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A new allergen from ragweed (Ambrosia artemisiifolia) with homology to art v 1 from mugwort.
J Biol Chem. 2010 Aug 27; 285(35):27192-200.JB

Abstract

Art v 1, the major pollen allergen of the composite plant mugwort (Artemisia vulgaris) has been identified recently as a thionin-like protein with a bulky arabinogalactan-protein moiety. A close relative of mugwort, ragweed (Ambrosia artemisiifolia) is an important allergen source in North America, and, since 1990, ragweed has become a growing health concern in Europe as well. Weed pollen-sensitized patients demonstrated IgE reactivity to a ragweed pollen protein of apparently 29-31 kDa. This reaction could be inhibited by the mugwort allergen Art v 1. The purified ragweed pollen protein consisted of a 57-amino acid-long defensin-like domain with high homology to Art v 1 and a C-terminal proline-rich domain. This part contained hydroxyproline-linked arabinogalactan chains with one galactose and 5 to 20 and more alpha-arabinofuranosyl residues with some beta-arabinoses in terminal positions as revealed by high field NMR. The ragweed protein contained only small amounts of the single hydroxyproline-linked beta-arabinosyl residues, which form an important IgE binding determinant in Art v 1. cDNA clones for this protein were obtained from ragweed flowers. Immunological characterization revealed that the recombinant ragweed protein reacted with >30% of the weed pollen allergic patients. Therefore, this protein from ragweed pollen constitutes a novel important ragweed allergen and has been designated Amb a 4.

Authors+Show Affiliations

Department of Chemistry, University of Natural Resources and Applied Life Sciences BOKU, 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 availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

20576600

Citation

Léonard, Renaud, et al. "A New Allergen From Ragweed (Ambrosia Artemisiifolia) With Homology to Art V 1 From Mugwort." The Journal of Biological Chemistry, vol. 285, no. 35, 2010, pp. 27192-200.
Léonard R, Wopfner N, Pabst M, et al. A new allergen from ragweed (Ambrosia artemisiifolia) with homology to art v 1 from mugwort. J Biol Chem. 2010;285(35):27192-200.
Léonard, R., Wopfner, N., Pabst, M., Stadlmann, J., Petersen, B. O., Duus, J. Ø., Himly, M., Radauer, C., Gadermaier, G., Razzazi-Fazeli, E., Ferreira, F., & Altmann, F. (2010). A new allergen from ragweed (Ambrosia artemisiifolia) with homology to art v 1 from mugwort. The Journal of Biological Chemistry, 285(35), 27192-200. https://doi.org/10.1074/jbc.M110.127118
Léonard R, et al. A New Allergen From Ragweed (Ambrosia Artemisiifolia) With Homology to Art V 1 From Mugwort. J Biol Chem. 2010 Aug 27;285(35):27192-200. PubMed PMID: 20576600.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A new allergen from ragweed (Ambrosia artemisiifolia) with homology to art v 1 from mugwort. AU - Léonard,Renaud, AU - Wopfner,Nicole, AU - Pabst,Martin, AU - Stadlmann,Johannes, AU - Petersen,Bent O, AU - Duus,Jens Ø, AU - Himly,Martin, AU - Radauer,Christian, AU - Gadermaier,Gabriele, AU - Razzazi-Fazeli,Ebrahim, AU - Ferreira,Fatima, AU - Altmann,Friedrich, Y1 - 2010/06/24/ PY - 2010/6/26/entrez PY - 2010/6/26/pubmed PY - 2010/9/21/medline SP - 27192 EP - 200 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 285 IS - 35 N2 - Art v 1, the major pollen allergen of the composite plant mugwort (Artemisia vulgaris) has been identified recently as a thionin-like protein with a bulky arabinogalactan-protein moiety. A close relative of mugwort, ragweed (Ambrosia artemisiifolia) is an important allergen source in North America, and, since 1990, ragweed has become a growing health concern in Europe as well. Weed pollen-sensitized patients demonstrated IgE reactivity to a ragweed pollen protein of apparently 29-31 kDa. This reaction could be inhibited by the mugwort allergen Art v 1. The purified ragweed pollen protein consisted of a 57-amino acid-long defensin-like domain with high homology to Art v 1 and a C-terminal proline-rich domain. This part contained hydroxyproline-linked arabinogalactan chains with one galactose and 5 to 20 and more alpha-arabinofuranosyl residues with some beta-arabinoses in terminal positions as revealed by high field NMR. The ragweed protein contained only small amounts of the single hydroxyproline-linked beta-arabinosyl residues, which form an important IgE binding determinant in Art v 1. cDNA clones for this protein were obtained from ragweed flowers. Immunological characterization revealed that the recombinant ragweed protein reacted with >30% of the weed pollen allergic patients. Therefore, this protein from ragweed pollen constitutes a novel important ragweed allergen and has been designated Amb a 4. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/20576600/A_new_allergen_from_ragweed__Ambrosia_artemisiifolia__with_homology_to_art_v_1_from_mugwort_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=20576600 DB - PRIME DP - Unbound Medicine ER -