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J. Biol. Chem., Vol. 280, Issue 9, 7932-7940, March 4, 2005

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Two Novel Types of O-Glycans on the Mugwort Pollen Allergen Art v 1 and Their Role in Antibody Binding^*

Renaud Leonard, Bent O. Petersen, Martin Himly¶, Waltraud Kaar, Nicole Wopfner¶, Daniel Kolarich, Ronald van Ree||, Christof Ebner**, Jens Ø. Duus, Fátima Ferreira¶, and Friedrich Altmann

From the Division of Biochemistry, Department of Chemistry, Universitaet fuer Bodenkultur Wien, Muthgasse 18, A-1190 Vienna, Austria, the Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Denmark, the ^¶Division of Allergy and Immunology, Department of Molecular Biology, University of Salzburg, Hellbrunnerstrasse 34, A-5020 Salzburg, Austria, the ^||Department of Immunopathology, Sanquin Research at CLB, Plesmanlaan 125, 1066 CX, Amsterdam, Netherlands, and the ^**Institute of Pathophysiology, Medical University of Vienna, Spitalgasse 23, A-1090 Wien, Austria

Art v 1, the major allergen of mugwort (Artemisia vulgaris) pollen contains galactose and arabinose. As the sera of some allergic patients react with natural but not with recombinant Art v 1 produced in bacteria, the glycosylation of Art v 1 may play a role in IgE binding and human allergic reactions. Chemical and enzymatic degradation, mass spectrometry, and 800 MHz ¹H and ¹³C nuclear magnetic resonance spectroscopy indicated the proline-rich domain to be glycosylated in two ways. We found a large hydroxyproline-linked arabinogalactan composed of a short 1,6-galactan core, which is substituted by a variable number (5–28) of -arabinofuranose residues, which form branched side chains with 5-, 2,5-, 3,5-, and 2,3,5-substituted arabinoses. Thus, the design of the Art v 1 polysaccharide differs from that of the well known type II arabinogalactans, and we suggest it be named type III arabinogalactan. The other type of glycosylation was formed by single (but adjacent) -arabinofuranoses linked to hydroxyproline. In contrast to the arabinosylation of Ser-Hyp₄ motifs in other hydroxyproline-rich glycoproteins, such as extensins or solanaceous lectins, no oligo-arabinosides were found in Art v 1. Art v 1 and parts thereof produced by alkaline degradation, chemical deglycosylation, proteolytic degradation, and/or digestion with -arabinofuranosidase were used in enzyme-linked immunosorbent assay and immunoblot experiments with rabbit serum and with the sera of patients. Although we could not observe antibody binding by the polysaccharide, the single hydroxyproline-linked -arabinose residues appeared to react with the antibodies. Mono--arabinosylated hydroxyproline residues thus constitute a new, potentially cross-reactive, carbohydrate determinant in plant proteins.

Received for publication, September 10, 2004 , and in revised form, November 19, 2004.

^* This work was supported by the Joint Research Project S88-MED (S8802, S8803, S8808) of the Austrian Science Fund. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Chemistry, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Wien, Austria. Tel.: 43-1-36006-6062; Fax: 43-1-36006-6059; E-mail: friedrich.altmann{at}boku.ac.at.

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				B. Jahn-Schmid, P. Sirven, V. Leb, W. F. Pickl, G. F. Fischer, G. Gadermaier, M. Egger, C. Ebner, F. Ferreira, B. Maillere, et al. Characterization of HLA Class II/Peptide-TCR Interactions of the Immunodominant T Cell Epitope in Art v 1, the Major Mugwort Pollen Allergen J. Immunol., September 1, 2008; 181(5): 3636 - 3642. [Abstract] [Full Text] [PDF]