Search results for "sequence data"

showing 10 items of 1952 documents

Antibody Induction Directed against the Tumor-Associated MUC4 Glycoprotein

2015

Mucin glycoproteins are important diagnostic and therapeutic targets for cancer treatment. Although several strategies have been developed to explore anti-tumor vaccines based on MUC1 glycopeptides, only few studies have focused on vaccines directed against the tumor-associated MUC4 glycoprotein. MUC4 is an important tumor marker overexpressed in lung cancer and uniquely expressed in pancreatic ductual adenocarcinoma. The aberrant glycosylation of MUC4 in tumor cells results in an exposure of its peptide backbone and the formation of tumor-associated glycopeptide antigens. Due to the low immunogenicity of these endogenous structures, their conjugation with immune stimulating peptide or prot…

Antibodies NeoplasmMolecular Sequence DataCancer VaccinesBiochemistryEpitopeEpitopesMiceAntigenAntibody SpecificityCell Line TumorTetanus ToxoidAnimalsHumansAmino Acid SequenceMolecular BiologyMUC1chemistry.chemical_classificationMice Inbred BALB CMucin-4biologyImmune SeraImmunogenicityVaccinationOrganic ChemistryToxoidGlycopeptidePancreatic NeoplasmschemistryTandem Repeat SequencesImmunologybiology.proteinMolecular MedicineFemalesense organsAntibodyGlycoproteinChemBioChem
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Antibody Complementarity-Determining Regions (CDRs) Can Display Differential Antimicrobial, Antiviral and Antitumor Activities

2008

9 p. Background: Complementarity-determining regions (CDRs) are immunoglobulin (Ig) hypervariable domains that determine specific antibody (Ab) binding. We have shown that synthetic CDR-related peptides and many decapeptides spanning the variable region of a recombinant yeast killer toxin-like antiidiotypic Ab are candidacidal in vitro. An alanine-substituted decapeptide from the variable region of this Ab displayed increased cytotoxicity in vitro and/or therapeutic effects in vivo against various bacteria, fungi, protozoa and viruses. The possibility that isolated CDRs, represented by short synthetic peptides, may display antimicrobial, antiviral and antitumor activities irrespective of Ab…

Antifungal AgentsBIOCHEMISTRY AND MOLECULAR BIOLOGYMolecular Sequence DataImmunologylcsh:MedicineAntineoplastic AgentsMicrobial Sensitivity TestsComplementarity determining regionBiologyAntiviral AgentsOncology/Skin CancersAntibodiesMiceMicrobiology/Applied MicrobiologyAntigenBiochemistry/Protein ChemistryInfectious Diseases/Fungal InfectionsIn vivoCell Line TumorCandida albicansInfectious Diseases/Viral InfectionsAnimalsHumansAmino Acid Sequencelcsh:SciencePeptide sequenceMultidisciplinaryMEDICINElcsh:RAntimicrobialComplementarity Determining RegionsVirologyIn vitroOncologyBiochemistryViral replicationAGRICULTURAL AND BIOLOGICAL SCIENCESVirology/Immunodeficiency VirusesHIV-1biology.proteinlcsh:QAntibodyResearch ArticlePLoS ONE
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Diversity and Evolution of the Phenazine Biosynthesis Pathway

2010

ABSTRACT Phenazines are versatile secondary metabolites of bacterial origin that function in biological control of plant pathogens and contribute to the ecological fitness and pathogenicity of the producing strains. In this study, we employed a collection of 94 strains having various geographic, environmental, and clinical origins to study the distribution and evolution of phenazine genes in members of the genera Pseudomonas , Burkholderia , Pectobacterium , Brevibacterium , and Streptomyces . Our results confirmed the diversity of phenazine producers and revealed that most of them appear to be soil-dwelling and/or plant-associated species. Genome analyses and comparisons of phylogenies inf…

Antifungal Agentsgenome sequenceaeruginosa pao1virulence factorsphenazine-1-carboxylic acidVIRULENCE FACTORS GENE-CLUSTERApplied Microbiology and Biotechnologychemistry.chemical_compoundGene clusterEnvironmental MicrobiologyPhylogenySoil Microbiologyfluorescent pseudomonas2. Zero hungerGenetics0303 health sciencesEcologybiologyEPS-2PseudomonasPlants[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMultigene FamilyHorizontal gene transferBiotechnologyDNA BacterialWashingtonPectobacteriumGene Transfer HorizontalGenotypeSequence analysisMolecular Sequence DataPhenazineerwinia-herbicola eh1087pseudomonas-chlororaphis pcl1391Evolution Molecular03 medical and health sciencesBacterial ProteinsPseudomonasBotanyEscherichia coli030304 developmental biologyBacteriaBase SequencePSEUDOMONAS-CHLORORAPHIS030306 microbiologybiological-controlGene Expression Regulation BacterialSequence Analysis DNA15. Life on landbiology.organism_classificationrpoBERWINIA-HERBICOLAPHENAZINEBiosynthetic Pathwaysgene-clusterLaboratorium voor PhytopathologieBurkholderiachemistryGenes BacterialLaboratory of PhytopathologyPhenazinesburkholderia-cepacia complexSequence AlignmentFood Science
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Steroidal saponins from the roots of Smilax aspera subsp. mauritanica

2008

Two new steroidal saponins (1, 2) were isolated from the roots of Smilax aspera subsp. mauritanica (POIR.) ARCANG. (Liliaceae), together with the known curillin G (3), asparagoside E (4), asparoside A (5), asparoside B (6) and the phenolic compound resveratrol (7). Their structures were established mainly on the basis of 600 MHz 2D-NMR spectral data. 3 exhibited antifungal activity against the human pathogenic yeasts Candida albicans, C. glabrata and C. tropicalis (minimum inhibitory concentrations of 25, 25 and 50 microg/ml, respectively) whereas the other compounds were inactive.

