Search results for "tetraspanin"

showing 10 items of 27 documents

Tetraspanin CD151 Promotes Initial Events in Human Cytomegalovirus Infection.

2016

ABSTRACT Human cytomegalovirus (HCMV), a betaherpesvirus, can cause life-threatening disease in immunocompromised individuals. Viral envelope glycoproteins that mediate binding to and penetration into target cells have been identified previously. In contrast, cellular proteins supporting HCMV during entry are largely unknown. In order to systematically identify host genes affecting initial steps of HCMV infection, a targeted RNA interference screen of 96 cellular genes was performed in endothelial cells by use of a virus strain expressing the full set of known glycoprotein H and L (gH/gL) complexes. The approach yielded five proviral host factors from different protein families and eight an…

0301 basic medicineHuman cytomegalovirusvirusesImmunologyCytomegalovirusBiologyTetraspanin 24MicrobiologyVirus03 medical and health sciencesViral envelopeTetraspaninViral Envelope ProteinsRNA interferenceVirologymedicineHuman Umbilical Vein Endothelial CellsHumansRNA Small InterferingTropismCells CulturedHost factorchemistry.chemical_classificationFibroblastsVirus Internalizationmedicine.diseaseVirologyVirus-Cell Interactions030104 developmental biologychemistryInsect ScienceRNA InterferenceGlycoproteinGene DeletionJournal of virology
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2014

Human papillomaviruses (HPV) are non-enveloped DNA tumor viruses that infect skin and mucosa. The most oncogenic subtype, HPV16, causes various types of cancer, including cervical, anal, and head and neck cancers. During the multistep process of infection, numerous host proteins are required for the delivery of virus genetic information into the nucleus of target cells. Over the last two decades, many host-cell proteins such as heparan sulfate proteoglycans, integrins, growth factor receptors, actin and the tetraspanin CD151 have been described to be involved in the process of infectious entry of HPV16. Tetraspanins have the ability to organize membrane microdomains and to directly influenc…

biologyIntegrinHPV infectionbiology.organism_classificationmedicine.diseaseVirologyCell biologyInfectious DiseasesGrowth factor receptorTetraspaninViral entryVirologybiology.proteinmedicineSignal transductionPapillomaviridaeReceptorViruses
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2018

Tetraspanins (Tspans) are a family of four-span transmembrane proteins, known as plasma membrane “master organizers.” They form Tspan-enriched microdomains (TEMs or TERMs) through lateral association with one another and other membrane proteins. If multiple microdomains associate with each other, larger platforms can form. For infection, viruses interact with multiple cell surface components, including receptors, activating proteases, and signaling molecules. It appears that Tspans, such as CD151, CD82, CD81, CD63, CD9, Tspan9, and Tspan7, coordinate these associations by concentrating the interacting partners into Tspan platforms. In addition to mediating viral attachment and entry, these …

lcsh:Immunologic diseases. Allergy0301 basic medicineCell signalingTetraspaninsMini ReviewreceptorImmunology610 MedizinbuddingvirusBiologyVirusStructure-Activity Relationship03 medical and health sciencesMembrane MicrodomainsTetraspanintrafficking610 Medical sciencesAnimalsHumansendocytosisImmunology and Allergy030102 biochemistry & molecular biologymicrodomainLipid microdomainMembrane ProteinsVirus InternalizationTransmembrane proteinCell biologytetraspanin030104 developmental biologyMembrane proteinViral replicationVirus DiseasesHost-Pathogen Interactionsentrylcsh:RC581-607BiomarkersCD81Frontiers in Immunology
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Inhibition of tetraspanin functions impairs human papillomavirus and cytomegalovirus infections

