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Abstract：
Food allergy to sunflower seed (SFS) protein is not frequent and only non-specific lipid transfert protein (nsLTP) Hel a 3 is officially recognized as a food allergen. Out of the eleven seed storage 2S-albumins (SESA) detected in SFS, only SFA-8 allergenicity has been investigated so far. The study aimed then to evaluate SFS protein allergenicity and particularly, to compare the sensitization potency of SESA in a mouse model.
The most abundant SESA and nsLTP were isolated from SFS through a combination of chromatographic methods. Purified proteins were then used to measure specific IgG1 and IgE responses in BALB/c mice orally sensitized to different SFS protein isolates. The study, thus, confirmed the allergenicity of SFA-8 and Hel a 3 but mice were also highly sensitized to other SESA such as SESA2-1 or SESA20-2. Furthermore, competitive inhibition of IgE-binding revealed that SFA-8 IgE-reactivity was due to cross-reactivity with other SESA. 11S-globulins were weakly immunogenic and were rapidly degraded in an in vitro model of gastroduodenal digestion. In contrast, Hel a 3, SESA2-1 and SFA-8 were more resistant to proteolysis and gastroduodenal digestion did not affect their IgE-reactivity.
SESA2-1 or SESA20-2 were more potent allergens than SFA-8 in this mouse model. Allergenicity of SESA must be now confirmed in SFS-allergic patients.
The most abundant SESA and nsLTP were isolated from SFS through a combination of chromatographic methods. Purified proteins were then used to measure specific IgG1 and IgE responses in BALB/c mice orally sensitized to different SFS protein isolates. The study, thus, confirmed the allergenicity of SFA-8 and Hel a 3 but mice were also highly sensitized to other SESA such as SESA2-1 or SESA20-2. Furthermore, competitive inhibition of IgE-binding revealed that SFA-8 IgE-reactivity was due to cross-reactivity with other SESA. 11S-globulins were weakly immunogenic and were rapidly degraded in an in vitro model of gastroduodenal digestion. In contrast, Hel a 3, SESA2-1 and SFA-8 were more resistant to proteolysis and gastroduodenal digestion did not affect their IgE-reactivity.
SESA2-1 or SESA20-2 were more potent allergens than SFA-8 in this mouse model. Allergenicity of SESA must be now confirmed in SFS-allergic patients.
摘要：
对葵花籽（SFS）蛋白的食物过敏并不常见，只有非特异性脂质转移蛋白（nsLTP）Hel一3被正式确认为食物过敏原。在SFS中检测到的11种种子储存2S-白蛋白(SESA)中，到目前为止，只有SFA-8过敏原被调查。该研究旨在评估SFS蛋白的致敏性，特别是，比较小鼠模型中SESA的致敏效能。
通过色谱方法的组合从SFS中分离出最丰富的SESA和nsLTP。然后将纯化的蛋白用于测量对不同SFS蛋白分离物口服致敏的BALB/c小鼠中的特异性IgG1和IgE应答。这项研究,因此，证实了SFA-8和Hel一3的变应原性，但小鼠对其他SESA如SESA2-1或SESA20-2也高度敏感。此外，IgE结合的竞争性抑制表明SFA-8IgE反应性归因于与其他SESA的交叉反应性。11S-球蛋白的免疫原性弱，在胃十二指肠消化的体外模型中迅速降解。相比之下,Hela3，SESA2-1和SFA-8对蛋白水解更具抗性，胃十二指肠消化不影响其IgE反应性。
在该小鼠模型中,SESA2-1或SESA20-2是比SFA-8更有效的变应原。现在必须在SFS过敏患者中确认SESA的致敏性。
通过色谱方法的组合从SFS中分离出最丰富的SESA和nsLTP。然后将纯化的蛋白用于测量对不同SFS蛋白分离物口服致敏的BALB/c小鼠中的特异性IgG1和IgE应答。这项研究,因此，证实了SFA-8和Hel一3的变应原性，但小鼠对其他SESA如SESA2-1或SESA20-2也高度敏感。此外，IgE结合的竞争性抑制表明SFA-8IgE反应性归因于与其他SESA的交叉反应性。11S-球蛋白的免疫原性弱，在胃十二指肠消化的体外模型中迅速降解。相比之下,Hela3，SESA2-1和SFA-8对蛋白水解更具抗性，胃十二指肠消化不影响其IgE反应性。
在该小鼠模型中,SESA2-1或SESA20-2是比SFA-8更有效的变应原。现在必须在SFS过敏患者中确认SESA的致敏性。
