Search results for "Mannan"

showing 10 items of 50 documents

Preparation of Anti-protein and Anti-mannan Antisera against Fungal Cell Wall by Affinity Chromatography

1994

Abstract Iranzo, M., Marcilla, A., Elorza, M. V., Mormeneo, S., and Sentandreu, R. 1994. Preparation of anti-protein and anti-mannan antisera against fungal cell wall by affinity chromatography. Experimental Mycology 18, 159-167. A novel and easy chromatographic method has been developed for the isolation of anti-protein and anti-mannan antisera from a population of polyclonal antibodies obtained against Candida albicans and Yarrowia lipolytica cell wall mannoproteins. The technique is based on the immobilization of mannan (to be used as immunoadsorbent) by Affi-Prep H z resin after the oxidation of neighboring hydroxyl groups of the polysaccharide with sodium periodate. For Y. lipolytica p…

Antiserumeducation.field_of_studymedicine.diagnostic_testPopulationYarrowiaBiologyImmunofluorescencebiology.organism_classificationApplied Microbiology and Biotechnologycarbohydrates (lipids)Affinity chromatographyBiochemistryPolyclonal antibodiesmedicinebiology.proteinCandida albicanseducationMannanExperimental Mycology
researchProduct

HPMA-Based Nanocarriers for Effective Immune System Stimulation.

2019

The selective activation of the immune system using nanoparticles as a drug delivery system is a promising field in cancer therapy. Block copolymers from HPMA and laurylmethacrylate-co-hymecromone-methacrylate allow the preparation of multifunctionalized core-crosslinked micelles of variable size. To activate dendritic cells (DCs) as antigen presenting cells, the carbohydrates mannose and trimannose are introduced into the hydrophilic corona as DC targeting units. To activate DCs, a lipophilic adjuvant (L18-MDP) is incorporated into the core of the micelles. To elicit an immune response, a model antigen peptide (SIINFEKL) is attached to the polymeric nanoparticle-in addition-via a click rea…

AzidesPolymers and PlasticsOvalbuminPolymersMannoseBioengineering02 engineering and technology010402 general chemistry01 natural sciencesMicelleBiomaterialschemistry.chemical_compoundDrug Delivery SystemsAntigenAdjuvants ImmunologicMaterials ChemistryHumansParticle SizeAntigen-presenting cellMicellesMannanChemistryDendritic Cells021001 nanoscience & nanotechnologyPeptide Fragments0104 chemical sciencesImmune SystemDrug deliveryBiophysicsMethacrylatesNanoparticlesClick ChemistryNanocarriers0210 nano-technologyHydrophobic and Hydrophilic InteractionsMannose receptorBiotechnologyMacromolecular bioscience
researchProduct

Influence of pro- and prebiotics on gastric, duodenal and colonic bioaccessibility of the mycotoxin beauvericin

2013

Abstract Beauvericin (BEA) is a bioactive compound produced by the secondary metabolism of several Fusarium strains and known to have various biological activities. This study investigates the influence of several dietary fibers (galactomanan, glucomannan, citrus fiber, bamboo fiber, carrot fiber, pie fiber, β-glucan, xilan, and cellulose) and probiotic strains ( Lactobacillus animalis , Lb. casei , Lb. casei , Lb. plantarum , Lb. rhuminis , Lb. casei casei , Bifidobacterium breve , Bf. Adolescents , Bf. bifidum , Corynebacterium vitaeruminis , Streptococcus faecalis , Eubacterium crispatus , and Saccharomyces cerevisiae ) on the minor Fusarium mycotoxin BEA bioaccessibility employing a mod…

Bifidobacterium brevebiologyved/biologyPrebioticmedicine.medical_treatmentved/biology.organism_classification_rank.speciesfood and beveragesGlucomannanbiology.organism_classificationBeauvericinBioactive compoundlaw.inventionMicrobiologyProbioticchemistry.chemical_compoundchemistrylawmedicineEubacteriumFood scienceMycotoxinFood ScienceJournal of Food Composition and Analysis
researchProduct

Inhibition of human immunodeficiency virus-1 infection by human conglutinin-like protein: in vitro studies.

