原标题：标准化过敏原Blo t 12 的免疫学特征：IgE表位的鉴定
①IgE对标准化过敏原反应的差异可能具有临床意义;因此，对其进行分析将有助于设计出更好的诊断和治疗过敏性呼吸道疾病的方法。已有研究对螨虫过敏原中的几种亚型进行了特征描述，但是还没有有关热带无爪螨标准化过敏原的临床意义的信息。②评价两种Blo t 12标准化过敏原的IgE反应性的差异。③用ELISA法、皮肤点试验和ELISA交叉抑制法分析了Blo t 12标准化过敏原的IgE结合特性。用合成的重叠多肽进行表位定位。采用折叠识别方法对两种过敏原的甲壳素结合域进行建模。④Blo t 12.0101的IgE反应频率和强度大于Blo t 12.0102。在Blo t 12.0101中确定了3个IgE结合区;其中一个包含了Blo t 12.0102中不同的两个残基。这些过敏原的甲壳素结合区模型预测，它们具有结构差异，可能影响抗体对这些表位中的其中一个的识别。在Blo t 12生物信息学的结构分析和免疫学表征中发现过敏原多态性影响IgE反应性。⑤Blo t 12.0101是卡塔赫纳地区最具IgE活性的无爪螨过敏原亚型。鉴定出的IgE表位可以经过突变，来获得可能用于免疫治疗的低过敏性分子。
Clin Exp Allergy
Immunological characterization of a Blo t 12 isoallergen: identification of immunoglobulin E epitopes
Differences in the IgE response to isoallergens could have clinical implications; therefore, its analysis will contribute to the design of better strategies for the diagnosis and treatment of allergic respiratory diseases. Several isoforms have been described from mites but there is no information about the clinical impact of Blomia tropicalis isoallergens.
Objective To evaluate the differences in the IgE response against two Blo t 12 isoallergens.
Methods The IgE‐binding properties of Blo t 12 isoallergens were analysed by ELISA, a skin prick test and ELISA cross‐inhibition. Epitope mapping was performed using synthetic overlapping peptides. Fold recognition methods were used to model the chitin‐binding domain of the two isoallergens. Results The frequency and strength of the IgE response were greater for Blo t 12.0101 than for Blo t 12.0102. Three IgE‐binding areas were identified in Blo t 12.0101; one of them included two residues that are different in Blo t 12.0102. Modelling of the chitin‐binding domains of these allergens predicted that they have structural differences that could influence antibody recognition of one of these epitopes. Conclusion In silico structural analysis and immunological characterization of Blo t 12 reveals that allergen polymorphism influences IgE reactivity. Blo t 12.0101 is the most IgE‐reactive isoform in Cartagena. The identified IgE epitopes could be mutated to obtain hypoallergenic molecules of potential use for immunotherapy.
J. Zakzuk S. Jiménez N. Cheong L. Puerta B. W. Lee K. Y. Chua L. Caraballo