Search results for "Peptide sequence"

showing 10 items of 330 documents

Identification of a peptide mimicking the binding pattern of an antiphospholipid antibody

2006

Our objective was to characterize monoclonal antiphospholipid antibodies (APL) and identify disease-associated antigens in patients with the antiphospholipid syndrome (APS). We used the monoclonal antibody HL-5B, derived from a patient with APS suffering from multiple ischemic events, to screen a 12-mer peptide phage display library (New England Biolabs, London, England). The identified phage clones were sequenced and the derived consensus peptide was synthesized. The peptide was used to perform competitive inhibition experiments for their ability to inhibit the binding of the monoclonal antibody and of serum antibodies to cardiolipin and phosphatidylserine. Additionally patients and contro…

AdultMalePhage displaymedicine.drug_classMolecular Sequence DataImmunologyEnzyme-Linked Immunosorbent AssayMonoclonal antibodyEpitopeAntigenAntibody SpecificityPeptide LibraryAntiphospholipid syndromemedicineHumansImmunology and AllergyAmino Acid SequencePeptide libraryPeptide sequenceAgedbiologyMolecular MimicryAntibodies MonoclonalHematologyMiddle AgedAntiphospholipid Syndromemedicine.diseaseVirologyMolecular biologyAntibodies Antiphospholipidbiology.proteinFemaleAntibodyPeptidesProtein BindingImmunobiology
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A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

2014

Abstract The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is p…

AgglutinationGram-negative bacteriaErythrocytesRhamnoselectin; D. labraxImmunologyAmino Acid MotifsMolecular Sequence DataRhamnoseArticlechemistry.chemical_compoundPlasmaPhagocytosisLectinsEscherichia coliAnimalsAmino Acid SequenceSea bassPeptide sequencePhylogenybiologyD. labraxLectinRhamnose bindingBacterial Infectionsbiology.organism_classificationImmunity InnateProtein Structure TertiaryBiochemistrychemistrybiology.proteinMacrophages PeritoneallectinBassRabbitsProtein MultimerizationSequence motifDevelopmental BiologyHomotetramerProtein Binding
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N-Terminal amino acid sequence analysis indicates that isolated atrial amyloid is derived from atrial natriuretic peptide

1988

Isolated atrial amyloid, the most frequent senile cardiac amyloid type, was chemically analysed. Amyloid fibrils obtained from a patient (NIP) were extracted and the predominant low-molecular-weight polypeptide (approximately 3.5 kDa, designated ASc2 NIP) was isolated by size exclusion high performance liquid chromatography in 60% formic acid. N-Terminal amino acid sequence analysis of this polypeptide was identical to that of the atrial natriuretic peptide alpha-hANP for the first 12 residues determined.

AmyloidAmyloidFormic acidMolecular Sequence DataSize-exclusion chromatographyIsolated atrial amyloidHigh-performance liquid chromatographyPathology and Forensic Medicinechemistry.chemical_compoundAtrial natriuretic peptidechemistryBiochemistrymental disordersHumansNIPFemaleAmino Acid SequencePeptide sequenceAtrial Natriuretic FactorAgedVirchows Archiv B Cell Pathology
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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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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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Molecular and Functional Characterisation of Hemocyanin of the Giant African Millipede Archispirostreptus gigas

2013

SummaryIn contrast to other terrestrial arthropods where gaseous O2 that fuels aerobic metabolism diffuses to the tissues in tracheal tubes, and most other metazoans where O2 is transported to tissues by circulating respiratory proteins, the myriapods (millipedes and centipedes) strikingly have tracheal systems as well as circulating hemocyanin (Hc). In order to elucidate the evolutionary origin and biological significance of millipede Hc we report the molecular structure (subunit composition and amino acid sequence) of multimeric (36-mer) Hc from the forest-floor dwelling giant African millipede Archispirostreptus gigas and its allosteric oxygen binding properties under various physico-che…

Archispirostreptus gigasGlycosylationPhysiologymedicine.medical_treatmentProtein subunitAllosteric regulationMolecular Sequence DataCoenzymesBohr effectCooperativityAquatic ScienceBiologyModels Biologicalchemistry.chemical_compoundAllosteric RegulationmedicineAnimalsBody SizeMolecular BiologyPeptide sequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenyHemocyaninBayes TheoremHydrogen-Ion Concentrationbiology.organism_classificationOxygenchemistryBiochemistryInsect ScienceAfricaHemocyaninsAnimal Science and ZoologyCalciumElectrophoresis Polyacrylamide GelProtein Binding
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Bacterial sensor kinases using Fe–S cluster binding PAS or GAF domains for O2sensing

