Centro Nacional de Ressonância Magnética Nuclear, Universidade Federal do Rio de Janeiro, Instituto de Bioquímica Médica, Rio de Janeiro, Brazil.
Structure. 2010 Aug 11;18(8):1011-21. doi: 10.1016/j.str.2010.05.012.
The interaction of specific IgE antibodies with allergens is a key event in the induction of allergic symptoms, thus representing an important target for therapeutic interventions in Type I allergies. We report here the solution NMR structure of Art v 1, the major mugwort pollen allergen. Art v 1 is the first protein structure with an allergenic defensin fold linked to a polyproline domain, which has not been identified in any reported allergen structure in the PDB. Moreover, the direct interaction of polyclonal IgE antibodies from an allergic patient has been mapped on the surface of an allergen for the first time. The data presented herein provide the basis for the design of tools for safe and effective vaccination against mugwort pollen allergy.
特异性 IgE 抗体与过敏原的相互作用是诱导过敏症状的关键事件,因此代表了 I 型过敏治疗干预的重要目标。我们在这里报告 Art v 1 的溶液 NMR 结构,Art v 1 是具有过敏原防御折叠与多脯氨酸结构域相连的第一个蛋白质结构,在 PDB 中报告的任何过敏原结构中都未识别出这种结构域。此外,首次在过敏原表面上绘制了来自过敏患者的多克隆 IgE 抗体的直接相互作用。本文提供的资料为设计安全有效的艾蒿花粉过敏疫苗的工具提供了基础。