1992

The lectin-like protein analogous to bovine conglutinin was purified from human serum. The carbohydrate-binding ability of conglutinin-like protein was inhibited by D-mannose, N-acetylglucosamine and L-fucose as well as by mannan-containing oligosaccharides. By applying a lectin-based ELISA system it was demonstrated that conglutinin-like protein binds to human immunodeficiency virus-1 (HIV-1) glycoprotein 120 (gp120) via its carbohydrate binding site. In vitro experiments with T-lymphoblastoid CEM cells revealed that conglutinin-like protein abolishes infection by HIV-1; a 50% cytoprotective concentration of 23.9 micrograms/ml was measured. These findings demonstrate that human conglutinin…

Cancer ResearchMolecular Sequence DataCarbohydratesImmunoglobulinsEnzyme-Linked Immunosorbent AssayHIV Envelope Protein gp120Mannose-Binding LectinVirusChromatography AffinityArticleViral ProteinsConglutininProtein A/GHumansImmunoconglutininsBinding siteKey wordsConglutinin‐like proteinchemistry.chemical_classificationAcquired Immunodeficiency SyndromebiologyHIV‐1Immunization PassiveLectinMolecular biologyMannanIn vitrogp120OncologychemistryCarbohydrate Sequencebiology.proteinHIV-1Protein GGlycoproteinCarrier ProteinsLectinJapanese journal of cancer research : Gann
researchProduct

Binding and activation of human and mouse complement by Cryptosporidium parvum (Apicomplexa) and susceptibility of C1q- and MBL-deficient mice to inf…

2008

Cryptosporidium parvum is a protozoan parasite (Apicomplexa) that causes gastrointestinal disease in animals and humans. Whereas immunocompetent hosts can limit the infection within 1 or 2 weeks, immunocompromised individuals develop a chronic, life-threatening disease. The importance of the adaptive cellular immune response, with CD4+ T-lymphocytes being the major players, has been clearly demonstrated. Several non-adaptive immune mechanisms have been suggested to contribute to the host defence, such as interferon-gamma (IFN-gamma) from NK cells, certain chemokines, beta-defensins and pro-inflammatory cytokines, but the influence of the complement systems has been less well studied. We ana…

ChemokineImmunologyProtozoan ProteinsCryptosporidiosisComplement factor ISodium ChlorideMannose-Binding LectinMicrobiologyMiceImmune systemmedicineAnimalsHumansRNA MessengerMolecular BiologyComplement ActivationImmunodeficiencyMannan-binding lectinCryptosporidium parvumbiologyReverse Transcriptase Polymerase Chain ReactionComplement C1qOocystsTemperaturemedicine.diseasebiology.organism_classificationVirologyComplement systemMice Inbred C57BLCryptosporidium parvumGene Expression RegulationLectin pathwayComplement C3bbiology.proteinCattleDisease SusceptibilityMolecular immunology
researchProduct

The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, …

2001

The proteases of the lectin pathway of complement activation, MASP-1 and MASP-2, are encoded by two separate genes. The MASP1 gene is located on chromosome 3q27, the MASP2 gene on chromosome 1p36.23-31. The genes for the classical complement activation pathway proteases, C1r and C1s, are linked on chromosome 12p13. We have shown that the MASP2 gene encodes two gene products, the 76 kDa MASP-2 serine protease and a plasma protein of 19 kDa, termed MAp19 or sMAP. Both gene products are components of the lectin pathway activation complex. We present the complete primary structure of the human MASP2 gene and the tight cluster that this locus forms with non-complement genes. A comparison of the …

Chromosomes Artificial BacterialTranscription GeneticGenetic LinkageRNA SplicingImmunologyMolecular Sequence DataBiologyGeneticsHumansPromoter Regions GeneticComplement ActivationGenetics (clinical)Mannan-binding lectinGeneticsComplement component 2Base SequenceCD69Serine EndopeptidasesC4AChromosome MappingCollectinsKLRB1Chromosomes Human Pair 1Lectin pathwayMannose-Binding Protein-Associated Serine ProteasesMultigene Familybiology.proteinCarrier ProteinsMASP2MASP1
researchProduct

Identification of Leguminosae gums and evaluation of carob-guar mixtures by capillary zone electrophoresis of protein extracts.

