Asero R, Mistrello G, Roncarolo D, de Vries S C, Gautier M F, Ciurana C L, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas J H, Bulder I, Aalberse R C, van Ree R
Ambulatorio di Allergologia, Ospedale Caduti Bollatesi, Bollate, Italy.
Int Arch Allergy Immunol. 2000 May;122(1):20-32. doi: 10.1159/000024355.
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.
The aim of this study was to investigate the cross-reactivity to non-Rosaceae LTPs, and to study the role of protein stability in allergenicity.
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 RAST 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.
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 cross-reactivities 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.
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.
脂质转移蛋白(LTPs)是分子量约为10 kD的小分子,具有高度稳定性。它们最近被鉴定为李属(桃、杏、李)和苹果亚科(苹果)蔷薇科亚族中的过敏原。它们属于一类结构高度保守的蛋白质家族,在非蔷薇科蔬菜食品中也存在。
本研究旨在调查对非蔷薇科LTPs的交叉反应性,并研究蛋白质稳定性在致敏性中的作用。
通过访谈和皮肤点刺试验(SPT)对38例对富含LTP的蔷薇科水果提取物SPT呈阳性的患者进行特征分析。为了研究蔷薇科和非蔷薇科LTPs之间的IgE交叉反应性,使用全食物提取物和纯化的LTPs进行了放射性变应原吸附试验(RAST)和RAST抑制试验以及酶联免疫吸附测定(ELISA)和ELISA抑制试验。其中包括纯化的天然LTPs(桃、胡萝卜和西兰花)和毕赤酵母重组LTPs(胡萝卜和小麦)。采用胃蛋白酶消化来研究稳定性在LTPs致敏性中的作用。
对蔷薇科LTPs的IgE抗体与多种蔬菜食品发生反应,包括禾本科(谷物)、豆科(花生)、胡桃科(核桃)、漆树科(开心果)、十字花科(西兰花)、伞形科(胡萝卜、芹菜)、茄科(番茄)、葫芦科(甜瓜)和猕猴桃科(猕猴桃)。用纯化的天然和重组LTPs进行的结合和抑制研究证实了它们在这种交叉反应性中的作用。许多这种交叉反应伴有临床食物过敏,经常包括全身反应。抗体与LTP的结合显示对全提取物或纯化LTP的胃蛋白酶处理具有抗性。
LTP是一种泛过敏原,其交叉反应程度与肌动蛋白结合蛋白相当。由于其对胃蛋白酶消化具有极强的抗性,LTP是一种潜在的严重食物过敏原。