A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

被引:69
|
作者
Leonard, Renaud [1 ]
Wopfner, Nicole [2 ]
Pabst, Martin [1 ]
Stadlmann, Johannes [1 ]
Petersen, Bent O. [3 ]
Duus, Jens O. [3 ]
Himly, Martin [2 ]
Radauer, Christian [4 ]
Gadermaier, Gabriele [2 ]
Razzazi-Fazeli, Ebrahim [5 ]
Ferreira, Fatima [2 ]
Altmann, Friedrich [1 ]
机构
[1] Univ Nat Resources & Appl Life Sci BOKU, Dept Chem, A-1190 Vienna, Austria
[2] Salzburg Univ, Christian Doppler Lab Allergy Diag & Therapy, Dept Mol Biol, A-5020 Salzburg, Austria
[3] Carlsberg Lab, DK-2500 Valby, Denmark
[4] Med Univ Vienna, Dept Pathophysiol, A-1090 Vienna, Austria
[5] Univ Vet Med, Core Facil Res, VetOMICS, A-1220 Vienna, Austria
基金
奥地利科学基金会;
关键词
POLLEN ALLERGENS; AMINO-ACIDS; O-GLYCANS; HYPERSENSITIVITY; GLYCOSYLATION; SENSITIZATION; PROTEINS; RESIDUES; BIOLOGY; BINDING;
D O I
10.1074/jbc.M110.127118
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:27192 / 27200
页数:9
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