{"title":"Peanut allergens.","authors":"Wolf-Meinhard Becker, Uta Jappe","doi":"10.1159/000359916","DOIUrl":null,"url":null,"abstract":"<p><p>The earliest known evidence of peanut farming dates back 7,600 years. With a prevalence of roughly 1%, peanut allergy is a diagnostic and treatment challenge, but is also a very good model for studying all aspects of food allergy, including its molecular basis and pathomechanisms. Therefore, the very starting point for elucidating all these aspects is the identification of peanut allergens with subsequent clearing of their structure and their preparation as pure recombinant and/or natural allergens. This is the basis for in vitro diagnostic tests as well as the development of immunotherapeutic drugs. With regard to class I food allergy, peanut allergy affects by far the largest group of patients. In peanuts, 12 allergens have been identified and their molecular characteristics are described herein. Ara h 1, Ara h 3.01 and Ara h 3.02 (the former Ara h 4) belong to the cupin superfamily. The conglutins Ara h 2, Ara h 6 and Ara h 7, and the non-specific lipid transfer protein Ara h 9 belong to the prolamin superfamily. Ara h 5 (profilin) and Ara h 8 (Bet v 1-homologous protein) cause class II food allergies and are associated with inhalation allergy to pollen via the sequential and/or conformational similarity of molecules. Two peanut oleosins are listed as Ara h 10 and Ara h 11 and two defensins as Ara h 12 and Ara h 13 by the WHO/IUIS Allergen Nomenclature Subcommittee. The effect of the above-specified allergens has to be considered in the context of their matrix, which is influenced by processing factors and the individual's immune system.</p>","PeriodicalId":86023,"journal":{"name":"Chemical immunology and allergy","volume":"100 ","pages":"256-67"},"PeriodicalIF":0.0000,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000359916","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemical immunology and allergy","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000359916","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2014/5/22 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 4
Abstract
The earliest known evidence of peanut farming dates back 7,600 years. With a prevalence of roughly 1%, peanut allergy is a diagnostic and treatment challenge, but is also a very good model for studying all aspects of food allergy, including its molecular basis and pathomechanisms. Therefore, the very starting point for elucidating all these aspects is the identification of peanut allergens with subsequent clearing of their structure and their preparation as pure recombinant and/or natural allergens. This is the basis for in vitro diagnostic tests as well as the development of immunotherapeutic drugs. With regard to class I food allergy, peanut allergy affects by far the largest group of patients. In peanuts, 12 allergens have been identified and their molecular characteristics are described herein. Ara h 1, Ara h 3.01 and Ara h 3.02 (the former Ara h 4) belong to the cupin superfamily. The conglutins Ara h 2, Ara h 6 and Ara h 7, and the non-specific lipid transfer protein Ara h 9 belong to the prolamin superfamily. Ara h 5 (profilin) and Ara h 8 (Bet v 1-homologous protein) cause class II food allergies and are associated with inhalation allergy to pollen via the sequential and/or conformational similarity of molecules. Two peanut oleosins are listed as Ara h 10 and Ara h 11 and two defensins as Ara h 12 and Ara h 13 by the WHO/IUIS Allergen Nomenclature Subcommittee. The effect of the above-specified allergens has to be considered in the context of their matrix, which is influenced by processing factors and the individual's immune system.
已知最早的花生种植证据可以追溯到7600年前。花生过敏的患病率约为1%,是诊断和治疗方面的挑战,但也是研究食物过敏各方面的一个很好的模型,包括其分子基础和病理机制。因此,阐明所有这些方面的起点是花生过敏原的鉴定,随后清除其结构,并将其制备为纯重组和/或天然过敏原。这是体外诊断试验以及开发免疫治疗药物的基础。在I类食物过敏中,花生过敏影响的患者人数最多。在花生中,已鉴定出12种过敏原,本文描述了它们的分子特征。Ara h 1、Ara h 3.01和Ara h 3.02(前Ara h 4)属于cupin超族。粘连蛋白Ara h2、Ara h6和Ara h7以及非特异性脂质转移蛋白Ara h9属于蛋白超家族。arah5 (profilin)和arah8 (betv1同源蛋白)引起II类食物过敏,并通过分子的序列和/或构象相似性与花粉的吸入性过敏相关。世界卫生组织/美国过敏原命名小组委员会将两种花生油苷列为Ara h10和Ara h11,将两种防御素列为Ara h12和Ara h13。上述特定过敏原的作用必须在其基质的背景下考虑,基质受加工因素和个体免疫系统的影响。