2018

Tetraspanins are suggested to regulate the composition of cell membrane components and control intracellular transport, which leaves them vulnerable to utilization by pathogens such as human papillomaviruses (HPV) and cytomegaloviruses (HCMV) to facilitate host cell entry and subsequent infection. In this study, by means of cellular depletion, the cluster of differentiation (CD) tetraspanins CD9, CD63, and CD151 were found to reduce HPV16 infection in HeLa cells by 50 to 80%. Moreover, we tested recombinant proteins or peptides of specific tetraspanin domains on their effect on the most oncogenic HPV type, HPV16, and HCMV. We found that the C-terminal tails of CD63 and CD151 significantly i…

0301 basic medicineHuman cytomegalovirusMaleTelomeraseTetraspaninsviruses610 MedizinCytomegalovirusIC50virus entrylcsh:ChemistryTetraspanin610 Medical scienceshuman papillomaviruslcsh:QH301-705.5SpectroscopyHuman papillomavirus 16virus diseasesGeneral MedicineBiología y Biomedicina / BiologíaEntry into hostComputer Science ApplicationsCytomegalovirus Infectionsembryonic structuresIC<sub>50</sub>HPV16BiologyCatalysisArticleInorganic Chemistry03 medical and health sciencesInhibitory Concentration 50AntigenViral entrymedicineHumansddc:610Physical and Theoretical ChemistryHumanes PapillomavirusMolecular BiologyCluster of differentiationOrganic ChemistryVirus internalizationCytomegalie-VirusIC 50Human papillomavirus virusesmedicine.diseaseVirologyHaCaT030104 developmental biologytetraspaninlcsh:Biology (General)lcsh:QD1-999human cytomegalovirusPeptidesDDC 610 / Medicine &amp; healthblocking peptideHeLa Cells
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Tetraspanins in infections by human cytomegalo- and papillomaviruses

2017

Members of the tetraspanin family have been identified as essential cellular membrane proteins in infectious diseases by nearly all types of pathogens. The present review highlights recently published data on the role of tetraspanin CD151, CD81, and CD63 and their interaction partners in host cell entry by human cytomegalo- and human papillomaviruses. Moreover, we discuss a model for tetraspanin assembly into trafficking platforms at the plasma membrane. These platforms might persist during intracellular viral trafficking.

Models Molecular0301 basic medicineCellular membraneTetraspaninsCytomegalovirusTetraspanin 24BiologyEndocytosismedicine.disease_causeBiochemistryTetraspanin 28Viral Proteins03 medical and health sciencesTetraspaninmedicineHumansPapillomaviridaeCD151Tetraspanin 30Cell MembranePapillomavirus InfectionsCytomegalovirusVirus InternalizationVirologyCell biology030104 developmental biologyCytomegalovirus Infectionsembryonic structuresIntracellularCD81Biochemical Society Transactions
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Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles.

2018

Abstract Background Virtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization…

0301 basic medicineAlix (also known as PDCD6IP)Protein ConformationLipoylationLipid BilayersBiophysicsSkeletal muscle cellsCell Cycle ProteinsExosomesBiochemistryExosomeTetraspanin 29Cell Line03 medical and health sciencesExtracellular VesiclesPalmitoylationTetraspaninExtracellularHumansLipid bilayerMuscle SkeletalMolecular BiologyCells CulturedEndosomal Sorting Complexes Required for TransportChemistryVesicleCalcium-Binding ProteinsCell MembraneExtracellular vesicleTetraspaninSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cell biologyExosomeProtein Transport030104 developmental biologyS-palmitoylationMembrane proteinextracellular vesicles (EVs)Skeletal muscle cellProtein Processing Post-TranslationalProtein BindingSignal TransductionBiochimica et biophysica acta. General subjects
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Quantitative and integrative proteome analysis of peripheral nerve myelin identifies novel myelin proteins and candidate neuropathy loci

