Wallowitz M L, Chen R J Y, Tzen J T C, Teuber S S
Department of Internal Medicine, Division of Rheumatology, Allergy and Clinical Immunology, School of Medicine, University of California, Davis, CA 95616, USA.
Clin Exp Allergy. 2007 Jun;37(6):929-38. doi: 10.1111/j.1365-2222.2007.02725.x.
Sesame allergy is increasingly being reported, and multi-sensitization to peanut and tree nuts has been described. The clinical relevance and cross-reactivity of many sesame proteins, such as Ses i 6, are unknown.
The aims of this study were to perform a preliminary examination of the cross-reactivity of Ses i 6 in vitro, examine the ability of Ses i 6 to activate basophils in a modified basophil activation test (mBAT), and assess whether such an assay may help to distinguish between potentially relevant and irrelevant IgE reactivity towards 11S globulin proteins.
Inhibition immunoblotting and chicken anti-rJug r 4 antibodies were used to determine the cross-reactivity of rSes i 6. Basophils from atopic donors were stripped of resident IgE before passive sensitization with food-allergic sera and challenged with protein extracts or recombinant protein. Basophil activation was measured using two activation markers, CD203c and CD63, via flow cytometry.
IgE immunoblotting showed cross-reactivity between rJug r 4 and rSes i 6 using sera from two human donors and chicken IgY. Additionally, rSes i 6 activated basophils passively sensitized with sesame-allergic sera. Cross-reactive serum from a sesame-allergic but walnut-tolerant donor was not able to activate basophils when challenged by walnut extract despite IgE reactivity to walnut determined by immunoblotting.
The sesame 11S globulin shows partial immunological cross-reactivity with walnut, and although it is classified as a minor allergen, activated basophils sensitized with serum from seven out of eleven sesame-allergic donors. Additionally, the mBAT may help distinguish between clinically relevant and irrelevant in vitro IgE cross-reactivity of seed storage proteins in nuts and seeds and thus warrants use in further studies.
芝麻过敏的报道日益增多,且已有对花生和坚果多重致敏的描述。许多芝麻蛋白(如Ses i 6)的临床相关性和交叉反应性尚不清楚。
本研究旨在对Ses i 6的体外交叉反应性进行初步检测,在改良嗜碱性粒细胞活化试验(mBAT)中检测Ses i 6激活嗜碱性粒细胞的能力,并评估该试验是否有助于区分针对11S球蛋白的潜在相关和无关IgE反应性。
采用抑制免疫印迹法和鸡抗rJug r 4抗体测定rSes i 6的交叉反应性。来自特应性供体的嗜碱性粒细胞在用食物过敏血清进行被动致敏前去除固有IgE,然后用蛋白提取物或重组蛋白进行激发。通过流式细胞术使用两种活化标记物CD203c和CD63测量嗜碱性粒细胞活化。
IgE免疫印迹显示,使用两名人类供体的血清和鸡IgY时,rJug r 4与rSes i 6之间存在交叉反应性。此外,rSes i 6激活了用芝麻过敏血清被动致敏的嗜碱性粒细胞。尽管通过免疫印迹确定对核桃有IgE反应性,但来自对芝麻过敏但对核桃耐受的供体的交叉反应性血清在用核桃提取物激发时无法激活嗜碱性粒细胞。
芝麻11S球蛋白与核桃显示出部分免疫交叉反应性,尽管它被归类为次要过敏原,但用11名芝麻过敏供体中7名的血清致敏的嗜碱性粒细胞被激活。此外,mBAT可能有助于区分坚果和种子中种子储存蛋白的临床相关和无关体外IgE交叉反应性,因此值得在进一步研究中使用。