Art v 1, the major mugwort pollen allergen, consists of two domains, a defensin-like and a proline-rich domain, which shows two different glycosylation patterns: an arabinogalactan residue and -arabinofuranoses linked to hydroxyproline. The aim of this work was to gain insights about the role of the different protein domains in allergenicity and the clinical relevance of the glycosylation of Art v 1. For examination of the influence of glycans on IgG binding to Art v 1, immunoblot and inhibition ELISA were performed. First, the antibody recognition capacity to natural and recombinant Art v 1, as well as to the defensin-like and proline-rich domain expressed in E.coli and Pichia pastoris was analyzed, using a rabbit serum sensitized to natArt v 1. The second part of this study focused on the inhibition of glycan-specific antibodies with synthetic -arabinofuranoses linked to hydroxyprolines. IgG reactivity to natural Art v 1 could be inhibited up to 80% by adding 10 M natArt v 1 to the rabbit serum. The inhibition capacity of recArt v 1 amounted to only 20%. In comparison, antibody binding to recArt v 1 was totally abolished by natural and recombi-nant Art v 1 using the same concentrations as before. The recombinant defensin-like do-main showed results comparable to the full length recArt v 1. Polyclonal antibodies of rabbit serum possessed activity against the defensin-like domain, but no activity against the proline-rich domain, which indicated that all relevant peptide-based IgG epitopes of Art v 1 are located in the defensin-like domain. The proline-rich domain influences the antibody-reactivity only by virtue of post translational modifications. These results dem-onstrated that post translational modifications play a role in antibody-binding. The inhibition capacity of synthetic -Araf-Hyp could not be measured reproducibly. Thus, it is not possible to draw any firm conclusion on the extent of which these sugar residues influence the allergenic-response.