β(1,2)-xylose and α(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens
β(1,2)-xylose and α(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens
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DOI：
10.1074/jbc.275.15.11451
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发表时间：
2000-04-14
影响因子：
4.8
通讯作者：
Lerouge, P
中科院分区：
文献类型：
--
作者：
van Ree, R;Cabanes-Macheteau, M;Lerouge, P
确定了两种主要花粉过敏原（Lol p 11和Ole e 1）和一种主要花生过敏原（Ara h 1）的N-聚糖的一级结构。Ole e 1和Ara h 1携带高甘露糖和复合N-聚糖，而Lol p 11仅携带复合物。复合物结构都具有与核心甘露糖连接的β（1，2）-木糖。在Lol p 11和Ole e 1的小部分上观察到近端N-乙酰葡糖胺被α（1，3）-岩藻糖取代，但在Ara h 1上没有。用三种变应原的蛋白酶和一组具有已知N-聚糖结构的糖蛋白进行放射性变应原吸附试验分析。已证明α（1，3）-岩藻糖和β（1，2）-木糖均参与IgE结合。令人惊讶的是，与Lol p 11和菠萝蛋白酶结合的木糖特异性IgE抗体不识别辣根过氧化物酶、植物半乳糖苷酶、Ole e 1和Ara h 1上密切相关的含木糖结构。在Lol p 11和菠萝蛋白酶上，核心β-甘露糖仅被α（1，6）-甘露糖取代。在其他含木糖的N-聚糖上，存在额外的α（1，3）-甘露糖。这些观察结果表明，IgE与木糖的结合在空间上受到α（1，3）-天线的阻碍。
Primary structures of the N-glycans of two major pollen allergens (Lol p 11 and Ole e 1) and a major peanut allergen (Ara h 1) were determined. Ole e 1 and Ara h 1 carried high mannose and complex N-glycans, whereas Lol p 11 carried only the complex. The complex structures all had a beta(1,2)-xylose linked to the core mannose, Substitution of the proximal N-acetylglucosamine with an alpha(1,3)-fucose was observed on Lol p 11 and a minor fraction of Ole e 1 but not on Ara h 1, To elucidate the structural basis for IgE recognition of plant N-glycans, radioallergosorbent test analysis with protease digests of the three allergens and a panel of glycoproteins with known N-glycan structures was performed. It was demonstrated that both alpha(1,3)-fucose and beta(1,2)-xylose are involved in IgE binding. Surprisingly, xylose-specific IgE antibodies that bound to Lol p 11 and bromelain did not recognize closely related xylose-containing structures on horseradish peroxidase, phytohemeagglutinin, Ole e 1, and Ara h 1, On Lol p 11 and bromelain, the core beta-mannose is substituted with just an alpha(1,6)-mannose. On the other xylose-containing N-glycans, an additional alpha(1,3)-mannose is present. These observations indicate that IgE binding to xylose is sterically hampered by the presence of an alpha(1,3)-antenna.