0000000000004483

AUTHOR

Katrin A. Becker

showing 4 related works from this author

Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

2003

Abstract We have recently shown that the minor capsid protein L2 of human papillomavirus type 33 (HPV33) recruits the transcriptional repressor Daxx into nuclear domains (ND) 10 and causes the loss of the transcriptional activator Sp100 from these subnuclear structures (Florin et al., 2002b) . In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed. Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (S…

ImmunoprecipitationRecombinant Fusion ProteinsGreen Fluorescent ProteinsNuclear Localization SignalsActive Transport Cell NucleusFluorescent Antibody TechniqueBiologyImmunofluorescenceAutoantigensGreen fluorescent proteinDeath-associated protein 6DaxxVirologyTumor Cells CulturedmedicineSp100HumansNLSPapillomaviridaeAdaptor Proteins Signal TransducingCell Nucleusmedicine.diagnostic_testIntracellular Signaling Peptides and ProteinsND10Nuclear ProteinsAntigens NuclearL2Oncogene Proteins ViralPapillomavirusbiochemical phenomena metabolism and nutritionMolecular biologyDeletion MutagenesisLuminescent ProteinsCapsidMutagenesisCapsid ProteinsCarrier ProteinsCo-Repressor ProteinsGene DeletionNuclear localization sequenceMolecular ChaperonesVirology
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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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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Identification of a Dynein Interacting Domain in the Papillomavirus Minor Capsid Protein L2

2006

ABSTRACT Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluoresce…

ImmunoprecipitationImmunologyDyneinActive Transport Cell NucleusGenome ViralMicrotubulesMicrobiologyMotor proteinPromyelocytic leukemia proteinMicrotubuleDynein ATPaseVirologyHumansPapillomaviridaebiologyPapillomavirus InfectionsDyneinsOncogene Proteins ViralMolecular biologyEndocytosisVirus-Cell InteractionsMicroscopy FluorescenceCapsidInsect ScienceDNA Viralbiology.proteinDynactinCapsid ProteinsIntranuclear SpaceHeLa CellsProtein BindingJournal of Virology
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