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首页> 外文会议>Collegium Internationale Allergologicum >Epitope Mapping and Characterization of the Binding Specificity of Monoclonal Antibodies Directed Against Allergens of Grass Group 1
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Epitope Mapping and Characterization of the Binding Specificity of Monoclonal Antibodies Directed Against Allergens of Grass Group 1

机译：针对草组过敏原的单克隆抗体结合特异性的表位测绘和表征

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Background: Grass group 1 allergens consist of potent IgE-binding components which are found in all grass species. For studies of allergen extracts and for use as diagnostic markers we examined the epitope requirements for three monoclonal antibodies (mAbs) HB7, IG12 and Bol4 in detail. Methods: To determine the epitopes of the three mAbs we performed a screening of recombinantly produced group 1 allergen fragments. Further delimiting investigations were done by the PEPSCAN and SPOT technique using synthesized overlapping decapeptides covering the complete Phl p 1 molecule. Definition of the epitopes was performed with synthesized peptides spanning the respective epitopes and mutating each amino acid position by the 20 possible amino acid residues. By competition ELISA we analyzed whether the mAbs competed with patients' IgE for binding sites. Results: The epitopes of Phl p 1-directed mAbs were located on three different regions on the allergen. In case of HB7, we could encircle the epitope to the 27 N-terminal amino acids employing a set of recombinant fragments. The epitopes of IG12 and Bol4 could be limited to amino acid residues 48-53 and 225-232, respectively, and their exact epitope structure was studied by amino acid exchanges. None of the antibodies revealed an inhibitory influence on IgE binding. Conclusion: The results demonstrate clearly definable linear epitopes for the mAbs IG12 and Bol4, while the HB7 epitope seems to span a wider region probably due to conformational segments. These studies will help designing assays for monitoring and isolating group 1 allergens by affinity chromatography.
机译：背景：Grass组1过敏原由所有草种中发现的有效的IgE结合组分组成。对于过敏原提取物以及用作诊断标志物研究中，我们详细研究了三种单克隆抗体（mAb）HB7，IG12和Bol4表位的要求。方法：确定三种mAb的表位，我们进行了重组产生的第1组过敏原片段的筛选。使用覆盖完整的PHL P 1分子的合成重叠的抑制肽，通过PEPSCAN和现货技术进行进一步分隔调查。用跨越相应表位的合成肽进行表位的定义，并通过20个可能的氨基酸残基突变每个氨基酸位置。通过竞争ELISA，我们分析了MAB是否与患者的IGE竞争结合。结果：PHL P 1针对主的MAb的表位位于过敏原的三个不同地区。在HB7的情况下，我们可以将表位环绕到采用一组重组片段的27 n末端氨基酸。 IG12和Bol4的表位可以被分别限制为氨基酸残基48-53和225-232，并通过氨基酸交换研究了它们的确切的表位的结构。没有抗体揭示对IgE结合的抑制作用。结论：结果表明对单抗IG12和Bol4明确定义的线性表位，而表位HB7似乎可能跨越更宽的区域，由于构象段。这些研究将有助于设计试验通过亲和层析监测和隔离组1种过敏原。

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