Recombinant Proteins and Peptides as Tools for Studying IgE Reactivity with Low-Molecular-Weight Glutenin Subunits in Some Wheat Allergies

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• 作者：Jacques Sné ; garoff ; Gé ; rard Branlard ; Isabelle Bouchez-Mahiout ; Bé ; atrice Laudet ; Martina Tylichova ; Thierry Chardot ; Catherine Pecquet ; Dominique Choudat ; N. Raison-Peyron ; M. Vigan ; S. K
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2007
• 出版时间：November 28, 2007
• 年：2007
• 卷：55
• 期：24
• 页码：9837 - 9845
• 全文大小：1555K
• 年卷期：v.55,no.24(November 28, 2007)
• ISSN：1520-5118

文摘

Two genes of wheat low-molecular-weight glutenin subunits (LMW-GS), B16 and P73, were cloned and expressed in E. coli. They were homologous to proteins encoded respectively at Glu-B3 and Glu-D3 loci. The N-terminal and C-terminal halves of B16 (NB16 and B16C) and the two chimeras combining the halves of the two genes (B16-P73 and P73- B16) were also expressed. All these constructs were compared for their reactivity with IgE from 24 patients suffering from different forms of wheat allergies. The results confirmed that LMW-GSs bound IgE in all adult allergies tested. Strong differences in reactivity between all the constructs were observed. They were disease-dependent. In wheat-dependent exercise-induced anaphylaxis (WDEIA), the reactivity of the constructs depended partly on common epitopes with ω-5 gliadins but also on differences in molecule conformation. The presence of NB16 in the constructs greatly influenced their IgE reactivity.