Mousavi Fateme, Majd Ahmad, Shahali Youcef, Ghahremaninejad Farrokh, Shokouhi Shoormasti Raheleh, Pourpak Zahra
Department of Plant Sciences, Faculty of Biological Sciences, Kharazmi University, Tehran, Iran.
Department of Plant Sciences, Faculty of Biological Sciences, Kharazmi University, Tehran, Iran; Department of Biology, Faculty of Biological Sciences, Islamic Azad University, North Tehran Branch, Tehran, Iran.
J Proteomics. 2017 Feb 10;154:94-101. doi: 10.1016/j.jprot.2016.12.013. Epub 2016 Dec 30.
Ailanthus altissima pollen (AAP) is considered as an emerging cause of respiratory allergy in United States, Italy and Iran. However, the allergenic composition of AAP is still unknown and has yet to be characterized. The present study aimed to identify AAP allergens using a proteomics-based approach. For this purpose, optimized AAP protein extracts were analyzed using 1D- and 2D- gel electrophoresis and confronted to twenty sera from individuals with respiratory allergy during the AAP season. Candidate allergens were detected using the serum from an allergic patient with clinical history of AAP pollinosis. IgE-binding spots were identified using MALDI-TOF/TOF mass spectrometry and database searching. According to our results, AAP extracts were rich in proteins (up to 16.25mg/ml) with a molecular-weight distribution ranging from 10 to 175kDa. Two-D electrophoresis of AAP extracts revealed 125 protein spots from which 13 were IgE reactive. These IgE-binding proteins were identified as enolase, calreticulin, probable pectate lyase 6, conserved hypothetical protein and ras-related protein RHN1-like. By our knowledge, this study is the first report identifying AAP allergens. These findings will open up further avenues for the diagnosis and immunotherapy of the AAP allergy as well as for the cloning and molecular characterization of relevant allergens.
Ailanthus altissima colonizes new areas every year in Iran and is spreading aggressively worldwide. According to USDA, the tree of heaven is now present as an invasive plant in 30 states in US (www.invasivespeciesinfo.gov/plants/treeheaven.shtml) and come to dominate large areas in many regions. Up to now, several cases of allergy to A. altissima pollen have been reported in United States, Italy and Iran [1-4]. However, there is still no information on the sensitizing allergens and the molecular origin of these clinical symptoms, which constitutes a serious threat to patients suffering from respiratory allergies in these regions. To our knowledge, the current study describes, therefore, the first panel of proteins responsible for IgE-mediated A. altissima pollinosis by using a gel-based proteomic approach. This work represents the pioneer proteomic investigation on Simaroubaceae spp. and provides useful insights for further studies on the allergens of this widely distributed plant family.
在美国、意大利和伊朗，臭椿花粉（AAP）被认为是引起呼吸道过敏的一个新原因。然而，AAP的致敏成分仍然未知，尚未得到鉴定。本研究旨在采用基于蛋白质组学的方法鉴定AAP过敏原。为此，使用一维和二维凝胶电泳分析优化后的AAP蛋白提取物，并与AAP季节期间患有呼吸道过敏的20名个体的血清进行比对。使用一名有AAP花粉症临床病史的过敏患者的血清检测候选过敏原。使用基质辅助激光解吸电离飞行时间/串联飞行时间质谱（MALDI-TOF/TOF MS）和数据库搜索鉴定IgE结合斑点。根据我们的结果，AAP提取物富含蛋白质（高达16.25mg/ml），分子量分布范围为10至175kDa。AAP提取物的双向电泳显示125个蛋白斑点，其中13个具有IgE反应性。这些IgE结合蛋白被鉴定为烯醇化酶、钙网蛋白、可能的果胶酸裂解酶6、保守的假定蛋白和类ras相关蛋白RHN1。据我们所知，本研究是鉴定AAP过敏原的首篇报道。这些发现将为AAP过敏的诊断和免疫治疗以及相关过敏原的克隆和分子表征开辟进一步的途径。
臭椿在伊朗每年都在开拓新的区域，并在全球范围内迅速蔓延。根据美国农业部的数据，臭椿现已作为一种入侵植物出现在美国30个州（www.invasivespeciesinfo.gov/plants/treeheaven.shtml），并在许多地区占据大片区域。到目前为止，在美国、意大利和伊朗已经报道了几例对臭椿花粉过敏病例[1-4]。然而，关于致敏过敏原以及这些临床症状的分子起源仍然没有信息，这对这些地区患有呼吸道过敏的患者构成了严重威胁。据我们所知，本研究因此首次通过基于凝胶的蛋白质组学方法描述了一组负责IgE介导的臭椿花粉症的蛋白质。这项工作代表了对苦木科植物的开创性蛋白质组学研究，并为进一步研究这个广泛分布的植物科的过敏原提供了有用的见解。
