assembly and Translocation of Papillomavirus Capsid Proteins

2002

ABSTRACT The major and minor capsid proteins of polyomavirus are preassembled in the cytoplasm and translocated to the nucleus only as a VP1-VP2/VP3 complex. In this study, we describe independent nuclear translocation of the L1 major protein and the L2 minor capsid protein of human papillomavirus type 33 by several approaches. First, we observed that expression and nuclear translocation of L2 in natural lesions precede expression of L1. Second, using a cell culture system for coexpression, we found that accumulation of L2 in nuclear domain 10 (ND10) subnuclear structures precedes L1 by several hours. In contrast, complexes of L2 and mutants of L1 forced to assemble in the cytoplasm are tra…

virusesImmunologyActive Transport Cell NucleusChromosomal translocationBiologyMicrobiologychemistry.chemical_compoundCapsidVirologyMG132medicineAnimalsHumansPapillomaviridaeCOS cellsStructure and AssemblyVirus AssemblyOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologymedicine.anatomical_structureCapsidchemistryCytoplasmCell cultureInsect ScienceCOS CellsProteasome inhibitorCapsid ProteinsFemaleNucleusmedicine.drug
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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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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Enhancement of hepatitis C virus RNA replication by cell culture-adaptive mutations.

2001

ABSTRACT Studies of the Hepatitis C virus (HCV) replication cycle have been made possible with the development of subgenomic selectable RNAs that replicate autonomously in cultured cells. In these replicons the region encoding the HCV structural proteins was replaced by the neomycin phosphotransferase gene, allowing the selection of transfected cells that support high-level replication of these RNAs. Subsequent analyses revealed that, within selected cells, HCV RNAs had acquired adaptive mutations that increased the efficiency of colony formation by an unknown mechanism. Using a panel of replicons that differed in their degrees of cell culture adaptation, in this study we show that adaptive…

virusesImmunologyCell Culture TechniquesRNA-dependent RNA polymeraseReplicationHepacivirusBiologyViral Nonstructural ProteinsOrigin of replicationVirus ReplicationMicrobiologyReplication factor CControl of chromosome duplicationGenes ReporterVirologyTumor Cells CulturedHumansRepliconLuciferasesGeneRNAVirologyAdaptation PhysiologicalViral replicationInsect ScienceMutationRNA ViralRepliconJournal of virology
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Viral and cellular determinants of hepatitis C virus RNA replication in cell culture.

2003

Studies on the replication of hepatitis C virus (HCV) have been facilitated by the development of selectable subgenomic replicons replicating in the human hepatoma cell line Huh-7 at a surprisingly high level. Analysis of the replicon population in selected cells revealed the occurrence of cell culture-adaptive mutations that enhance RNA replication substantially. To gain a better understanding of HCV cell culture adaptation, we characterized conserved mutations identified by sequence analysis of 26 independent replicon cell clones for their effect on RNA replication. Mutations enhancing replication were found in nearly every nonstructural (NS) protein, and they could be subdivided into at …

virusesImmunologyCell Culture TechniquesReplicationRNA-dependent RNA polymeraseEukaryotic DNA replicationHepacivirusViral Nonstructural ProteinsBiologyVirus ReplicationOrigin of replicationMicrobiologyReplication factor CControl of chromosome duplicationVirologyTumor Cells Cultured[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumansRepliconVirologyAmino Acid SubstitutionViral replicationInsect ScienceRNA ViralOrigin recognition complexRepliconRibosomes
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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
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Human Papillomavirus Types 16, 18, and 31 Share Similar Endocytic Requirements for Entry

2013

ABSTRACT Human papillomavirus type 18 (HPV18), one of the HPVs with malignant potential, enters cells by an unknown endocytic mechanism. The key cellular requirements for HPV18 endocytosis were tested in comparison to those for HPV16 and -31 endocytoses. HPV18 (like HPV16 and -31) entry was independent of clathrin, caveolin, dynamin, and lipid rafts but required actin polymerization and tetraspanin CD151, and the viruses were routed to the same LAMP-1-positive compartment. Hence, the viruses shared similar cellular requirements for endocytic entry.

virusesImmunologyEndocytic cycleTetraspanin 24EndocytosisMicrobiologyClathrinDynamin IIPolymerizationDynamin IIMembrane MicrodomainsTetraspaninVirologyCaveolinHumansHuman papillomavirus 31Lipid raftDynaminHuman papillomavirus 16Microscopy ConfocalHuman papillomavirus 18biologyvirus diseasesLysosome-Associated Membrane GlycoproteinsVirus InternalizationVirologyActinsEndocytosisVirus-Cell InteractionsCell biologyMicroscopy ElectronMicroscopy FluorescenceInsect Sciencebiology.proteinElectrophoresis Polyacrylamide GelHeLa CellsJournal of Virology
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