Landa-Pineda C M, Arroyo-Becerra A, Rosas-Alvarado A, Terán L M, Garcia-Cruz M L, Marchat L A, Reyes-López C A
Sección de Estudios de Posgrado e Investigación, ENMyH, IPN, México.
CIBA, IPN, México.
Allergol Immunopathol (Madr). 2016 Mar-Apr;44(2):160-6. doi: 10.1016/j.aller.2015.05.002. Epub 2015 Aug 24.
Pollens represent a rich source of proteins that are also potential elicitors of IgE-mediated pollen allergy. Sensitisation to panallergens could play an important role in diagnosis and specific immunotherapy, because these molecules are present in different plant pollens and plant foods and have marked structural similarity in different species. Profilins are one of the most common panallergens to be studied because they are responsible for a large number of sensitisations and are clearly related to cross-reactivity and co-sensitisation. This study aimed to isolate and characterise a new allergen of Amaranthus palmeri pollen and to determine its allergenicity.
A. palmeri pollen profilin was purified using poly-l-proline-Sepharose affinity chromatography followed by anion exchanger chromatography. Identification of purified protein was carried out by mass spectrometry. Specific IgE was estimated in sera of patients with positive skin prick test to A. palmeri pollen extract, by enzyme-linked immunosorbent assay (ELISA).
Purified protein appeared as a single band at 14 kDa in SDS-PAGE gel. Mass spectrometric analysis of the gel band identified two highly conserved peptides corresponding to allergenic profilins from pollen of other plants. Sera from about 60% of allergic patients have IgE that recognises the purified A. palmeri protein.
A 14 kDa protein of A. palmeri pollen was purified and identified as allergenic profilin, which was recognised by sera from pollen allergic patients.
花粉是蛋白质的丰富来源，也是IgE介导的花粉过敏的潜在诱发因素。对泛过敏原的致敏在诊断和特异性免疫治疗中可能起重要作用，因为这些分子存在于不同的植物花粉和植物性食物中，并且在不同物种中具有显著的结构相似性。肌动蛋白单体结合蛋白是研究最多的常见泛过敏原之一，因为它们导致大量致敏反应，并且与交叉反应性和共同致敏明显相关。本研究旨在分离和鉴定一种新的帕尔默苋花粉过敏原，并确定其致敏性。
使用聚-L-脯氨酸-琼脂糖亲和层析，随后进行阴离子交换层析，纯化帕尔默苋花粉肌动蛋白单体结合蛋白。通过质谱法对纯化的蛋白质进行鉴定。通过酶联免疫吸附测定（ELISA），在对帕尔默苋花粉提取物皮肤点刺试验呈阳性的患者血清中估计特异性IgE。
纯化的蛋白质在SDS-PAGE凝胶中呈现为一条14 kDa的单带。对凝胶条带的质谱分析鉴定出两条高度保守的肽段，对应于来自其他植物花粉的致敏性肌动蛋白单体结合蛋白。约60%过敏患者的血清中有可识别纯化的帕尔默苋蛋白的IgE。
纯化并鉴定出帕尔默苋花粉一种14 kDa的蛋白质为致敏性肌动蛋白单体结合蛋白，花粉过敏患者的血清可识别该蛋白。