2002

A procedure for the extraction and capillary zone electrophoresis (CZE) separation of proteins from carob, guar and tara gums in a background electrolyte (BGE) of pH 9 containing 0.1% polyvinyl alcohol is described. The CZE protein profiles exhibit characteristic peaks for each one of the Leguminosae gums, which can be used to construct models capable of identifying samples of carob, guar and tara gums, and predicting the guar content in binary carob-guar mixtures of different geographical origin and harvested in different years. The classification and prediction models are constructed by using linear discriminant analysis (LDA) and multiple linear regression (MLR), respectively. An excelle…

Detection limitChromatographyGuar gumResolution (mass spectrometry)ChemistryPlant ExtractsClinical BiochemistryExtraction (chemistry)GuarElectrophoresis CapillaryFabaceaeBiochemistryGalactansAnalytical ChemistryMannansCapillary electrophoresisModels ChemicalPolysaccharidesLinear regressionCalibrationPlant GumsElectrophoresis
researchProduct

Isolation and characterization of anavirulent Candida albicansyeast monomorphic mutant

2003

Mutagenesis of Candida albicans strain ATCC 26555 with N-methyl-nitro-N-nitrosoguanidine followed by plating on solid yeast nitrogen base-N-acetylglucosamine medium at 37 degrees C yielded colony morphology variants that were characterized as forming smooth colonies, in contrast to the rough colonies formed by the parental strain. One yeast monomorphic mutant, CAL4, was studied in detail. Strain CAL4 is defective in filamentous growth, unable to form hyphae or pseudohyphae in vivo and in vitro. These filamentous structures are not elicited by commonly used external stimuli such as serum. The mutant had no obvious alterations in its mannan, glucan or chitin content. The total quantity of non…

ElectrophoresisMaleVirulenceHyphaStrain (chemistry)biologyMutantCandidiasisMutagenesis (molecular biology technique)General Medicinebiology.organism_classificationYeastMicrobiologyFungal ProteinsCell wallMiceInfectious DiseasesCell WallCandida albicansMutationAnimalsCandida albicansMannanMedical Mycology
researchProduct

Complement component C1 and the collectins – first-line defense molecules in innate and acquired immunity

2002

Abstract The 5th International Workshop on C1 and the Collectins was held in Lufthansa-Bildungszentrum, Seeheim, Germany from 26–28 October 2001.

First lineImmunologyImmunologyImmunology and AllergyCollectinCancer biologyBiologyAcquired immune systemFicolinMannan-binding lectinMicrobiologyComplement (complexity)Trends in Immunology
researchProduct

Structural and functional diversity of the lectin repertoire in teleost fish: Relevance to innate and adaptive immunity

2011

Protein–carbohydrate interactions mediated by lectins have been recognized as key components of innate immunity in vertebrates and invertebrates, not only for recognition of potential pathogens, but also for participating in downstream effector functions, such as their agglutination, immobilization, and complement-mediated opsonization and killing. More recently, lectins have been identified as critical regulators of mammalian adaptive immune responses. Fish are endowed with virtually all components of the mammalian adaptive immunity, and are equipped with a complex lectin repertoire. In this review, we discuss evidence suggesting that: (a) lectin repertoires in teleost fish are highly dive…

Fish ProteinsModels MolecularImmunologySettore BIO/05 - ZoologiaBiologyAdaptive ImmunityArticleImmune systemPhagocytosisC-type lectinAntifreeze ProteinsLectinsAnimalsLectins Innate immunity Fish Self/non-self recognition Effector Regulatory functions Complement activationProtein Structure QuaternaryAntigens ViralComplement ActivationMannan-binding lectinAntigens BacterialInnate immune systemBacteriaEffectorFishesLectinComplement System ProteinsOpsonin ProteinsAcquired immune systemInvertebratesImmunity InnateComplement systemCell biologyProtein Structure TertiaryGene Expression RegulationOrgan SpecificityVertebratesVirusesbiology.proteinDevelopmental Biology
researchProduct