Search results for "Phosphoprotein"

showing 10 items of 160 documents

Modification of the major tegument protein pp65 of human cytomegalovirus inhibits virus growth and leads to the enhancement of a protein complex with…

2010

The tegument protein pp65 of human cytomegalovirus (HCMV) is abundant in lytically infected human foreskin fibroblasts (HFF), as well as in virions and subviral dense bodies (DB). Despite this, we showed previously that pp65 is dispensable for growth in HFF. In the process of refining a DB-based vaccine candidate, different HCMV mutants were generated, expressing a dominant HLA-A2-presented peptide of the IE1 protein fused to pp65. One of the mutant viruses (RV-VM1) surprisingly showed marked impairment in virus release from HFF. We hypothesized that analysis of the phenotypic alterations of RV-VM1 would provide insight into the functions of pp65, poorly defined thus far. RV-VM1 infection r…

Human cytomegalovirusImmunoprecipitationvirusesMutantCytomegalovirusBiologyVirus ReplicationVirusInclusion bodiesViral Matrix ProteinsViral ProteinsVirologymedicineHumansImmunoprecipitationCells Culturedvirus diseasesRNAViral tegumentFibroblastsPhosphoproteinsmedicine.diseaseVirologyFusion proteinTrans-ActivatorsProtein MultimerizationProtein BindingJournal of General Virology
researchProduct

Experimental Preemptive Immunotherapy of Murine Cytomegalovirus Disease with CD8 T-Cell Lines Specific for ppM83 and pM84, the Two Homologs of Human …

2001

ABSTRACTCD8 T cells are the principal antiviral effectors controlling cytomegalovirus (CMV) infection. For human CMV, the virion tegument protein ppUL83 (pp65) has been identified as a source of immunodominant peptides and is regarded as a candidate for cytoimmunotherapy and vaccination. Two sequence homologs of ppUL83 are known for murine CMV, namely the virion protein ppM83 (pp105) expressed late in the viral replication cycle and the nonstructural protein pM84 (p65) expressed in the early phase. Here we show that ppM83, unlike ppUL83, is not delivered into the antigen presentation pathway after virus penetration before or in absence of viral gene expression, while other virion proteins o…

Human cytomegalovirusMuromegalovirusmedicine.medical_treatmentImmunologyImmunodominanceCD8-Positive T-LymphocytesBiologyMicrobiologyCell LineViral Matrix ProteinsInterferon-gammaMiceImmune systemAntigenVirologyVaccines and Antiviral AgentsmedicineAnimalsCytotoxic T cellMice Inbred BALB CHerpesviridae InfectionsImmunotherapyPhosphoproteinsmedicine.diseaseAdoptive TransferVirologyPeptide FragmentsDisease Models AnimalViral replicationInsect ScienceImmunologyFemaleCytokine secretionImmunologic MemoryJournal of Virology
researchProduct

The immunogenicity of human and murine cytomegaloviruses.

2000

Cytomegaloviruses are strictly host-species-specific. During an aeon of co-evolution, virus and host have found an arrangement: the productive and cytopathogenic cycle of viral gene expression is held in check by the host's immune response. As a consequence, cytomegalovirus disease is restricted to the immunocompromised host. The virus has evolved strategies to avoid its elimination and eventually hides itself in a silent state, referred to as 'viral latency'. Redundant molecular mechanisms have been identified by which cytomegaloviruses interfere with antigen presentation pathways to 'evade' immune control. In the annual period covered by this review, the IE1 protein was revisited as an im…

Human cytomegalovirusMuromegalovirusvirusesImmunologyAntigen presentationCongenital cytomegalovirus infectionCytomegalovirusImmunodominanceBiologyVirusImmediate early proteinImmediate-Early ProteinsViral Matrix ProteinsMiceViral ProteinsAntigenmedicineImmunology and AllergyAnimalsHumansAntigen PresentationImmunogenicityHistocompatibility Antigens Class IIvirus diseasesReceptors Antigen T-Cell gamma-deltamedicine.diseasePhosphoproteinsVirologyKiller Cells NaturalImmunologyCurrent opinion in immunology
researchProduct

Immune evasion proteins gpUS2 and gpUS11 of human cytomegalovirus incompletely protect infected cells from CD8 T cell recognition

2009

AbstractHuman cytomegalovirus (HCMV) encodes four glycoproteins, termed gpUS2, gpUS3, gpUS6 and gpUS11 that interfere with MHC class I biosynthesis and antigen presentation. Despite gpUS2–11 expression, however, HCMV infection is efficiently controlled by cytolytic CD8 T lymphocytes (CTL). To address the role of gpUS2 and gpUS11 in antigen presentation during viral infection, HCMV mutants were generated that expressed either gpUS2 or gpUS11 alone without coexpression of the three other proteins. Fibroblasts infected with these viruses showed reduced HLA-A2 and HLA-B7 surface expression. Surprisingly, however, CTL directed against the tegument protein pp65 and the regulatory IE1 protein stil…

