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Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin-like and a hydroxyproline-rich domain.
FASEB J. 2003 Jan; 17(1):106-8.FJ

Abstract

In late summer, pollen grains originating from Compositae weeds (e.g., mugwort, ragweed) are a major source of allergens worldwide. Here, we report the isolation of a cDNA clone coding for Art v 1, the major allergen of mugwort pollen. Sequence analysis showed that Art v 1 is a secreted allergen with an N-terminal cysteine-rich domain homologous to plant defensins and a C-terminal proline-rich region containing several (Ser/Ala)(Pro)2-4 repeats. Structural analysis showed that some of the proline residues in the C-terminal domain of Art v 1 are posttranslationally modified by hydroxylation and O-glycosylation. The O-glycans are composed of 3 galactoses and 9-16 arabinoses linked to a hydroxyproline and represent a new type of plant O-glycan. A 3-D structural model of Art v 1 was generated showing a characteristic "head and tail" structure. Evaluation of the antibody binding properties of natural and recombinant Art v 1 produced in Escherichia coli revealed the involvement of the defensin fold and posttranslational modifications in the formation of epitopes recognized by IgE antibodies from allergic patients. However, posttranslational modifications did not influence T-cell recognition. Thus, recombinant nonglycosylated Art v 1 is a good starting template for engineering hypoallergenic vaccines for weed-pollen therapy.

Authors+Show Affiliations

Institute of Genetics and General Biology, University of Salzburg, A-5020 Salzburg, 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)

Comparative Study
Journal Article

Language

eng

PubMed ID

12475905

Citation

Himly, Martin, et al. "Art V 1, the Major Allergen of Mugwort Pollen, Is a Modular Glycoprotein With a Defensin-like and a Hydroxyproline-rich Domain." FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, vol. 17, no. 1, 2003, pp. 106-8.
Himly M, Jahn-Schmid B, Dedic A, et al. Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin-like and a hydroxyproline-rich domain. FASEB J. 2003;17(1):106-8.
Himly, M., Jahn-Schmid, B., Dedic, A., Kelemen, P., Wopfner, N., Altmann, F., van Ree, R., Briza, P., Richter, K., Ebner, C., & Ferreira, F. (2003). Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin-like and a hydroxyproline-rich domain. FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, 17(1), 106-8.
Himly M, et al. Art V 1, the Major Allergen of Mugwort Pollen, Is a Modular Glycoprotein With a Defensin-like and a Hydroxyproline-rich Domain. FASEB J. 2003;17(1):106-8. PubMed PMID: 12475905.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Art v 1, the major allergen of mugwort pollen, is a modular glycoprotein with a defensin-like and a hydroxyproline-rich domain. AU - Himly,Martin, AU - Jahn-Schmid,Beatrice, AU - Dedic,Azra, AU - Kelemen,Peter, AU - Wopfner,Nicole, AU - Altmann,Friedrich, AU - van Ree,Ronald, AU - Briza,Peter, AU - Richter,Klaus, AU - Ebner,Christof, AU - Ferreira,Fátima, Y1 - 2002/11/15/ PY - 2002/12/12/pubmed PY - 2003/2/11/medline PY - 2002/12/12/entrez SP - 106 EP - 8 JF - FASEB journal : official publication of the Federation of American Societies for Experimental Biology JO - FASEB J. VL - 17 IS - 1 N2 - In late summer, pollen grains originating from Compositae weeds (e.g., mugwort, ragweed) are a major source of allergens worldwide. Here, we report the isolation of a cDNA clone coding for Art v 1, the major allergen of mugwort pollen. Sequence analysis showed that Art v 1 is a secreted allergen with an N-terminal cysteine-rich domain homologous to plant defensins and a C-terminal proline-rich region containing several (Ser/Ala)(Pro)2-4 repeats. Structural analysis showed that some of the proline residues in the C-terminal domain of Art v 1 are posttranslationally modified by hydroxylation and O-glycosylation. The O-glycans are composed of 3 galactoses and 9-16 arabinoses linked to a hydroxyproline and represent a new type of plant O-glycan. A 3-D structural model of Art v 1 was generated showing a characteristic "head and tail" structure. Evaluation of the antibody binding properties of natural and recombinant Art v 1 produced in Escherichia coli revealed the involvement of the defensin fold and posttranslational modifications in the formation of epitopes recognized by IgE antibodies from allergic patients. However, posttranslational modifications did not influence T-cell recognition. Thus, recombinant nonglycosylated Art v 1 is a good starting template for engineering hypoallergenic vaccines for weed-pollen therapy. SN - 1530-6860 UR - https://www.unboundmedicine.com/medline/citation/12475905/Art_v_1_the_major_allergen_of_mugwort_pollen_is_a_modular_glycoprotein_with_a_defensin_like_and_a_hydroxyproline_rich_domain_ L2 - http://www.fasebj.org/doi/full/10.1096/fj.02-0472fje?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -