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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of the major celery allergen Api g 1: Molecular analysis of cross-reactivity
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Crystal structure of the major celery allergen Api g 1: Molecular analysis of cross-reactivity

机译：主要芹菜过敏原Api g的晶体结构1：交叉反应的分子分析

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摘要

Many patients who have been sensitised to pollen, display allergic symptoms after ingestion of certain plant food such as fresh fruit, vegetables and nuts. The cause is the cross-reactivity between structurally very similar major plant allergens. In particular, allergy to celery is very frequently associated with birch and mugwort pollen sensitization, known as to the birch-mugwort-celery syndrome. The crystal structure of the major celery allergen Api g 1, a homologue of the major birch pollen allergen Bet v 1, has been determined to a resolution of 2.9 angstrom. The structure of Api g 1 is very similar to that of Bet v 1 with major differences occurring in the segment comprised of residues 23-45, preceding the well conserved glycine-rich P-loop, as well as in loops beta 3-beta 4 and beta 5-beta 6. In particular, Api g I lacks E45, which has been shown to be a crucial residue for antibody recognition in the crystal complex of Bet v I with the Fab fragment of a murine monoclonal IgG (BV16) antibody. The absence of E45 and the structural differences in the preceding segment suggest that this region of the Api g 1 surface is probably not responsible for the observed cross-reactivity with Bet v 1. A detailed analysis of the molecular surface in combination with sequence alignment revealed three conserved surface patches which may account for cross-reactivity with Bet v 1. Several residues of Bet v 1 which have been shown by mutagenesis studies to be involved in IgE recognition belong to these conserved surface regions. The structure of Api g I and the related epitope analysis provides a molecular basis for a better understanding of allergen cross-reactivity and may lead to the development of hypoallergens which would allow a safer immunotherapy. (c) 2005 Elsevier Ltd. All rights reserved.
机译：许多对花粉敏感的患者在摄入某些植物性食物（如新鲜水果，蔬菜和坚果）后会出现过敏症状。原因是结构上非常相似的主要植物过敏原之间的交叉反应性。特别是，对芹菜的过敏症经常与桦树和艾蒿花粉过敏有关，这被称为桦木-艾蒿芹菜综合征。主要芹菜过敏原Api g 1（主要桦树花粉过敏原Bet v 1的同系物）的晶体结构已确定为2.9埃的分辨率。 Api g 1的结构与Bet v 1的结构非常相似，主要区别在于富含保守性的富含甘氨酸的P环之前的残基23-45，以及beta 3-beta 4环尤其是Api g I和beta 5-beta6。E45缺乏E45，E45被证明是Bet v I与鼠单克隆IgG（BV16）抗体的Fab片段晶体复合物中抗体识别的关键残基。 E45的缺乏和前段的结构差异表明，Api g 1表面的该区域可能不负责与Bet v 1的观察到的交叉反应。对分子表面的详细分析以及序列比对显示三个保守的表面斑块可能解释了与Bet v 1的交叉反应性。诱变研究表明，参与IgE识别的Bet v 1的一些残基属于这些保守的表面区域。 Api g I的结构和相关的表位分析为更好地了解变应原交叉反应性提供了分子基础，并可能导致低变应原的发展，这将使免疫治疗更安全。 （c）2005 Elsevier Ltd.保留所有权利。

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