Indoor Biotechnologies, Inc., Charlottesville, Va., USA.
Int Arch Allergy Immunol. 2010;152(1):1-11. doi: 10.1159/000260078. Epub 2009 Nov 26.
The 3-dimensional structure of an allergen defines the accessible parts on the surface of the molecule or epitopes that interact with antibodies. Mapping the antigenic determinants for IgE antibody binding has been pursued through strategies based on the use of overlapping synthetic peptides, recombinant allergenic fragments or unfolded allergens. These approaches led to the identification of mostly linear epitopes and are useful for food allergens that undergo digestion or food processing. For inhaled allergens, conformational epitopes appear to be the primary targets of IgE responses. Knowledge of the molecular structure of allergens alone and in complex with antibodies that interfere with IgE antibody binding is important to understand the immune recognition of B cell-antigenic determinants on allergens and the design of recombinant allergens for immunotherapy. Starting with the molecular cloning and expression of allergens, and with the advent of X-ray crystallography and nuclear magnetic resonance techniques, we have been able to visualize conformational epitopes on allergens.
过敏原的三维结构决定了分子表面可及的部分或与抗体相互作用的表位。通过基于使用重叠合成肽、重组变应原片段或未折叠变应原的策略来定位 IgE 抗体结合的抗原决定簇已经得到了探索。这些方法主要导致了线性表位的鉴定，并且对于经历消化或食品加工的食物过敏原很有用。对于吸入性过敏原，构象表位似乎是 IgE 反应的主要靶标。了解过敏原的分子结构以及与干扰 IgE 抗体结合的抗体的结合对于理解 B 细胞抗原决定簇在过敏原上的免疫识别以及为免疫治疗设计重组过敏原非常重要。从过敏原的分子克隆和表达开始，随着 X 射线晶体学和核磁共振技术的出现，我们已经能够在过敏原上可视化构象表位。
