Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin‐like and a hydroxyproline‐rich domain

• DOI: 10.1096/fj.02-0472fje
• Publication Date: 2003-01-14T00:44:17Z
• Authors: Martin Himly; Beatrice Jahn‐Schmid; Azra Dedic; Peter Kelemen; Nicole Wopfner; Friedrich Altmann; Ronald Ree; Peter Briza; Klaus Richter; Christof Ebner; Fátima Ferreira
• Keywords: Mugwort

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 cDNA clone coding for Art v 1, allergen mugwort pollen. Sequence analysis showed that 1 is secreted with an N-terminal cysteine-rich domain homologous to plant defensins and C-terminal proline-rich region containing several (Ser/Ala)(Pro)2-4 repeats. Structural some proline residues in posttranslationally modified by hydroxylation O-glycosylation. The O-glycans composed 3 galactoses 9-16 arabinoses linked hydroxyproline represent new type O-glycan. A 3-D structural model was generated showing characteristic "head tail" structure. Evaluation antibody binding properties natural recombinant produced Escherichia coli revealed involvement defensin fold posttranslational modifications formation epitopes recognized IgE antibodies allergic patients. However, did not influence T-cell recognition. Thus, nonglycosylated good starting template engineering hypoallergenic vaccines weed-pollen therapy.