Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin-like and a hydroxyproline-rich domain
| Autor: | Martin Himly, Azra Dedic, Nicole Wopfner, Ronald van Ree, Klaus Richter, B. Jahn-Schmid, Peter Kelemen, Friedrich Altmann, Christof Ebner, Peter Briza, Fatima Ferreira |
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| Přispěvatelé: | Experimental Immunology |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Sequence analysis T-Lymphocytes Molecular Sequence Data Biology medicine.disease_cause Biochemistry Epitope law.invention Cell Line Defensins Mugwort Allergen law Genetics medicine Escherichia coli Humans Amino Acid Sequence Molecular Biology Defensin Peptide sequence Cells Cultured Glycoproteins Plant Proteins chemistry.chemical_classification Rhinitis Allergic Seasonal food and beverages Allergens Antigens Plant Immunoglobulin E Models Theoretical Recombinant Proteins Protein Structure Tertiary Hydroxyproline chemistry Artemisia Recombinant DNA Pollen Glycoprotein Protein Processing Post-Translational Sequence Alignment Biotechnology |
| Zdroj: | Scopus-Elsevier ResearcherID FASEB journal, 17(1), 106-108. FASEB |
| ISSN: | 0892-6638 |
| DOI: | 10.1096/fj.02-0472fje |
| Popis: | In late summer, pollen grains originating from Compositae weeds (e.g., mugwort, ragweed) are a major source of allergens worldwide. Here, we report the isolation of a cDNA clone coding for Art v 1, the major allergen of mugwort pollen. Sequence analysis showed that Art v 1 is a secreted allergen with an N-terminal cysteine-rich domain homologous to plant defensins and a C-terminal proline-rich region containing several (Ser/Ala)(Pro)2-4 repeats. Structural analysis showed that some of the proline residues in the C-terminal domain of Art v 1 are posttranslationally modified by hydroxylation and O-glycosylation. The O-glycans are composed of 3 galactoses and 9-16 arabinoses linked to a hydroxyproline and represent a new type of plant O-glycan. A 3-D structural model of Art v 1 was generated showing a characteristic "head and tail" structure. Evaluation of the antibody binding properties of natural and recombinant Art v 1 produced in Escherichia coli revealed the involvement of the defensin fold and posttranslational modifications in the formation of epitopes recognized by IgE antibodies from allergic patients. However, posttranslational modifications did not influence T-cell recognition. Thus, recombinant nonglycosylated Art v 1 is a good starting template for engineering hypoallergenic vaccines for weed-pollen therapy. |
| Databáze: | OpenAIRE |
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