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首页> 外文期刊>Clinical and experimental allergy : >A pectin methylesterase as an allergenic marker for the sensitization to Russian thistle (Salsola kali) pollen.
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A pectin methylesterase as an allergenic marker for the sensitization to Russian thistle (Salsola kali) pollen.

机译：果胶甲基酯酶作为对俄罗斯蓟（Salsola kali）花粉致敏的致敏标记。

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Background Chenopodiaceae pollen is considered the main cause of pollen allergy in desert countries and its incidence is world-wide increasing by the desertization of extensive zones. Although the correlation between the sensitization to Chenopodium album and Salsola kali pollens of patients suffering from allergy to Chenopodiaceae pollens is high, a significant number of patients exhibited IgE sensitivity exclusively towards S. kali. Objective To analyse this differential reactivity and to purify, clone and characterize the putative responsible allergen. Methods Immunoblotting was used to analyse the IgE binding to pollen extract for S. kali and C. album. The protein was isolated by two chromatographic steps and characterized by Edman degradation, mass spectrometry, finger print analysis and Concanavalin A lectin staining. Specific cDNA was amplified by polymerase chain reaction, cloned in Escherichia coli and sequenced. Immunologic characterization was performed by immunoblotting, enzyme-linked immunoassay detection and inhibition experiments using sera from 11 patients allergic to S. kali pollen. Results cDNA codifies for a mature protein of 339 amino acids plus a putative signal peptide of 23 residues and it belongs to the plant pectin methylesterase (PME) family. It is a mildly basic and polymorphic protein and was recognized by the IgE from all the patients allergic to S. kali included in the study, and was called Sal k 1. The protein was not recognized in the C. album pollen extract using the sera of these patients. Conclusion Sal k 1 is a protein from the PME family with a high allergenic relevance. Considering this allergen as responsible for the different sensitization between S. kali and C. album pollen, it may be a useful marker to classify patients allergic to Chenopodiaceae allowing a safer and more specific immunotherapy.
机译：背景藜科花粉被认为是沙漠国家花粉过敏的主要原因，由于广泛地区的沙漠化，其发生率在世界范围内呈上升趋势。尽管对藜科花粉过敏的患者对藜科白粉病的敏感性和对Salsola kali花粉的敏感性之间的相关性很高，但仍有大量患者仅对卡氏链球菌表现出IgE敏感性。目的分析这种差异反应性，并纯化，克隆和表征可能的负责任过敏原。方法采用免疫印迹法分析卡利链球菌和相册链球菌的IgE与花粉提取物的结合。通过两个色谱步骤分离了该蛋白，并通过Edman降解，质谱，指纹分析和伴刀豆球蛋白A凝集素染色进行了表征。通过聚合酶链反应扩增特异性cDNA，克隆到大肠杆菌中并测序。通过免疫印迹，酶联免疫测定和抑制实验，使用11名对卡利链球菌花粉过敏的患者的血清进行免疫学表征。结果cDNA编码一个339个氨基酸的成熟蛋白和一个23个残基的推定信号肽，属于植物果胶甲基酯酶（PME）家族。它是一种轻度碱性且多态的蛋白，被研究中包括的所有对卡氏链球菌过敏的患者均被IgE识别，被称为Sal k1。该蛋白在血清中的C. album花粉提取物中无法识别。这些患者中。结论Sal k 1是PME家族的一种蛋白，具有很高的过敏原相关性。考虑到这种变应原是造成卡氏链球菌和相册隐孢子虫花粉不同致敏性的原因，它可能是有用的标记，可将对藜科过敏的患者分类，从而实现更安全，更特异性的免疫治疗。

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