Lipid transfer protein: A pan-allergen in plant-derived foods that is highly resistant to pepsin digestion

被引:251
作者
Asero, R
Mistrello, G
Roncarolo, D
de Vries, SC
Gautier, MF
Ciurana, LF
Verbeek, E
Mohammadi, T
Knul-Brettlova, V
Akkerdaas, JH
Bulder, I
Aalberse, RC
van Ree, R
机构
[1] CLB, Dept Allergy, NL-1066 CX Amsterdam, Netherlands
[2] Osped Caduti Bollatesi, Ambulatorio Allergol, Bollate, Italy
[3] Lofarma SPA, Milan, Italy
[4] Wageningen Univ Agr, Dept Biol Mol, Wageningen, Netherlands
[5] INRA, Unite Biochim & Biol Mol Cereales, F-34060 Montpellier, France
[6] Univ Amsterdam, Acad Med Ctr, Expt & Clin Immunol Lab, Amsterdam, Netherlands
[7] Prinsengracht Hosp, Dept Allergol, Amsterdam, Netherlands
关键词
food allergy; cross-reactivity; lipid transfer protein; protein stability; recombinant allergens;
D O I
10.1159/000024355
中图分类号
R392 [医学免疫学];
学科分类号
100102 ;
摘要
Background: Lipid transfer proteins (LTPs) are small molecules of approximately 10 kD that demonstrate high stability. They have recently been identified as allergens in the Rosaceae subfamilies of the Prunoideae (peach, apricot, plum) and of the Pomoideae (apple). They belong to a family of structurally highly conserved proteins that are also present in non-Rosaceae vegetable foods. Objective: The aim of this study was to investigate the crossreactivity to non-Rosaceae LTPs, and to study the role of protein stability in allergenicity. Methods: Thirty-eight patients with a positive SPT to Rosaceae fruit extracts enriched for LTP were characterized by interview and SPT. To investigate IgE cross-reactivity between Rosaceae and non-Rosaceae LTPs, RAST and PAST inhibition as well as ELISA and ELISA inhibition were performed, using whole food extracts and purified LTPs. Both purified natural LTPs (peach, carrot and broccoli) and Pichia pastoris recombinant LTPs (carrot and wheat) were included. Pepsin digestion was used to address the role of stability in the allergenicity of LTPs. Results: IgE antibodies to Rosaceae LTPs reacted to a broad range of vegetable foods, including Gramineae (cereals), Leguminosae (peanut), Juglandaceae (walnut), Anacardiaceae (pistachio), Brassicaceae (broccoli), Umbelliferae (carrot, celery), Solanaceae (tomato), Cucurbitaceae (melon), and Actinidiaceae (kiwi). Binding and inhibition studies with purified natural and recombinant LTPs confirmed their role in this cross-reactivity. Many of these crossreactivities were accompanied by clinical food allergy, frequently including systemic reactions. Antibody binding to LTP was shown to be resistant to pepsin treatment of whole extract or purified LTP. Conclusion: LTP is a pan-allergen with a degree of cross-reactivity comparable to profilin. Due to its extreme resistance to pepsin digestion, LTP is a potentially severe food allergen. Copyright (C) 2000 S. Karger AG, Basel.
引用
收藏
页码:20 / 32
页数:13
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