Search results for "Peptide sequence"

showing 10 items of 330 documents

Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein

2003

After screening of aCandida albicansgenome database, the product of an ORF (IPF 3054) that has 62 % homology withSaccharomyces cerevisiaeSsr1p, an internal cell-wall protein, was identified and named CaSsr1p. The deduced amino acid sequence shows that CaSsr1p contains an N-terminal hydrophobic signal peptide, is rich in Ser and Thr amino acids and has a potential glycosylphosphatidylinositol-attachment signal. CaSsr1p is released following degradation of isolated cell walls by zymolyase (mainly a 1,3-β-glucanase) and therefore seems to be covalently linked to theβ-glucan of the cell walls. Both disruption and overexpression of theCaSSR1gene caused an increased sensitivity to calcofluor whit…

Signal peptideSaccharomyces cerevisiae ProteinsMolecular Sequence DataSaccharomyces cerevisiaeGene ExpressionSaccharomyces cerevisiaeCalcofluor-whiteMicrobiologyFungal ProteinsCell wallSpecies SpecificityCell WallCandida albicansAmino Acid SequenceCloning MolecularDNA FungalCandida albicansGenePeptide sequencechemistry.chemical_classificationBase SequenceSequence Homology Amino Acidbiologybiology.organism_classificationAmino acidBiochemistrychemistryGene DeletionMicrobiology
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F17-like fimbriae from an invasive Escherichia coli strain producing cytotoxic necrotizing factor type 2 toxin

1994

The F17b fimbriae encoded by the transmissible virulence plasmid Vir, also coding for cytotoxic necrotizing factor type 2, were characterized. A 5.7-kb region of Vir mediates in vitro N-acetylglucosamine-sensitive adhesion to calf intestinal villi. Sequence analysis revealed that this region codes for a structural subunit and an adhesin closely related to the F17-A and F17-G proteins encoded by the F17 fimbrial gene cluster. The F17b-A gene presents an open reading frame of 540 bp encoding a polypeptide of 180 amino acids with a putative signal peptide of 21 residues. The mature protein shows an identity of 74% with the F17-A structural subunit. This 20-kDa protein is recognized by antiseru…

Signal peptideVirulence Factors[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataImmunologyFimbriaMutantBiologymedicine.disease_causeMicrobiologyMicrobiologyBacterial ProteinsGene clusterEscherichia colimedicineAmino Acid SequenceEscherichia coliPeptide sequenceAdhesins Escherichia coliAntigens BacterialBase SequenceCytotoxinsEscherichia coli ProteinsSEQUENCE NULECOTIDIQUEbiochemical phenomena metabolism and nutritionMolecular biology[SDV] Life Sciences [q-bio]Bacterial adhesinOpen reading frameInfectious DiseasesFimbriae BacterialCLONAGE DE GENEParasitologyResearch ArticleBacterial Outer Membrane ProteinsPlasmidsInfection and Immunity
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2-D differential membrane proteome analysis of scarce protein samples

2006

Proteome studies with small sample amounts are difficult to perform, especially when membrane proteins are the focus of interest. In our study a new method for the analysis of scarce membrane protein samples combining large gel 2-D-CTAB/SDS-PAGE with fluorescence dye saturation labelling (satDIGE) was developed, allowing a highly sensitive differential analysis of different cell states. After Triton X-114 phase partitioning, enriched membrane protein samples of T cells were labelled at cysteine residues using fluorescence dyes and separated by large gel 2D-CTAB/SDS-PAGE. For a differential analysis 3 mug protein was found to be sufficient to detect proteins in a widespread well-separated di…

Spectrometry Mass Electrospray IonizationChromatographyProteomeMolecular Sequence DataCellMembrane ProteinsBiologyProteomicsBiochemistryFluorescenceMicemedicine.anatomical_structureMembrane proteinLabellingProteomemedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceMolecular BiologyPeptide sequenceCells CulturedFluorescent DyesCysteinePROTEOMICS
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The silicatein propeptide acts as inhibitor/modulator of self-organization during spicule axial filament formation.

