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Table of Contents
Vol. 138, No. 4, 2005
Issue release date: December 2005
Section title: Review
Int Arch Allergy Immunol 2005;138:337–346
(DOI:10.1159/000089188)

The Spectrum of Allergens in Ragweed and Mugwort Pollen

Wopfner N. · Gadermaier G. · Egger M. · Asero R. · Ebner C. · Jahn-Schmid B. · Ferreira F.
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

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Article / Publication Details

First-Page Preview
Abstract of Review

Received: 6/7/2005
Accepted: 9/20/2005
Published online: 11/18/2005

Number of Print Pages: 10
Number of Figures: 1
Number of Tables: 1

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA

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 β1,6-galactan core substituted by a variable number (5–28) of α-arabinofuranose residues forming branched side chains with 5-, 2,5-, 3,5-, and 2,3,5-substituted arabinoses, and (2) single and adjacent β-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.


Article / Publication Details

First-Page Preview
Abstract of Review

Received: 6/7/2005
Accepted: 9/20/2005
Published online: 11/18/2005

Number of Print Pages: 10
Number of Figures: 1
Number of Tables: 1

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA


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