Search results for "membrane"

showing 10 items of 4477 documents

Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling

2021

Abstract The sensor kinase DcuS of Escherichia coli perceives extracellular fumarate by a periplasmic PASP sensor domain. Transmembrane (TM) helix TM2, present as TM2-TM2′ homo-dimer, transmits fumarate activation in a piston-slide across the membrane. The second TM helix of DcuS, TM1, is known to lack piston movement. Structural and functional properties of TM1 were analyzed. Oxidative Cys-crosslinking (CL) revealed homo-dimerization of TM1 over the complete membrane, but only the central part showed α-helical +3/+4 spacing of the CL maxima. The GALLEX bacterial two-hybrid system indicates TM1/TM1′ interaction, and the presence of a TM1-TM1′ homo-dimer is suggested. The peripheral TM1 regi…

urogenital systemChemistryClinical BiochemistryPeriplasmic spaceOxidative phosphorylationmedicine.disease_causeBiochemistryTransmembrane proteinTransmembrane domainMembraneMembrane regionHelixmedicineBiophysicsMolecular BiologyEscherichia coliBiological Chemistry
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Impact assessment of a solar powered water treatment project

2015

Water treatment technologies are seen as the best alternative to be considered for adoption in developing countries where access to portable water supply that is free of pathogens is yet a challenge. This study intended to assess impact brought forth by a project, which employed a water treatment technology in rural settings of Morogoro Region in Tanzania. The project used solar photovoltaic panels to trap solar energy, converted to mechanical power to treat water with the help of sterilization ultraviolet membrane. A comparative analysis was used as an assessment framework to study impacts of the project with respect to the quality of approach used during the project life cycle. Determinan…

vaikutuksetUV membraneSolar EnergyAssessmentaurinkoenergiavedenkäsittelyarviointiWater Treatment System
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CYGD: the Comprehensive Yeast Genome Database.

2005

The comprehensive resource is available under http://mips.gsf.de/genre/proj/yeast/.; International audience; The Comprehensive Yeast Genome Database (CYGD) compiles a comprehensive data resource for information on the cellular functions of the yeast Saccharomyces cerevisiae and related species, chosen as the best understood model organism for eukaryotes. The database serves as a common resource generated by a European consortium, going beyond the provision of sequence information and functional annotations on individual genes and proteins. In addition, it provides information on the physical and functional interactions among proteins as well as other genetic elements. These cellular network…

ved/biology.organism_classification_rank.speciesSACCHAROMYCES CEREVISIAE GENOME;COMPREHENSIVE YEAST GENOME DATABASE;CYGD;PROTEIN INTERACTION;EUROPEAN CONSORTIUM;SEQUENCE INFORMATION;YEAST GENOME;SEQUENCED EUKARYOTIC GENOMEcomputer.software_genreGenomeSaccharomycesUser-Computer InterfaceSequence Analysis ProteinDatabases GeneticYEAST GENOME[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]0303 health sciences[SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]biologyDatabase030302 biochemistry & molecular biologyEUROPEAN CONSORTIUMArticlesGenomicsCYGD[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]PROTEIN INTERACTIONSEQUENCED EUKARYOTIC GENOMEnucleic acidsCOMPREHENSIVE YEAST GENOME DATABASEBio-informatiqueGenome FungalSEQUENCE INFORMATIONSaccharomyces cerevisiae ProteinsBioinformaticsSaccharomyces cerevisiae610Saccharomyces cerevisiaeGenètica molecularSACCHAROMYCES CEREVISIAE GENOMESaccharomyces03 medical and health sciencesAnnotationGeneticsSIMAPModel organismGene030304 developmental biologyBinding Sitesved/biologyMembrane ProteinsMembrane Transport Proteinsbiology.organism_classificationYeast[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]computerSDV:BIBSTranscription Factors
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Infection-induced chromatin modifications facilitate translocation of herpes simplex virus capsids to the inner nuclear membrane

2021

Herpes simplex virus capsids are assembled and packaged in the nucleus and move by diffusion through the nucleoplasm to the nuclear envelope for egress. Analyzing their motion provides conclusions not only on capsid transport but also on the properties of the nuclear environment during infection. We utilized live-cell imaging and single-particle tracking to characterize capsid motion relative to the host chromatin. The data indicate that as the chromatin was marginalized toward the nuclear envelope it presented a restrictive barrier to the capsids. However, later in infection this barrier became more permissive and the probability of capsids to enter the chromatin increased. Thus, although …

virusesGene ExpressionVirus ReplicationPathology and Laboratory Medicineherpes simplex -virusChlorocebus aethiopsCapsidsMedicine and Health SciencesSimplexvirusBiology (General)Mass DiffusivityStainingChromosome BiologyPhysicsChromatinChemistryMedical MicrobiologyViral PathogensPhysical SciencesVirusesHerpes Simplex Virus-1EpigeneticsCellular Structures and OrganellesPathogenskapsidiResearch ArticleHerpesvirusesNuclear EnvelopeQH301-705.5Biological Transport ActiveViral StructureResearch and Analysis MethodsinfektiotMicrobiologydiffuusio (fysikaaliset ilmiöt)CapsidNuclear MembraneVirologyGeneticsAnimalsherpesviruksetVero CellsMicrobial PathogensCell NucleusChemical PhysicsOrganismsBiology and Life SciencesHerpes SimplexCell Biologybiochemical phenomena metabolism and nutritionRC581-607Viral ReplicationHerpes Simplex VirusNuclear StainingSpecimen Preparation and TreatmentImmunologic diseases. AllergyDNA viruses
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The Nasal Epithelium as a Factory for Systemic Protein Delivery

