The Spectrum of Allergens in Ragweed and Mugwort Pollen

Vol. 138, No. 4, 2005

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The Spectrum of Allergens in Ragweed and Mugwort Pollen
Nicole Wopfner^a, Gabriele Gadermaier^a, Matthias Egger^a, Riccardo Asero^d, Christof Ebner^b, Beatrice Jahn-Schmid^c, Fatima Ferreira^a

^aDepartment of Molecular Biology, Division of Allergy and Immunology, University of Salzburg, Salzburg, and
^bAllergieambulatorium and
^cDepartment of Pathophysiology, Medical University of Vienna, Vienna, Austria;
^dAmbulatorio di Allergologia, Clinica San Carlo, Paderno Dugnano, Italy

Address of Corresponding Author

Int Arch Allergy Immunol 2005;138:337-346 (DOI: 10.1159/000089188)

Key Words

Ragweed pollen
Mugwort pollen
Allergen
IgE
T cell
Cross-reactivity
Weed pollen allergens

Abstract

Ragweed and mugwort are important allergenic weeds belonging to the Asteraceae or Compositae plant family. Pollen of mugwort is one of the main causes of allergic reactions in late summer and autumn in Europe and affects about 10-14% of the patients suffering from pollinosis. Ragweed pollen represents the major source of allergenic protein in the United States, with a prevalence of about 50% in atopic individuals. In Europe, ragweed allergy is now rapidly increasing particularly in certain areas in France, Italy, Austria, Hungary, Croatia, and Bulgaria. Amb a 1 and Art v 1, the major allergens of ragweed and mugwort, respectively, are unrelated proteins. Amb a 1 is an acidic 38-kDa nonglycosylated protein. The natural protein undergoes proteolysis during purification and is cleaved into a 26-kDa alpha chain, which associates noncovalently with the beta chain of 12 kDa. The two-chain form seems to be immunologically indistinguishable from the full-length molecule. Art v 1 is a basic glycoprotein comprising two domains: an N-terminal cysteine-rich, defensin-like domain and a C-terminal proline/hydroxyproline-rich module. The proline/hydroxyproline-rich domain was recently shown to contain two types of glycosylation: (1) a large hydroxyproline-linked arabinogalactan composed of a short beta 1,6-galactan core substituted by a variable number (5-28) of alpha -arabinofuranose residues forming branched side chains with 5-, 2,5-, 3,5-, and 2,3,5-substituted arabinoses, and (2) single and adjacent beta -arabinofuranoses linked to hydroxyproline. As described for other pollen, ragweed and mugwort pollen also contain the pan-allergen profilin and calcium-binding proteins, which are responsible for extensive cross-reactivity among pollen-sensitized patients.

Author Contacts

Correspondence to: Dr. Fatima Ferreira
Department of Molecular Biology, University of Salzburg
Hellbrunnerstrasse 34
AT-5020 Salzburg (Austria)
Tel. +43 662 8044 5734, Fax +43 662 8044 183, E-Mail fatima.ferreira@sbg.ac.at

Article Information

Published online: October 24, 2005
Number of Print Pages : 10
Number of Figures : 1, Number of Tables : 1, Number of References : 71

Medline Abstract (ID 16254437)

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