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Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding.
J Biol Chem. 2005 Mar 04; 280(9):7932-40.JB

Abstract

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 (1)H and (13)C 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 beta1,6-galactan core, which is substituted by a variable number (5-28) of alpha-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) beta-arabinofuranoses linked to hydroxyproline. In contrast to the arabinosylation of Ser-Hyp(4) 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 alpha-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 beta-arabinose residues appeared to react with the antibodies. Mono-beta-arabinosylated hydroxyproline residues thus constitute a new, potentially cross-reactive, carbohydrate determinant in plant proteins.

Authors+Show Affiliations

Division of Biochemistry, Department of Chemistry, Universitaet fuer Bodenkultur Wien, Muthgasse 18, A-1190 Vienna, Austria.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15591314

Citation

Leonard, Renaud, et al. "Two Novel Types of O-glycans On the Mugwort Pollen Allergen Art V 1 and Their Role in Antibody Binding." The Journal of Biological Chemistry, vol. 280, no. 9, 2005, pp. 7932-40.
Leonard R, Petersen BO, Himly M, et al. Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding. J Biol Chem. 2005;280(9):7932-40.
Leonard, R., Petersen, B. O., Himly, M., Kaar, W., Wopfner, N., Kolarich, D., van Ree, R., Ebner, C., Duus, J. Ø., Ferreira, F., & Altmann, F. (2005). Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding. The Journal of Biological Chemistry, 280(9), 7932-40.
Leonard R, et al. Two Novel Types of O-glycans On the Mugwort Pollen Allergen Art V 1 and Their Role in Antibody Binding. J Biol Chem. 2005 Mar 4;280(9):7932-40. PubMed PMID: 15591314.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding. AU - Leonard,Renaud, AU - Petersen,Bent O, AU - Himly,Martin, AU - Kaar,Waltraud, AU - Wopfner,Nicole, AU - Kolarich,Daniel, AU - van Ree,Ronald, AU - Ebner,Christof, AU - Duus,Jens Ø, AU - Ferreira,Fátima, AU - Altmann,Friedrich, Y1 - 2004/12/10/ PY - 2004/12/14/pubmed PY - 2005/4/9/medline PY - 2004/12/14/entrez SP - 7932 EP - 40 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 280 IS - 9 N2 - 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 (1)H and (13)C 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 beta1,6-galactan core, which is substituted by a variable number (5-28) of alpha-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) beta-arabinofuranoses linked to hydroxyproline. In contrast to the arabinosylation of Ser-Hyp(4) 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 alpha-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 beta-arabinose residues appeared to react with the antibodies. Mono-beta-arabinosylated hydroxyproline residues thus constitute a new, potentially cross-reactive, carbohydrate determinant in plant proteins. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/15591314/Two_novel_types_of_O_glycans_on_the_mugwort_pollen_allergen_Art_v_1_and_their_role_in_antibody_binding_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15591314 DB - PRIME DP - Unbound Medicine ER -