Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins
Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins
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DOI：
10.1042/bsr20080117
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发表时间：
2009-06-01
影响因子：
4
通讯作者：
Roesch, Paul
中科院分区：
文献类型：
--
作者：
Berkner, Hanna;Neudecker, Philipp;Roesch, Paul
在许多情况下，对桦树花粉过敏的患者在摄入某些水果或蔬菜后也会出现过敏反应。这种观察在分子水平上是由于主要的桦树花粉变应原Bet v 1与同源食物变应原致敏而引起的IgE抗体的交叉反应。由于IgE抗体识别构象表位，因此需要对所涉及的过敏原进行精确的结构表征，以了解交叉反应，从而为过敏患者开发新的过敏原特异性免疫治疗方法。在这里，我们报道了大豆变应原Gly m4的三维溶液结构，Gly m4是Bet v1同源蛋白超家族的成员，它与最初针对Bet v1产生的IgE抗体发生交叉反应，通过免疫印迹抑制和组胺释放试验显示。虽然Gly m 4的整体折叠结构与Bet v 1非常相似，但它们的三维结构在细节上有所不同。显示这些差异的Gly m4局部结构也在已知生理功能的黄色羽扇豆蛋白中发现。因此，Gly m 4的三维结构可能会揭示PR10蛋白亚群(病程相关蛋白10类)的生理功能，并结合免疫学数据，允许我们提出可能代表交叉反应表位的表面补丁。
In many cases, patients allergic to birch pollen also show allergic reactions after ingestion of certain fruits or vegetables. This observation is explained at the molecular level by cross-reactivity of IgE antibodies induced by sensitization to the major birch pollen allergen Bet v 1 with homologous food allergens. As IgE antibodies recognize conformational epitopes, a precise structural characterization of the allergens involved is necessary to understand cross-reactivity and thus to develop new methods of allergen-specific immunotherapy for allergic patients. Here, we report the three-dimensional solution structure of the soybean allergen Gly m 4, a member of the superfamily of Bet v 1 homologous proteins and a cross-reactant with IgE antibodies originally raised against Bet v 1 as shown by immunoblot inhibition and histamine release assays. Although the overall fold of Gly m 4 is very similar to that of Bet v 1, the three-dimensional structures of these proteins differ in detail. The Gly m 4 local structures that display those differences are also found in proteins from yellow lupine with known physiological function. The three-dimensional structure of Gly m 4 may thus shed some light on the physiological function of this subgroup of PR10 proteins (class 10 of pathogenesis-related proteins) and, in combination with immunological data, allow us to propose surface patches that might represent cross-reactive epitopes.