Search results for "ONCOGENE"

showing 5 items of 1005 documents

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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Human Papillomavirus Type 16 E7 Peptide-Directed CD8+ T Cells from Patients with Cervical Cancer Are Cross-Reactive with the Coronavirus NS2 Protein

2003

ABSTRACTHuman papillomavirus type 16 (HPV16) E6 and E7 oncoproteins are required for cellular transformation and represent candidate targets for HPV-specific and major histocompatibility complex class I-restricted CD8+-T-cell responses in patients with cervical cancer. Recent evidence suggests that cross-reactivity represents the inherent nature of the T-cell repertoire. We identified HLA-A2 binding HPV16 E7 variant peptides from human, bacterial, or viral origin which are able to drive CD8+-T-cell responses directed against wild-type HPV16 E7 amino acid 11 to 19/20 (E711-19/20) epitope YMLDLQPET(T) in vitro. CD8+T cells reacting to the HLA-A2-presented peptide from HPV16 E711-19(20)recogni…

virusesPapillomavirus E7 ProteinsImmunologyMolecular Sequence DataPriming (immunology)Epitopes T-LymphocyteUterine Cervical NeoplasmsCD8-Positive T-LymphocytesCross ReactionsViral Nonstructural Proteinsmedicine.disease_causeMajor histocompatibility complexLymphocyte ActivationMicrobiologyEpitopeImmune systemVirologyHLA-A2 AntigenmedicineCytotoxic T cellHumansHuman coronavirus OC43Amino Acid SequencePapillomaviridaeCoronavirusbiologyPapillomavirus Infectionsvirus diseasesOncogene Proteins Viralbiology.organism_classificationVirologyMolecular biologyCoronavirusTumor Virus InfectionsInsect Sciencebiology.proteinPathogenesis and ImmunityFemalePeptidesCD8Journal of Virology
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Evaluation of HBs, HBc, and frCP virus-like particles for expression of human papillomavirus 16 E7 oncoprotein epitopes.

2002

<i>Objectives:</i> In an attempt to develop virus-like particles (VLPs) as experimental vaccine against human papilloma virus (HPV)-induced tumours, the HPV16 E7 oncoprotein epitopes spanning amino acid (aa) residues 35–98 were expressed on three proteins capable of VLP formation: hepatitis B virus (HBV) surface (HBs) and core (HBc) antigens, and RNA phage fr coats (frCP). <i>Methods:</i> The profile of immunoglobulin isotypes induced in Balb/C mice after immunization with purified chimeric proteins was studied. <i>Results:</i> The HBs*-E7(35–54) protein expressing E7 residues 35–54 between residues 139 and 142 of the HBs carrier formed HBs-like particles…

virusesPapillomavirus E7 ProteinsRecombinant Fusion ProteinsMolecular Sequence DataRNA PhagesAntibodies ViralEpitopeVirusEpitopesMiceHpv16 e7Immune systemCapsidPapillomavirus E7 ProteinsVirologyAnimalsHumansAmino Acid SequenceHuman papillomavirusneoplasmsMice Inbred BALB CHepatitis B Surface AntigensbiologyVirionvirus diseasesOncogene Proteins ViralVirologyHepatitis B Core Antigensfemale genital diseases and pregnancy complicationsImmunoglobulin IsotypesInfectious DiseasesImmunizationbiology.proteinFemaleImmunizationAntibodyIntervirology
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