AntifungalSpectrometry Mass Electrospray IonizationAntifungal AgentsMagnetic Resonance SpectroscopySpectrophotometry Infraredmedicine.drug_classMolecular Sequence DataPharmaceutical ScienceMicrobial Sensitivity TestsSpectrometry Mass Fast Atom BombardmentResveratrolPlant RootsAnalytical Chemistrychemistry.chemical_compoundDrug DiscoveryBotanymedicineCandida albicansSpectral dataSmilax asperaCandidaPharmacologybiologyTraditional medicineLiliaceaeHydrolysisOrganic ChemistryFungiGeneral ChemistryGeneral MedicineSaponinsbiology.organism_classificationKetoconazoleCarbohydrate SequenceComplementary and alternative medicinechemistrySmilaxMolecular MedicineSteroidsPlanta Medica
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Secretion and antigenicity of hepatitis B virus small envelope proteins lacking cysteines in the major antigenic region.

1995

Abstract Disulfide bonds are of crucial importance for the structure and antigenic properties of the hepatitis B virus (HBV) envelope. We have evaluated the role of the eight highly conserved cysteines of the major antigenic region for assembly, secretion, and antigenicity of the envelope proteins. Mutants carrying single or multiple substitutions of alanine for cysteine were analyzed using epitope tagging and transient expression in COS-7 cells. The only single cysteines found to be indispensable for efficient secretion were Cys-107 and Cys-138, but double mutation of Cys-137 and Cys-139 also created a block to secretion. Poorly secreted mutants formed aberrant oligomeric structures. The a…

AntigenicityHepatitis B virusGlycosylationmedicine.drug_classMutantMolecular Sequence DataBiologymedicine.disease_causeMonoclonal antibodyEpitopeCell LineViral Envelope ProteinsVirologymedicineAnimalsSecretionCysteineDisulfidesHepatitis B virusAlanineImmunoassayHepatitis B Surface AntigensBase SequenceAntibodies MonoclonalOligonucleotides AntisenseHepatitis BMolecular biologyBiochemistryMutagenesis Site-DirectedCysteineVirology
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Specific bovine antibody response against a new recombinant Cryptosporidium parvum antigen containing 4 zinc-finger motifs

2002

A Cryptosporidium parvum sporozoite and oocyst lambda gt11 cDNA library was screened with a hyperimmune rabbit serum that was developed against insoluble fragments of ultrasonicated oocysts. A clone named Cp22.4.1 encoding a protein of 231 amino acids with 4 zinc-finger domains characterized by a Cys-X2-Cys-X4-His-X4-Cys motif was isolated and characterized. There was a complete match between the sequencing data of the coding region of Cp22.4.1 and the corresponding gene at chromosomal level. Cloning in a pBAD-TOPO-TA expression vector permitted to evaluate the antigenicity of the recombinant His-tagged antigen. This antigen was recognized by 2 out of 5 sera from Cryptosporidium immune calv…

Antigenicityanimal diseasesMolecular Sequence DataProtozoan ProteinsAntibodies ProtozoanAntigens ProtozoanMolecular cloningBrief Communicationlaw.inventionAntigenlawparasitic diseasesAnimalsAmino Acid SequenceZinc fingerCryptosporidium parvumExpression vectorbiologyBase SequencecDNA libraryZinc Fingersbiology.organism_classificationVirologyRecombinant ProteinsInfectious DiseasesCryptosporidium parvumRecombinant DNAParasitologyCattleRabbits
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The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen.

1997

A lambda gt11 cDNA library from Candida albicans ATCC 26555 was screened by using pooled sera from two patients with systemic candidiasis and five neutropenic patients with high levels of anti-C. albicans immunoglobulin M antibodies. Seven clones were isolated from 60,000 recombinant phages. The most reactive one contained a 0.9-kb cDNA encoding a polypeptide immunoreactive only with sera from patients with systemic candidiasis. The whole gene was isolated from a genomic library by using the cDNA as a probe. The nucleotide sequence of the coding region showed homology (78 to 79%) to the Saccharomyces cerevisiae TDH1 to TDH3 genes coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH), …

Antigens FungalDNA ComplementaryGenes FungalMolecular Sequence DataBiologyMicrobiologystomatognathic systemCell WallComplementary DNACandida albicansmedicineHumansCloning MolecularCandida albicansFluorescent Antibody Technique IndirectMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseAntibodies FungalAntiserumcDNA libraryCandidiasisAntibodies MonoclonalGlyceraldehyde-3-Phosphate Dehydrogenasesmedicine.diseasebiology.organism_classificationMolecular biologyCorpus albicansBlotting SouthernBiochemistryPolyclonal antibodiesAntigens Surfacebiology.proteinSystemic candidiasisGlycolysisResearch Article
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Cloning and characterization of PRA1, a gene encoding a novel pH-regulated antigen of Candida albicans.