2011

Peripheral nerve myelin facilitates rapid impulse conduction and normal motor and sensory functions. Many aspects of myelin biogenesis, glia–axonal interactions, and nerve homeostasis are poorly understood at the molecular level. We therefore hypothesized that only a fraction of all relevant myelin proteins has been identified so far. Combining gel-based and gel-free proteomic approaches, we identified 545 proteins in purified mouse sciatic nerve myelin, including 36 previously known myelin constituents. By mass spectrometric quantification, the predominant P0, periaxin, and myelin basic protein constitute 21, 16, and 8% of the total myelin protein, respectively, suggesting that their relat…

MaleProteomicsCandidate geneProteomePrions10208 Institute of Neuropathology610 Medicine & healthHereditary neuralgic amyotrophyTetraspanin 24BiologySeptinTranscriptomeMice03 medical and health sciencesMyelin0302 clinical medicinemedicineAnimalsElectrophoresis Gel Two-DimensionalRNA MessengerMyelin Sheath030304 developmental biologyMice KnockoutGenetics0303 health sciencesGeneral NeuroscienceComputational BiologyMembrane Proteins2800 General NeuroscienceArticlesmedicine.diseaseSciatic NerveCell biologyMyelin basic proteinMice Inbred C57BLMolecular Weightmedicine.anatomical_structureAnimals Newbornnervous systemSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomebiology.protein570 Life sciences; biologyChemokinesMyelin ProteinsSeptins030217 neurology & neurosurgeryBiogenesisDemyelinating Diseases
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The Cytoskeletal Adaptor Obscurin-Like 1 Interacts with the Human Papillomavirus 16 (HPV16) Capsid Protein L2 and Is Required for HPV16 Endocytosis.

2016

ABSTRACT The human papillomavirus (HPV) capsid protein L2 is essential for viral entry. To gain a deeper understanding of the role of L2, we searched for novel cellular L2-interacting proteins. A yeast two-hybrid analysis uncovered the actin-depolymerizing factor gelsolin, the membrane glycoprotein dysadherin, the centrosomal protein 68 (Cep68), and the cytoskeletal adaptor protein obscurin-like 1 protein (OBSL1) as putative L2 binding molecules. Pseudovirus (PsV) infection assays identified OBSL1 as a host factor required for gene transduction by three oncogenic human papillomavirus types, HPV16, HPV18, and HPV31. In addition, we detected OBSL1 expression in cervical tissue sections and no…

0301 basic medicineKeratinocytesvirusesImmunologyEndocytic cycleEndocytosisMicrobiologyClathrinCell Line03 medical and health sciencesTransduction (genetics)TetraspaninViral entryVirologyTwo-Hybrid System TechniquesCaveolinHumansHuman papillomavirus 16biologyPapillomavirus InfectionsSignal transducing adaptor proteinOncogene Proteins ViralVirus InternalizationEndocytosisCell biologyVirus-Cell InteractionsCytoskeletal Proteins030104 developmental biologyInsect ScienceGene Knockdown TechniquesHost-Pathogen Interactionsbiology.proteinCapsid ProteinsHeLa CellsJournal of virology
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Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane

2021

The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional protein clusters within the plasma membrane into so-called Tetraspanin-enriched microdomains (TEMs). Direct interactions between Tetraspanins are believed to be important for this organization. However, studies thus far have utilized mainly co-immunoprecipitation methods that cannot distinguish between direct and indirect, through common partners, interactions. Here we study Tetraspanin 8 homointeractions in living cells via quantitative fluorescence microscopy. We demonstrate that Tetraspanin 8 exists i…

Cell signalingTetraspaninsLipoylationDimerTransfectionBiochemistryArticleProtein–protein interactionchemistry.chemical_compoundMembrane MicrodomainsTetraspaninFluorescence Resonance Energy TransferHumansMolecular BiologyChemistryCell BiologyDissociation constantHEK293 CellsMembraneMicroscopy FluorescenceMembrane proteinembryonic structuresBiophysicsThermodynamicsProtein MultimerizationSignal transductionSignal TransductionBiochemical Journal
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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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