Role of complex asparagine-linked glycans in the allergenicity of plant glycoproteins
Role of complex asparagine-linked glycans in the allergenicity of plant glycoproteins
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DOI：
10.1093/glycob/6.4.471
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发表时间：
1996-06-01
期刊：
影响因子：
4.3
通讯作者：
Gomez, L
中科院分区：
文献类型：
--
作者：
GarciaCasado, G;SanchezMonge, R;Gomez, L
许多植物蛋白，特别是在食物和花粉中发现的植物蛋白，在反复接触后会对人类起致敏作用。在与哮喘反应有关的谷物面粉蛋白中，糖基化的a-淀粉酶抑制剂家族成员，多肽BMAI-1， BTAI-CMb*和WTAI-CM16*在体内和体外都具有特别的活性。我们在这里表明，这些主要的糖蛋白过敏原携带一个单一的天冬酰胺连接的复杂聚糖，包含β 1 -> 2木糖和α 1 -> 3焦点。证据表明，木糖基残基和聚焦基残基（在较小程度上）是关键的ige结合表位，在很大程度上负责这些和来自植物和昆虫的不相关蛋白质的致敏性。我们的研究结果表明，木糖和含焦的复合聚糖在过敏反应中的作用可能被低估了；这些聚糖为解释花粉、植物性食物和昆虫过敏原之间经常观察到的交叉反应提供了结构基础。
Many plant proteins, particularly those found in foods and pollen, are known to act as sensitizing agents in humans upon repeated exposure, Among the cereal flour proteins involved in asthmatic reactions, those members of the a-amylase inhibitor family which are glycosylated, polypeptides BMAI-1, BTAI-CMb*, and WTAI-CM16* are particularly reactive both in vivo and in vitro, We show here that these major glycoprotein allergens carry a single asparagine-linked complex glycan that contains both beta 1 --> 2 xylose and alpha 1 --> 3 fucose, Evidence is presented that the xylosyl residue and, to a lesser extent, the fucosyl residue are key IgE-binding epitopes and largely responsible for the allergenicity of these and unrelated proteins from plants and insects, Our results suggest that the involvement of xylose- and fucose-containing complex glycans in allergenic responses may have been underestimated previously; these glycans provide a structural basis to help explain the cross-reactivities often observed between pollen, vegetable food, and insect allergens.