Allergy is becoming an intensifying disease among the world population, particularly in the developed world. Once allergy develops, sufferers are permanently trapped in a hyper-immune response that makes them sensitive to innocuous substances. The immune pathway concerned with developing allergy is the Th immune pathway where the IgE antibody binds to its FcRI receptor on Mast and Basophil cells. This paper discusses a protocol that could disrupt the binding between the antibody and its receptor for a potential permanent treatment. Ten proteins were computationally designed to display a human IgE motif very close in proximity to the IgE antibody’s FcRI receptor’s binding site in an effort for these proteins to be used as a vaccine against our own IgE antibody. The motif of interest was the FG loop motif and it was excised and grafted onto a protein (PDB ID ), then the motif + scaffold structure had its sequence re-designed around the motif to find an amino acid sequence that would fold to the designed structure correctly. These ten computationally designed proteins showed successful folding when simulated using Rosetta’s AbinitioRelax folding simulation and the IgE epitope was clearly displayed in its native three-dimensional structure in all of them. These designed proteins have the potential to be used as a pan anti-allergy vaccine. This work employed

中文翻译：

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通过计算将 IgE 表位移植到支架上：对泛抗过敏疫苗设计​​的影响


过敏正在成为世界人口中一种日益严重的疾病，特别是在发达国家。一旦发生过敏，患者就会永久陷入过度免疫反应，使他们对无害物质敏感。与过敏有关的免疫途径是 Th 免疫途径，其中 IgE 抗体与肥大细胞和嗜碱性细胞上的 FcRI 受体结合。本文讨论了一种可能破坏抗体与其受体之间结合的方案，以实现潜在的永久性治疗。经过计算设计了十种蛋白质，以非常接近 IgE 抗体的 FcRI 受体结合位点显示人类 IgE 基序，以便将这些蛋白质用作针对我们自己的 IgE 抗体的疫苗。感兴趣的基序是 FG 环基序，将其切除并移植到蛋白质（PDB ID）上，然后基序 + 支架结构围绕该基序重新设计其序列，以找到可折叠为设计的氨基酸序列结构正确。当使用 Rosetta 的 AbinitioRelax 折叠模拟进行模拟时，这十种计算设计的蛋白质显示出成功的折叠，并且 IgE 表位在所有蛋白质中都以其天然三维结构清晰地显示。这些设计的蛋白质有潜力用作泛抗过敏疫苗。本工作聘用