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Genetic Modification Removes an Immunodominant Allergen from Soybean

机译:基因修饰可从大豆中去除免疫敏原

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摘要

AbstractThe increasing use of soybean (Glycine max) products in processed foods poses a potential threat to soybean-sensitive food-allergic individuals. In vitro assays on soybean seed proteins with sera from soybean-sensitive individuals have immunoglobulin E reactivity to abundant storage proteins and a few less-abundant seed proteins. One of these low abundance proteins, Gly m Bd 30 K, also referred to as P34, is in fact a major (i.e. immunodominant) soybean allergen. Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine in the conserved catalytic cysteine position found in all other cysteine proteases. Transgene-induced gene silencing was used to prevent the accumulation of Gly m Bd 30 K protein in soybean seeds. The Gly m Bd 30 K-silenced plants and their seeds lacked any compositional, developmental, structural, or ultrastructural phenotypic differences when compared with control plants. Proteomic analysis of extracts from transgenic seed detected the suppression of Gly m Bd 30 K-related peptides but no other significant changes in polypeptide pattern. The lack of a collateral alteration of any other seed protein in the Gly m Bd 30 K-silenced seeds supports the presumption that the protein does not have a role in seed protein processing and maturation. These data provide evidence for substantial equivalence of composition of transgenic and non-transgenic seed eliminating one of the dominant allergens of soybean seeds.
机译:摘要大豆(Glycine max)产品在加工食品中的使用日益增加,对大豆敏感的食物过敏者构成了潜在威胁。用大豆敏感个体的血清对大豆种子蛋白进行的体外测定具有对大量贮藏蛋白和一些不那么丰富的种子蛋白的免疫球蛋白E反应性。这些低丰度蛋白质之一Gly m Bd 30 K,也称为P34,实际上是主要的(即免疫显性)大豆过敏原。尽管是木瓜蛋白酶超家族的成员,但Gly m Bd 30 K在所有其他半胱氨酸蛋白酶中均处于保守的催化半胱氨酸位置中具有甘氨酸。使用转基因诱导的基因沉默来防止Gly m Bd 30 K蛋白在大豆种子中的积累。与对照植物相比,Gly m Bd 30 K沉默的植物及其种子没有任何成分,发育,结构或超微结构表型差异。从转基因种子中提取的蛋白质组学分析检测到Gly m Bd 30 K相关肽的抑制,但多肽模式没有其他显着变化。 Gly m Bd 30 K沉默的种子中没有任何其他种子蛋白质的附带改变,支持这种蛋白质在种子蛋白质加工和成熟中不起作用的推测。这些数据提供了消除大豆种子的主要变应原之一的转基因和非转基因种子组成的实质等效的证据。

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