Human cytomegalovirusvirusesAntigen presentationIE1CytomegalovirusCD8-Positive T-LymphocytesVirus ReplicationMajor histocompatibility complexpp65US2Immediate-Early ProteinsViral Matrix ProteinsHLA-B7 AntigenInterferon-gammaViral ProteinsImmune systemViral Envelope ProteinsVirologyHLA-A2 AntigenMHC class ImedicineHumansCytotoxic T cellCells CulturedAntigen PresentationbiologyImmune evasionRNA-Binding Proteinsvirus diseasesbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseVirologyCTL*MutagenesisCTLCytomegalovirus InfectionsMHC class Ibiology.proteinUS11CD8Virology
researchProduct

Polo-like kinase 1 as a target for human cytomegalovirus pp65 lower matrix protein

1999

ABSTRACT Human cytomegalovirus (HCMV) pp65 protein is the major constituent of viral dense bodies but is dispensable for viral growth in vitro. pp65 copurifies with a S/T kinase activity and has been implicated in phosphorylation of HCMV IE1 immediate-early protein and its escape from major histocompatibility complex 1 presentation. Furthermore, the presence of pp65 correlates with a virion-associated kinase activity. To clarify the role of pp65, yeast two-hybrid system (THS) screening was performed to identify pp65 cellular partners. A total of 18 out of 48 yeast clones harboring cDNAs for putative pp65 binding proteins encoded the Polo-like kinase 1 (Plk1) C-terminal domain. Plk1 behaved …

Human cytomegalovirusvirusesRecombinant Fusion ProteinsImmunologyCytomegalovirusCell Cycle ProteinsPolo-like kinaseBiologyProtein Serine-Threonine KinasesMicrobiologyDNA-binding proteinPLK1Cell LineViral Matrix ProteinsVirologyProto-Oncogene ProteinsmedicineAnimalsHumansKinase activityViral matrix proteinKinasevirus diseasesmedicine.diseasePhosphoproteinsMolecular biologyVirus-Cell Interactionssurgical procedures operativeInsect ScienceCOS CellsPhosphorylationProtein KinasesHeLa Cells
researchProduct

Cross-talk between oxidative stress and pro-inflammatory cytokines in acute pancreatitis: a key role for protein phosphatases.

2009

Acute pancreatitis is an acute inflammatory process localized in the pancreatic gland that frequently involves peripancreatic tissues. It is still under investigation why an episode of acute pancreatitis remains mild affecting only the pancreas or progresses to a severe form leading to multiple organ failure and death. Proinflammatory cytokines and oxidative stress play a pivotal role in the early pathophysiological events of the disease. Cytokines such as interleukin 1beta and tumor necrosis factor alpha initiate and propagate almost all consequences of the systemic inflammatory response syndrome. On the other hand, depletion of pancreatic glutathione is an early hallmark of acute pancreat…

Inflammationmedicine.disease_causeProinflammatory cytokineDrug DiscoveryPhosphoprotein PhosphatasesMedicineAnimalsHumansPharmacologyInflammationbiologybusiness.industrymedicine.diseaseSystemic inflammatory response syndromeOxidative StressPancreatitisMitogen-activated protein kinaseImmunologyAcute Diseasebiology.proteinAcute pancreatitisPancreatitisCytokinesTumor necrosis factor alphamedicine.symptomMitogen-Activated Protein KinasesbusinessOxidation-ReductionOxidative stressSignal TransductionCurrent pharmaceutical design
researchProduct

Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta.

2002

The integrins are a large family of heterodimeric transmembrane receptors composed of α and β subunits (22). In addition to mediating cell-matrix interactions, integrins have been shown to activate intracellular signaling pathways which, in collaboration with growth factor-induced signals, regulate cellular functions (46). Some integrin signaling cascades are activated via the β subunit cytoplasmic domain, and they are therefore triggered by several integrin heterodimers. These signals include the activation of protein tyrosine kinases of the Src and focal adhesion kinase (FAK) families (9, 47). More-recent studies have revealed signaling events that are activated specifically by an α subun…

IntegrinsReceptors CollagenIntegrinProtein Serine-Threonine KinasesCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorGlycogen Synthase Kinase 3Proto-Oncogene ProteinsCell AdhesionPhosphoprotein PhosphatasesHumansIntegrin-linked kinaseProtein Phosphatase 2cdc42 GTP-Binding ProteinMolecular BiologyCell Growth and DevelopmentCells CulturedbiologyAkt/PKB signaling pathwayCell adhesion moleculeGlycogen Synthase KinasesCell BiologyCell biologyEnzyme ActivationBiochemistryIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6CollagenMitogen-Activated Protein KinasesProto-Oncogene Proteins c-aktProtein BindingSignal TransductionMolecular and cellular biology
researchProduct

