0000000000336701

AUTHOR

Susanna Repo

showing 3 related works from this author

The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

2002

A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to which terminal or central parts of hevein were fused. Hevein and AMP share a structurally identical core region but have different N-terminal and C-terminal regions. Only 1 of 16 hevein-allergic patients showed weak IgE binding to purified native or recombinant AMP. Chimeric AMP with the hevein N terminus was recognized by IgE from 14 (88%) patients, and chimeric AMP with the hevein C terminus wa…

MaleModels MolecularProtein ConformationImmunoglobulin Emedicine.disease_causeBiochemistryEpitopelaw.inventionEpitopes0302 clinical medicineAllergenlawLectinsPlant Proteins0303 health sciencesbiologyMiddle Aged3. Good healthDatabases as TopicBiochemistryRecombinant DNAFemalePlant LectinsProtein BindingAdultPeptide BiosynthesisAdolescentRecombinant Fusion ProteinsEnzyme-Linked Immunosorbent Assay03 medical and health sciencesChimera (genetics)medicineAnimalsHumansMolecular BiologyAged030304 developmental biologyDose-Response Relationship DrugC-terminusCell BiologyAllergensImmunoglobulin EMolecular biologyAdenosine MonophosphateProtein Structure TertiaryN-terminusEpitope mappingSpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinChickensEpitope MappingAntimicrobial Cationic Peptides030215 immunologyJournal of Biological Chemistry
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Construction of hevein (Hev b 6.02) with reduced allergenicity for immunotherapy of latex allergy by comutation of six amino acid residues on the con…

2004

Abstract Recently we have established that IgE Abs bind to conformational epitopes in the N- and C-terminal regions of the major natural rubber latex allergen, hevein (Hev b 6.02). To identify the critical amino acid residues that interact with IgE, the hevein sequence was scanned by using site-specific mutations. Twenty-nine hevein mutants were designed and produced by a baculovirus expression system in insect cells and tested by IgE inhibition-ELISA using sera from 26 latex allergic patients. Six potential IgE-interacting residues of hevein (Arg5, Lys10, Glu29, Tyr30, His35, and Gln38) were identified and characterized further in detail. Based on these six residues, two triple mutants (HΔ…

MaleModels MolecularProtein ConformationMutantImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopes0302 clinical medicineProtein structureAllergenlawImmunology and AllergyCombinatorial Chemistry TechniquesChild0303 health sciencesbiologyChemistryMiddle AgedRecombinant Proteins3. Good healthBiochemistryLatex allergyRecombinant DNAFemalePlant LectinsProtein BindingAdultAdolescentImmunologyMutagenesis (molecular biology technique)Binding Competitive03 medical and health sciencesLatex HypersensitivitymedicineHumansPoint Mutation030304 developmental biologyAgedAllergensImmunoglobulin Emedicine.disease030228 respiratory systemAmino Acid SubstitutionDesensitization Immunologicbiology.proteinMutagenesis Site-DirectedBinding Sites AntibodyAntimicrobial Cationic PeptidesJournal of immunology (Baltimore, Md. : 1950)
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Binding Properties of HABA-Type Azo Derivatives to Avidin and Avidin-Related Protein 4

2006

Summary The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D -biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands β3 and β4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 A) X-ray stru…

Models MolecularMolecular modelOvalbuminProtein ConformationClinical BiochemistryCrystallography X-RayLigandsSensitivity and SpecificityBiochemistryAvian Proteinschemistry.chemical_compoundUltraviolet visible spectroscopyBiotinDrug DiscoveryAnimalsMolecular BiologyGlycoproteinschemistry.chemical_classificationPharmacologyAzo compoundBinding SitesbiologyCalorimetry Differential ScanningMolecular StructureStereoisomerismGeneral MedicineLigand (biochemistry)AvidinCombinatorial chemistryCHEMBIOchemistryBiochemistryBiotinylationbiology.proteinMolecular MedicineSpectrophotometry UltravioletGlycoproteinAzo CompoundsChickensAvidinChemistry & Biology
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