Cross-reactivity between peanut and lupin proteins

被引:16
|
作者
Sirtori, Elena [1 ]
Resta, Donatella [2 ]
Arnoldi, Anna [1 ,2 ]
Savelkoul, Huub F. J. [3 ]
Wichers, Harry J. [3 ,4 ]
机构
[1] Univ Milan, Lab Chim Alimenti & Spettrometria Massa, Dipartimento Endocrinol Fisiopatol & Biol Appl, I-20133 Milan, Italy
[2] HPF Nutraceut Srl, I-20133 Milan, Italy
[3] Univ Wageningen & Res Ctr, Cell Biol & Immunol Grp, NL-6709 PG Wageningen, Netherlands
[4] Univ Wageningen & Res Ctr, Agrotechnol & Food Sci Grp, NL-6703 HD Wageningen, Netherlands
关键词
de novo sequencing; ELISA; Food allergy; Glycoprotein; Two-dimensional electrophoresis; IGE-BINDING; PRIMARY SENSITIZATION; FOOD ALLERGENS; FLOUR; ANAPHYLAXIS; ASTHMA; CHILD; RISK; SEED; INHALATION;
D O I
10.1016/j.foodchem.2010.11.073
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Peanut-allergic individuals may also react to lupin, which, for this reason, has been included in the EU list of food allergens. Since there is not yet any general consensus on the major allergen/s in lupin, the objective of this investigation was to compare the reactivity of the main lupin proteins towards the IgE of the sera of allergic patients. Both Lupinus taus and Lupinus angustifolius were investigated. ELISA's, Western blotting and mass spectrometry, including also de novo sequencing of the unknown lupin proteins, were used for identifying the IgE-binding proteins. Significant differences in the protein reactivities were observed. In particular, there was a direct relationship between the level of peanut-specific IgE's and the cross-reactivity to lupin proteins; also the reactivity of each serum appeared to be unique. Although numerous lupin proteins bind IgE's, our data suggest a predominant contribution of alpha-conglutin in the reactivity of both L albus and L. angustifolius. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:902 / 910
页数:9
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