2013

Silicateins are crucial enzymes that are involved in formation of the inorganic biosilica scaffold of the spicular skeleton of siliceous sponges. We show that silicatein acquires its structure-guiding and enzymatically active state by processing of silicatein from pro-silicatein to the mature enzyme. A recombinant propeptide (PROP) of silicatein from the siliceous demosponge Suberites domuncula was prepared, and antibodies were raised against the peptide. In sponge tissue, these antibodies reacted with both surface structures and the central region of the spicules. Using phage display expression, spicule-binding 12-mer peptides were identified that are rich in histidine residues. In the pre…

SpiculeProtein ConformationMolecular Sequence Data02 engineering and technologyArginineBiochemistry03 medical and health sciencesProtein structurePeptide LibraryAnimalsUreaHistidineAmino Acid SequenceProtein PrecursorsProtein precursorMolecular BiologyPeptide sequenceHistidine030304 developmental biology0303 health sciencesbiologyLysineCell Biology021001 nanoscience & nanotechnologybiology.organism_classificationCathepsinsProtein tertiary structureRecombinant ProteinsSuberites domunculaBiochemistry0210 nano-technologyPeptidesSuberitesSuberitesThe FEBS journal
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Identification of N- and C-terminal Amino Acids of Lhca1 and Lhca4 Required for Formation of the Heterodimeric Peripheral Photosystem I Antenna LHCI-…

2002

Apoproteins of higher plant light-harvesting complexes (LHC) share considerable amino acid sequence identity/similarity. Despite this fact, they occur in different oligomeric states (i.e., monomeric, dimeric, and trimeric). As a step toward understanding the underlying structure requirements for different oligomerization behavior, we analyzed whether amino acids at the N- and C-termini of Lhca1 and Lhca4 are involved in the formation of the heterodimeric LHCI-730. Using altered proteins produced by deletion or site-directed mutagenesis for reconstitution, we were able to identify amino acids required for the assembly of LHCI-730. At the N-terminus of Lhca1, W4 is involved in heterodimerizat…

StereochemistryDimerPhotosynthetic Reaction Center Complex ProteinsMutantLight-Harvesting Protein ComplexesBiologyPhotosystem IBiochemistrychemistry.chemical_compoundResidue (chemistry)Point MutationAmino AcidsPeptide sequencePlant ProteinsSequence Deletionchemistry.chemical_classificationPhotosystem I Protein ComplexArabidopsis ProteinsMutagenesisRecombinant ProteinsAmino acidMonomerBiochemistrychemistryChlorophyll Binding ProteinsDimerizationBiochemistry
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Mutations affecting MHC class II binding of the superantigen streptococcal erythrogenic toxin A.

1993

Streptococcal pyrogenic exotoxin A (SPEA) is an important pathogenicity factor of group A streptococci. It is a member of the family of 'superantigens' produced by Staphylococcus aureus and Streptococcus pyogenes, and its T lymphocyte stimulating activity is involved in the pathogenesis of certain diseases caused by pyogenic streptococci. In this study we have generated nine mutant SPEA molecules by substituting amino acids in the regions of homology between different streptococcal and staphylococcal superantigens. An additional mutant was created by deletion of the 10 N-terminal amino acids. The mutants were expressed as fusion proteins. Several mutations led to a loss of function due to a…

Streptococcus pyogenesT-LymphocytesImmunologyMutantMolecular Sequence DataExotoxinsBiologymedicine.disease_causeLymphocyte ActivationMicrobiologyMiceStructure-Activity Relationshipstomatognathic systemBacterial ProteinsSuperantigenmedicineImmunology and AllergyAnimalsHumansAmino Acid SequencePeptide sequencechemistry.chemical_classificationMice Inbred BALB CSuperantigensBase SequenceHistocompatibility Antigens Class IIMembrane ProteinsGeneral Medicinebiology.organism_classificationFusion proteinAmino acidchemistrySpeaStreptococcus pyogenesMutationExotoxinInternational immunology
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Determinants essential for the transmissible gastroenteritis virus-receptor interaction reside within a domain of aminopeptidase-N that is distinct f…

1994

The swine-specific coronavirus transmissible gastroenteritis virus (TGEV) uses pig aminopeptidase-N (pAPN) as a cellular receptor. We showed that the human aminopeptidase-N (hAPN) cannot substitute for pAPN in this respect, although the two enzymes have 80% amino acid sequence identity. In order to map the TGEV binding site on pAPN, we constructed a series of APN cDNA chimeras between pAPN and hAPN and analyzed them for their capacity to confer infectivity. The region between residues 717 and 813 was found to be essential for infectivity. This region also contains the epitopes for three TGEV-blocking monoclonal antibodies directed against pAPN. These data support the view that the catalytic…