1998

ABSTRACT Candida albicans is an opportunistic fungal pathogen of humans. The cell wall of the organism defines the interface between the pathogen and host tissues and is likely to play an essential and pivotal role in the host-pathogen interaction. The components of the cell wall critical to this interaction are undefined. Immunoscreening of a lambda expression library with sera raised against mycelial cell walls of C. albicans was used to identify genes encoding cell surface proteins. One of the positive clones represented a candidal gene that was differentially expressed in response to changes in the pH of the culture medium. Maximal expression occurred at neutral pH, with no expression d…

Antigens FungalDNA ComplementaryMolecular Sequence DataReceptors Cell SurfaceMicrobiologyFungal ProteinsImmunoscreeningGene Expression Regulation FungalCandida albicansAmino Acid SequenceCloning MolecularCandida albicansMolecular BiologyGenePeptide sequencechemistry.chemical_classificationFungal proteinbiologyBase SequenceSequence Homology Amino AcidHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyCorpus albicansPhenotypeEukaryotic CellschemistryCell fractionationGlycoproteinJournal of bacteriology
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Identification of a mannoprotein present in the inner layer of the cell wall of Saccharomyces cerevisiae.

1997

Cell wall extracts from the double-mutant mnn1 mnn9 strain were used as the immunogen to obtain a monoclonal antibody (MAb), SAC A6, that recognizes a specific mannoprotein--which we have named Icwp--in the walls of cells of Saccharomyces cerevisiae. Icwp runs as a polydisperse band of over 180 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of Zymolyase extracts of cell walls, although an analysis of the secretory pattern of the mannoprotein shows that at the level of secretory vesicles, it behaves like a discrete band of 140 kDa. Immunofluorescence analysis with the MAb showed that Icwp lies at the inner layer of the cell wall, being accessible to the antibody on…

Antigens FungalDNA ComplementarySaccharomyces cerevisiae ProteinsGlycosylphosphatidylinositolsSaccharomyces cerevisiaeGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeCalcofluor-whiteBiologyMicrobiologySerineCell wallFungal Proteinschemistry.chemical_compoundCell WallThreonineMolecular BiologyGel electrophoresisMembrane GlycoproteinsBase SequenceAntibodies MonoclonalTunicamycinbiology.organism_classificationMolecular biologycarbohydrates (lipids)Open reading frameMutagenesis InsertionalchemistryBiochemistryResearch Article
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Genetic polymorphisms affecting the phenotypic expression in familial hypercholesterolemia

2004

The clinical expression of heterozygous familial hypercholesterolemia (FH) is highly variable even in patients carrying the same LDL receptor (LDL-R) gene mutation. This variability might be due to environmental factors as well as to modifying genes affecting lipoprotein metabolism. We investigated Apo E (2, 3, 4), MTP (-493G/T), Apo B (-516C/T), Apo A-V (-1131T/C), HL (-514C/T and -250G/A), FABP-2 (A54T), LPL (D9N, N291S, S447X) and ABCA1 (R219K) polymorphisms in 221 unrelated FH index cases and 349 FH relatives with defined LDL-R gene mutations. We found a significant and independent effect of the following polymorphisms on: (i) plasma LDL-C (Apo E, MTP and Apo B); (ii) plasma HDL-C (HL, …

Apolipoprotein EMaleSettore MED/09 - Medicina InternaApolipoprotein BFamilial hypercholesterolemiaGene mutationPolymerase Chain ReactionCoronary artery diseasecoronary artery disease; familial hypercholesterolemia; genetic polymorphisms; plasma lipidsCohort Studieschemistry.chemical_compoundGenotypePlasma lipidsOdds RatiobiologyFamilial hypercholesterolemia Plasma lipids Genetic polymorphisms Coronary artery diseaseIncidenceMiddle AgedPhenotypelipids (amino acids peptides and proteins)FemaleCardiology and Cardiovascular MedicineAdultmedicine.medical_specialtyMolecular Sequence DataFamilial hypercholesterolemiaPlasma lipidGenetic polymorphismsRisk AssessmentHyperlipoproteinemia Type IIFamilial hypercholesterolemia; Plasma lipids; Genetic polymorphisms; Coronary artery diseasePredictive Value of TestsInternal medicinemedicineConfidence IntervalsHumansGenetic Predisposition to DiseaseGenetic polymorphismPolymorphism GeneticBase SequenceCholesterolCholesterol HDLCase-control studyCholesterol LDLmedicine.diseaseEndocrinologyApolipoproteinschemistrySettore MED/03 - Genetica MedicaGene Expression RegulationReceptors LDLCase-Control StudiesLDL receptorbiology.protein
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