Breiteneder Heimo, Mills Clare
Department of Pathophysiology, Medical University of Vienna, Vienna, Austria.
Mol Nutr Food Res. 2006 Jul;50(7):628-32. doi: 10.1002/mnfr.200500274.
Cross-reactivity of allergens results from the presence of antibody-accessible conserved surface structures. These can best be studied when allergens have been structurally defined by X-ray crystallography or another structure determination method. When this is not the case, mimotope technology provides a useful alternative for elucidating antibody-binding sites on allergens. Structural bioinformatic approaches have been used to study the cross-reactivity of inhalant allergens with labile food allergens (Bet v 1 family) as well as the cross-reactivity between stable food allergens such as members of the nonspecific lipid transfer protein family. It was found that the degree of similarity of the structures correlated with the observed IgE cross-reactivities. However, IgE cross-reactivity between structurally unrelated allergens has not been demonstrated to date.
变应原的交叉反应性源于存在抗体可及的保守表面结构。当变应原已通过X射线晶体学或其他结构测定方法进行结构定义时,对这些结构进行研究最为理想。若情况并非如此,模拟表位技术为阐明变应原上的抗体结合位点提供了一种有用的替代方法。结构生物信息学方法已被用于研究吸入性变应原与不稳定食物变应原(Bet v 1家族)之间的交叉反应性,以及稳定食物变应原(如非特异性脂质转移蛋白家族成员)之间的交叉反应性。研究发现,结构的相似程度与观察到的IgE交叉反应性相关。然而,迄今为止,尚未证实结构不相关的变应原之间存在IgE交叉反应性。