SwineImmunologyMolecular Sequence DataBiologyCD13 Antigensmedicine.disease_causeVirus ReplicationMicrobiologyAminopeptidaseAminopeptidasesEpitopeVirusCatalysis03 medical and health sciencesSpecies SpecificityVirologymedicineVIRUS DE LA GASTROENTERITE TRANSMISSIBLEAnimalsHumansAmino Acid SequenceBinding siteCloning MolecularPeptide sequenceComputingMilieux_MISCELLANEOUS030304 developmental biologyCoronavirusInfectivity[SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology0303 health sciencesBinding SitesBase Sequence030302 biochemistry & molecular biologyTransmissible gastroenteritis virusVirology3. Good healthViral replicationMutagenesisInsect ScienceDNA Viral[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyReceptors VirusResearch Article
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Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B

1995

Strain 1470 is the standard typing strain for serogroup F of Clostridium difficile containing both toxin genes, toxA-1470 and toxB-1470. A polymerase chain reaction (PCR)-based approach to the sequencing of the total toxB-1470 gene identified an open reading frame (ORF) of 7104 nucleotides. In comparison with the previously sequenced toxB of C. difficile VP10463, the toxB-1470 gene has 16 additional nucleotides, 13 within the 5'-untranslated region and three within the coding region. The M(r) of ToxB-1470 is 269,262, with an isoelectric point (IP) of 4.16. The equivalent values for ToxB are M(r) 269,709 and IP 4.13. In comparison with ToxB, ToxB-1470 differs primarily in the N-terminal regi…

SwineSequence analysisBacterial ToxinsMolecular Sequence DataRestriction MappingClostridium sordelliiMicrobiologyCell LineMicrobiologyOpen Reading FramesBacterial ProteinsAnimalsCoding regionAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceGeneClostridiumBase SequencebiologyClostridioides difficileCytotoxinsSequence Analysis DNAClostridium difficileClostridium novyibiology.organism_classificationActinsOpen reading frameGenes BacterialEndothelium VascularMolecular Microbiology
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Molecular study of porcine transmissible gastroenteritis virus after serial animal passages revealed point mutations in S protein

2010

Porcine respiratory coronavirus is related genetically to porcine transmissible gastroenteritis virus with a large deletion in S protein. The respiratory virus is a mutated form that may be a consequence of the gastroen- teritis virus's evolution. Intensive passages of the virus in its natural host may enhance the appearance of mutations and therefore may contribute to any attenuated form of the virus. The objective of this study was to characterize the porcine transmissible gastroenteritis virus TMK22 strain after passages in piglets from 1992 until 2007. A typical experimental infection, molecular characterization, and serological analysis were also carried out to further char- acterize a…

SwineSequence analysisvirusesMolecular Sequence DataRT-PCRBiologymedicine.disease_causeArticleVirusViral Envelope ProteinsImmunityVirologyGeneticsmedicineAnimalsPoint MutationDNA sequencingAmino Acid SequenceExperimental infectionPorcine diseaseMolecular BiologyPeptide sequenceCells CulturedCoronavirusMembrane GlycoproteinsGastroenteritis Transmissible of SwineSequence Analysis RNAPoint mutationTransmissible gastroenteritis virusGeneral MedicineVirologyGastroenteritisSpike Glycoprotein CoronavirusRNA ViralRespiratory virusPorcine Respiratory CoronavirusVirus Genes
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Agouti-Related Proteins (AGRPs) and Agouti-Signaling Peptide (ASIP) in Fish and Chicken

2005

We performed an intensive search on sequence databases to identify orthologues of ASIP and AGRP peptides in a number of different species, revealing a number of genomic fragments coding for the C-terminal part of agouti-related motifs, different from annotated peptide sequences, including one fragment from chicken, two from zebrafish, two from Fugu (Takifugu rubripes), and three from Tetraodon (Tetraodon nigroviridis). We have thus shown for the first time that both AGRP and ASIP genes exist in many species in "lower vertebrates" and were most probably present in early stages of vertebrate evolution.

Takifugu rubripesMolecular Sequence DataTetraodon nigroviridisGeneral Biochemistry Genetics and Molecular BiologySpecies SpecificityHistory and Philosophy of Sciencebiology.animalDatabases GeneticAnimalsAgouti-Related ProteinAmino Acid SequenceTetraodonGeneZebrafishPeptide sequencePhylogenyGeneticsbiologyFuguGeneral Neurosciencedigestive oral and skin physiologyFishesProteinsVertebratebiology.organism_classificationAgouti Signaling ProteinIntercellular Signaling Peptides and ProteinsChickensAnnals of the New York Academy of Sciences
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