Induction of interferon regulatory factors, 2′‐5′ oligoadenylate synthetase, P68 kinase and RNase L in chronic myelogenous leukaemia cells and its re…

1996

The genes crucially determining the therapeutic response of chronic myelogenous leukaemia (CML) to interferon-alpha (IFN-alpha) are unknown. Recently, two independent IFN-alpha signalling pathways were identified: the classic pathway mediates induction of 2'-5' oligoadenylate synthetase (2-5 OAS), p68 kinase and IFN regulatory factor-2 (IRF-2), whereas the alternate pathway leads to activation of IFN regulatory factor-1 (IRF-1). We investigated whether deficient or imbalanced expression of components of these two pathways is associated with resistance of CML cells to antiproliferative action of IFN alpha/beta. Constitutive and IFN-induced transcript levels of IFN-dependent genes in mononucl…

Interferon Regulatory Factor 2T-LymphocytesCellular differentiationmedicine.medical_treatmentProtein Serine-Threonine KinaseseIF-2 KinaseLeukemia Myelogenous Chronic BCR-ABL PositiveEndoribonucleases2'5'-Oligoadenylate SynthetasemedicineHumansRNA MessengerTreatment FailureInterferon alfaEIF-2 kinasebiology2'-5'-OligoadenylateInterferon-alphaHematologyBlotting NorthernHematopoietic Stem CellsPhosphoproteinsDNA-Binding ProteinsGene Expression Regulation NeoplasticRepressor ProteinsCytokineIRF1Cancer researchbiology.proteinInterferon Regulatory Factor-2GranulocytesInterferon Regulatory Factor-1Transcription Factorsmedicine.drugInterferon regulatory factorsBritish Journal of Haematology
researchProduct

Functional analysis of the -2548G/A leptin gene polymorphism in breast cancer cells

2009

Leptin is overexpressed in human breast tumors and is produced by breast cancer cells in response to obesity-related stimuli. The leptin promoter polymorphism Lep-2548G/A can be associated with increased leptin secretion by adipocytes and elevated cancer risk. However, molecular mechanisms underlying the link between Lep-2548G/A and breast cancer have never been addressed. Lep-2548G/A is proximal to a binding site for the transcriptional factor Sp1. Furthermore nucleolin, a transcriptional repressor, can bind Sp1 or its consensus site. Consequently, we focused on the impact of Lep-2548G/A on Sp1- and nucleolin-dependent leptin transcription in breast cancer cells. The Lep-2548G/A was identi…

LeptinChromatin ImmunoprecipitationCancer Researchmedicine.medical_specialtyGenotypeSp1 Transcription FactorBlotting WesterneducationAdipokineBreast NeoplasmsBiologyBody Mass IndexBreast cancerInternal medicineTumor Cells CulturedmedicineHumansHypoglycemic AgentsInsulinObesityRNA MessengerPromoter Regions Genetichealth care economics and organizationsPolymorphism GeneticLeptin receptorReverse Transcriptase Polymerase Chain ReactionLeptinRNA-Binding ProteinsCancerPhosphoproteinsmedicine.diseaseEndocrinologyOncologyCancer researchImmunohistochemistryBreast diseaseNucleolinhormones hormone substitutes and hormone antagonistsInternational Journal of Cancer
researchProduct

Use of CDC2 from etoposide-treated cells as substrate to assay CDC25 phosphatase activity

1999

International audience; Cyclin-dependent kinases (CDKs) regulate the key transition of the cell cycle in all organisms. In response to Etoposide (VP-16) induced DNA damage, cells undergo a G2-phase arrest resulting in the accumulation of inactive CDK1 (CDC2) kinase complexes. Here we report that upon Etoposide treatment CDC2 is phosphorylated on tyrosine 15 and is dephosphorylated and activated in vitro by recombinant CDC25 phosphatase. We also show that inactive CDC2 kinase from Etoposide-treated cells can be used as a substrate in a sensitive two-step assay of CDC25 phosphatase. This assay, which is very simple to set-up, is based on the monitoring of CDC2 kinase activity after CDC25-depe…

MESH: HumansMESH: Phosphorylation[SDV]Life Sciences [q-bio]Cell Cycle Proteins[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]MESH: CDC2 Protein KinaseMESH: Tyrosine[SDV] Life Sciences [q-bio]AGENT ANTITUMORALenzymes and coenzymes (carbohydrates)MESH: Cell Cycle ProteinsMESH: cdc25 PhosphatasesCDC2 Protein KinaseMESH: HeLa CellsMESH: Phosphoprotein PhosphatasesPhosphoprotein PhosphatasesHumansTyrosinecdc25 PhosphatasesPhosphorylationbiological phenomena cell phenomena and immunityEtoposideHeLa CellsMESH: Etoposide
researchProduct