Search results for "Peptide Biosynthesis"

showing 2 items of 2 documents

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

Characterization of antigenic epitopes of potato virus Y.

1993

Immunochemical analysis of overlapping synthetic hexapeptides covering the entire length of the coat protein of potato virus Y (PVY) revealed immunodominant regions both at the N-terminal and at the C-terminal end of the coat protein. Immunization of rabbits with synthetic peptides representing N- and C-terminal regions of the coat protein resulted in production of antibodies that reacted with PVY. Antigenicity of PVY peptides was found to correlate with predicted beta turns, with hydrophilicity and with predicted chain flexibility. Characterization of the immunochemical properties of PVY will facilitate the development of detection methods for potyviruses.

Peptide BiosynthesisAntigenicity030303 biophysicsMolecular Sequence DataBiophysicsAntibodies ViralBiochemistryEpitopeVirusProtein Structure SecondaryPlant Viruses03 medical and health sciencesEpitopesCapsidAntigenStructural BiologyAnimalsAmino Acid SequenceMolecular BiologyProtein secondary structure030304 developmental biologyAntiserum0303 health sciencesbiologyPotyvirusbiology.organism_classificationVirologyMolecular biology3. Good healthPotato virus YRabbitsPeptidesBiochimica et biophysica acta
researchProduct