2002

We have previously shown that recombinant Sendai virus (SeV) produces efficient in vivo airway epithelial gene transfer. The ability to produce therapeutic levels of circulating proteins following noninvasive gene transfer would have widespread clinical application. Here, we compared nose, lung, and skeletal muscle for the ability to produce circulating levels of the secreted mouse antiinflammatory cytokine interleukin-10 (IL10) following SeV-mediated gene transfer. High levels of serum IL10 were obtained from each site with a potency order of lung > nose > muscle for a given viral titer. Serum levels from each site were within the likely required range for anti-inflammatory effects. The co…

virusesGenetic enhancementmedicine.medical_treatmentMucous membrane of noseSendai virus03 medical and health sciences0302 clinical medicineIn vivoDrug DiscoverymedicineGeneticsAnimalsHumansMuscle SkeletalLungMolecular BiologyNose030304 developmental biologyPharmacology0303 health sciencesLungbiologyGene Transfer TechniquesSkeletal musclerespiratory systembiology.organism_classificationSendai virus3. Good healthInterleukin-10Nasal Mucosamedicine.anatomical_structureCytokine030220 oncology & carcinogenesisImmunologyCOS CellsMolecular MedicineHeLa CellsMolecular Therapy
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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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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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The closest relatives of icosahedral viruses of thermophilic bacteria are among viruses and plasmids of the halophilic archaea.

2009

We have sequenced the genome and identified the structural proteins and lipids of the novel membranecontaining, icosahedral virus P23-77 of Thermus thermophilus. P23-77 has an 17-kb circular double-stranded DNA genome, which was annotated to contain 37 putative genes. Virions were subjected to dissociation analysis, and five protein species were shown to associate with the internal viral membrane, while three were constituents of the protein capsid. Analysis of the bacteriophage genome revealed it to be evolutionarily related to another Thermus phage (IN93), archaeal Halobacterium plasmid (pHH205), a genetic element integrated into Haloarcula genome (designated here as IHP for integrated Ha…

virusesImmunologyMicrobiologyGenomeVirusBacteriophage03 medical and health sciencesBacterial ProteinsVirologyGeneVirus classificationPhylogeny030304 developmental biologyGeneticsAdenosine Triphosphatases0303 health sciencesbiologyBase Sequence030306 microbiologyThermus thermophilusMembrane ProteinsViral membraneProvirusbiology.organism_classificationLipidsGenetic Diversity and EvolutionVirion assemblyGenes BacterialInsect ScienceCapsid ProteinsGenome BacterialJournal of virology
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Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix

2019

Abstract Coat protein (COP) I and COP II complexes are involved in the transport of proteins between the endoplasmic reticulum and the Golgi apparatus in eukaryotic cells. The formation of COP I/II complexes at membrane surfaces is an early step in vesicle formation and is mastered by p24, a type I transmembrane protein. Oligomerization of p24 monomers was suggested to be mediated and/or stabilized via interactions within the transmembrane domain, and the p24 transmembrane helix appears to selectively bind a single sphingomyelin C18:0 molecule. Furthermore, a potential cholesterol-binding sequence has also been predicted in the p24 transmembrane domain. Thus, sphingomyelin and/or cholestero…

virusesLipid BilayersBiophysicsProtein Structure Secondary03 medical and health sciencessymbols.namesake0302 clinical medicineimmune system diseasesAmino Acid Sequence030304 developmental biology0303 health sciencesChemistryEndoplasmic reticulumVesicleCholesterol bindingvirus diseasesArticlesCOPIGolgi apparatusLipidsTransmembrane proteinSphingomyelinsTransmembrane domainCholesterolsymbolsBiophysicsCapsid Proteinslipids (amino acids peptides and proteins)SphingomyelinDimerization030217 neurology & neurosurgeryBiophysical Journal
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The Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs

2014

AbstractCD81 is a ubiquitously expressed member of the tetraspanin family. It forms large molecular platforms, so-called tetraspanin webs that play physiological roles in a variety of cellular functions and are involved in viral and parasite infections. We have investigated which part of the CD81 molecule is required for the formation of domains in the cell membranes of T-cells and hepatocytes. Surprisingly, we find that large CD81 platforms assemble via the short extracellular δ-domain, independent from a strong primary partner binding and from weak interactions mediated by palmitoylation. The δ-domain is also essential for the platforms to function during viral entry. We propose that, ins…

virusesLipoylationBiophysicschemical and pharmacologic phenomenaPlasma protein bindingBiologyTetraspanin 28Jurkat CellsProtein structurePalmitoylationTetraspaninViral entryExtracellularHumansComputingMilieux_MISCELLANEOUS[PHYS]Physics [physics]MembranesHep G2 Cellsbiochemical phenomena metabolism and nutritionCell biologyProtein Structure TertiaryProtein MultimerizationProtein Processing Post-TranslationalFunction (biology)CD81Protein Binding
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