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The spectrum of allergens in ragweed and mugwort pollen.
Int Arch Allergy Immunol. 2005 Dec; 138(4):337-46.IA

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 beta1,6-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.

Authors+Show Affiliations

Department of Molecular Biology, Division of Allergy and Immunology, University of Salzburg, Salzburg, Austria.No 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
Review

Language

eng

PubMed ID

16254437

Citation

Wopfner, Nicole, et al. "The Spectrum of Allergens in Ragweed and Mugwort Pollen." International Archives of Allergy and Immunology, vol. 138, no. 4, 2005, pp. 337-46.
Wopfner N, Gadermaier G, Egger M, et al. The spectrum of allergens in ragweed and mugwort pollen. Int Arch Allergy Immunol. 2005;138(4):337-46.
Wopfner, N., Gadermaier, G., Egger, M., Asero, R., Ebner, C., Jahn-Schmid, B., & Ferreira, F. (2005). The spectrum of allergens in ragweed and mugwort pollen. International Archives of Allergy and Immunology, 138(4), 337-46.
Wopfner N, et al. The Spectrum of Allergens in Ragweed and Mugwort Pollen. Int Arch Allergy Immunol. 2005;138(4):337-46. PubMed PMID: 16254437.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The spectrum of allergens in ragweed and mugwort pollen. AU - Wopfner,Nicole, AU - Gadermaier,Gabriele, AU - Egger,Matthias, AU - Asero,Riccardo, AU - Ebner,Christof, AU - Jahn-Schmid,Beatrice, AU - Ferreira,Fatima, Y1 - 2005/10/24/ PY - 2005/10/29/pubmed PY - 2005/12/16/medline PY - 2005/10/29/entrez SP - 337 EP - 46 JF - International archives of allergy and immunology JO - Int. Arch. Allergy Immunol. VL - 138 IS - 4 N2 - 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 beta1,6-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. SN - 1018-2438 UR - https://www.unboundmedicine.com/medline/citation/16254437/The_spectrum_of_allergens_in_ragweed_and_mugwort_pollen_ L2 - https://www.karger.com?DOI=10.1159/000089188 DB - PRIME DP - Unbound Medicine ER -