2012

[4Fe-4S](2+) clusters are used by very diverse types of bacterial sensors for response to oxygen, including DNA-binding proteins of the CRP/FNR family and sensor kinases like NreB. In NreB the cluster is bound by an input domain of the PAS type. The [4Fe-4S](2+) cluster of NreB responds to O(2) by degradation to a [2Fe-2S](2+) cluster which is labile and decomposes. NreB constitutes together with AirS the NreB/AirS family of bacterial sensor kinases that contain PAS or GAF domains for binding of [4Fe-4S](2+) or [2Fe-2S](2+) clusters and oxygen sensing. The NreB/AirS family is related to the FixL sensor kinases that use hemeB binding PAS domains for oxygen sensing.

BacteriaKinaseStereochemistryChemistryIronOxygen metabolismMolecular Sequence DataPhosphotransferasesO2 sensingBioinformaticsProtein Structure TertiaryOxygenInorganic ChemistryProtein structureCluster (physics)Amino Acid SequencePeptide sequenceOxygen sensingSulfurDalton Trans.
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Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus…

1992

The homologous C-terminal repeats of Clostridium difficile toxins (ToxA and ToxB) and streptococcal glucosyltransferases appear to mediate protein-carbohydrate interactions at cellular binding sites with sugar moieties as substrates. A consensus sequence of 134 repeating units from gram-positive bacteria indicates that these repeats have a modular design with (i) a stretch of aromatic amino acids proposed to be involved in the primary carbohydrate-protein interaction, (ii) an amplification of this interaction by repetition of the respective sequences, and (iii) a second domain, not characterized, that is responsible for carbohydrate specificity.

Bacterial ToxinsMolecular Sequence DataEnterotoxinMicrobiologyMicrobiologyStreptococcus mutanschemistry.chemical_compoundEnterotoxinsGlucosyltransferasesBacterial ProteinsGlycosyltransferaseConsensus SequenceConsensus sequenceAromatic amino acidsAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceBinding SitesbiologySequence Homology Amino AcidClostridioides difficileCytotoxinsClostridium difficilechemistryBiochemistryGlucosyltransferasesbiology.proteinCarbohydrate MetabolismResearch ArticleJournal of bacteriology
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In vivo detection, RNA-binding properties and characterization of the RNA-binding domain of the p7 putative movement protein from carnation mottle ca…

1999

Biochemical and structural characterization studies on the p7 putative movement protein from a Spanish isolate of carnation mottle carmovirus (CarMV) have been conducted. The CarMV p7 gene was fused to a sequence coding for a six-histidine tag and expressed in bacteria, allowing the purification of CarMV p7 and the production of a specific antiserum. This antiserum led to the immunological identification of CarMV p7 in infected leaf tissue from the experimental host Chenopodium quinoa. Putative nucleic acid-binding properties of the CarMV p7 have been explored and demonstrated with both electrophoretic mobility shift and RNA-protein blot in vitro assays using digoxigenin-labeled riboprobes.…

Binding SitesCarmovirusRecombinant Fusion ProteinsMolecular Sequence DataCooperative bindingRNARNA-Binding ProteinsBiologybiology.organism_classificationMolecular biologyPlant Viral Movement ProteinsViral ProteinsBiochemistryVirologyNucleic acidEscherichia coliCarmovirusAmino Acid SequenceMovement proteinPeptide sequenceGeneBinding domainVirology
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Differential Proteomics Based on 2D-Difference In-Gel Electrophoresis and Tandem Mass Spectrometry for the Elucidation of Biological Processes in Ant…

2017

Proteomics based on 2D-Difference In Gel Electrophoresis (2D-DIGE) coupled with mass spectrometry (MS) procedures can be considered a “gold standard” to determine quantitatively and comparatively protein abundances in cell extracts from different biological sources/conditions according to a gel-based approach. In particular, 2D-DIGE is used for protein specie separation, detection, and relative quantification, whenever tandem MS is used to obtain peptide sequence information that is managed according to bioinformatic procedures to identify the differentially represented protein species. The proteomic results consist of a dynamic portray of over- and down-represented protein species that…

Bioinformatic0301 basic medicineGel electrophoresisfood.ingredientbiologyChemistryStreptomyces coelicolorComputational biologyRelative quantificationProteomicsbiology.organism_classificationTandem mass spectrometryPseudoalteromonas haloplanktis03 medical and health sciencesProtein separation030104 developmental biologyfoodMicrobisporaProtein purificationGenetics2D-DIGEProtein identificationMolecular BiologyPeptide sequenceNanoLC-ESI-LIT-MS/MS
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