0000000000147178

AUTHOR

Kristiina Turjanmaa

showing 5 related works from this author

N-terminal hevein-like domains (4.3 kDa) but not 31 kDa endochitinases are responsible for IgE-mediated in vitro and in vivo reactions in latex-fruit…

2005

0303 health sciences03 medical and health sciences0302 clinical medicineIge mediated030228 respiratory systemBiochemistryChemistryIn vivoImmunologyImmunology and AllergyMolecular biologyIn vitro030304 developmental biologyJournal of Allergy and Clinical Immunology
researchProduct

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
researchProduct

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)
researchProduct

Isolated hevein-like domains, but not 31-kd endochitinases, are responsible for IgE-mediated in vitro and in vivo reactions in latex-fruit syndrome.

2005

Background Individuals with natural rubber latex allergy often have immediate reactions to plant-derived foods and fresh fruits, such as avocado and banana. IgE of these patients has been shown to bind endochitinases containing an N-terminal hevein-like domain (HLD). However, evidence on 31-kd endochitinase-induced reactions in vivo is lacking. Objective We sought to assess the clinical significance of 31-kd endochitinases and isolated HLDs in latex-fruit syndrome. Methods The 31-kd endochitinases and corresponding HLDs were purified or produced from avocado, banana, latex, and wheat germ. Skin prick test reactivities against purified proteins were examined in 15 patients with natural rubbe…

AdultMaleLatexImmunologyMolecular Sequence DataEnzyme-Linked Immunosorbent Assaymedicine.disease_causeImmunoglobulin ECross-reactivityMicrobiology03 medical and health sciences0302 clinical medicineFood allergyChitin bindingLatex HypersensitivitymedicineImmunology and AllergyHumansAmino Acid Sequence030304 developmental biologyDNA PrimersSkin Tests0303 health sciencesbiologySequence Homology Amino AcidChemistryPerseaChitinasesfood and beveragesMusaAllergensImmunoglobulin EMiddle Agedmedicine.diseaseIn vitroWheat germ agglutinin3. Good healthProtein Structure Tertiary030228 respiratory systemSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinFemaleAntibodyPlant LectinsAnaphylaxisFood HypersensitivityAntimicrobial Cationic PeptidesThe Journal of allergy and clinical immunology
researchProduct

Latex allergy: the sum quantity of four major allergens shows the allergenic potential of medical gloves

2007

Background:  Assessment of allergenic potential of medical devices made of natural rubber latex (NRL) requires the measurement of concentrations of specific allergenic proteins or polypeptides eluting from rubber. Methods:  Four NRL allergens (Hev b 1, 3, 5, and 6.02) were quantified in all medical glove brands marketed in Finland in 1999, 2001, and 2003 (n = 208) by a capture enzyme immunoassay. The results were compared with those obtained from previous nationwide market surveys, using a skin prick test-validated human IgE-based ELISA-inhibition method. Results:  A high overall correlation (r = 0.87, 95% CI 0.83–0.90) emerged between the sum values of the four allergens(μg/g glove) and Ig…

0303 health sciencesAllergyLatex Hypersensitivitymedicine.diagnostic_testbusiness.industryImmunologymedicine.disease_causemedicine.diseaserespiratory tract diseases03 medical and health sciences0302 clinical medicineAllergen030228 respiratory systemHuman igeLatex allergyNatural rubber latexImmunoassayImmunologymedicineImmunology and AllergyFood sciencebusiness030304 developmental biologyAllergy
researchProduct