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首页> 外文期刊>The Internet Journal of Asthma, Allergy and Immunology >CD4 T-Cell Cytokine Response to Mite Recombinant Tropomyosin in Mite, Snail and Shrimp Allergic Patients
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CD4 T-Cell Cytokine Response to Mite Recombinant Tropomyosin in Mite, Snail and Shrimp Allergic Patients

机译：CD4 T细胞细胞因子对螨，蜗牛和虾过敏患者螨重组体肌球蛋白的反应

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Allergies to snails and mites are definitely linked. Snail allergens have been already identified and there is no evidence of cross-reaction between snail and mite tropomyosin. This work is a preliminary study on immune cell function, evaluating possible tropomyosin-triggering in a snail-mite-shrimp cross-reaction. Peripheral blood mononuclear cells from 6 different phenotype patients in relation to snails, mites and crustaceans, were cultured with mite recombinant tropomyosin (rDer p 10), anti-CD28 and brefeldin A. Phytohemagglutinin mitogen was used as a positive control. CD4 T-cell response was evaluated towards CD69, IFN-γ, IL-2, IL-4, IL-5 and IL-13, in flow cytometry. rDer p 10 induced different cytokine expression in the six phenotypes. Allergen-specific IFN-γ stimulation was suggested by an increase in IFN-γ, IL-5, and IL-13 only in allergic to crustaceans, with a dose-dependent effect on IL-5 and IL-13. Tropomyosin is probably the main allergen responsible for the mite-shrimp cross-reactivity but may not play a major role in snail-mite-shrimp cross-reactions. This work was done in the Laboratory of Immunology from Hospital de S. Bernardo, Setúbal, Portugal. Introduction Snails, a very popular delicacy in several European countries, are also considered as one of the worst causes of food allergy. In fact, some people may develop severe episodes of asthma [1] after ingestion of snails and a connection with house-dust-mite allergy is firmly established [23456789101112131415]. Food allergens are frequently glycoproteins with a molecular weight (MW) from 15 to 50 kDa, with the immunogenic effect depending precisely on the MW, which may facilitate the contact and further absorption through the digestive mucosa. The number of epitopes present on the antigen molecule may also play an important role [16], possibly due to their immune triggering potential. Helix aspersa, Otala lactea and Theba pisana allergen repertoires were exposed by immunochemical methods, showing a close pattern between them. Cross-reactivity between Dermatophagoides pteronyssinus, H. aspersa and Pandalus borealis shrimp was also evaluated by RAST inhibition. D. pteronyssinus was shown to be a strong inhibitor of the H. aspersa RAST (72,6%) and even stronger inhibitor of the P. borealis RAST (91,9%) [15]. Despite 65 sequence identities and 79 similarities between H. aspersa and D. pteronyssinus tropomyosins [17], the 36-kDa protein from H. aspersa extract and the natural and recombinant purified tropomyosins were IgE-recognized by only 4 sera out of 22 from patients reporting snail reactivity [18]. Another study also reported a 37-kDa protein from H. aspersa extract, has being recognized by only 1 patient out of 21 with specific IgE to H. aspersa above class 2 [15]. Extending the previous study, further unpublished data has shown recognition of the 37-kDa protein by only 4 from 36 patients with specific IgE to H. aspersa above class 2.The two major allergens from H. aspersa (recognized by 13 and 18 out of 21 patients, respectively) presented MW 208 kDa, probably corresponding to the heavy chains of snails’ myosin [15]. In view of the presented results, it seemed rather improbable that tropomyosin could be the key culprit in the snail-mite cross-reactivity with allergy. Therefore, it was then important to identify what could happen at the cellular level, as the cytokine response pattern may differ from what is expected by simple observation of the sensitizing spectrum [19]. In fact, atopy was observed in association with allergen-specific T helper (Th) cells, with a Th2 pattern of response dominated by IL-4, IL-5, IL-9 and IL-13, while IL-10, TNF-α and IFN-γ were present both in atopics and non-atopics [20]. Mostly in atopics, bronchial hyper-responsiveness revealed to be strongly associated with eosinophilia and IL-5 synthesis in conjunction with IgE production [20].Food allergy is, in fact, a hypersensitive reaction to frequently harmless anti
机译：蜗牛和螨虫的过敏肯定是有联系的。蜗牛过敏原已经被鉴定出来，没有证据表明蜗牛和螨原肌球蛋白之间发生交叉反应。这项工作是对免疫细胞功能的初步研究，评估了蜗牛螨对虾交叉反应中可能引发的原肌球蛋白触发。用螨重组原肌球蛋白（rDer p 10），抗CD28和布雷菲德菌素A培养来自6种不同表型患者的与蜗牛，螨和甲壳类有关的外周血单个核细胞。将植物血凝素有丝分裂原作为阳性对照。在流式细胞术中评估了对CD69，IFN-γ，IL-2，IL-4，IL-5和IL-13的CD4 T细胞应答。 rDer p 10在六种表型中诱导不同的细胞因子表达。仅在对甲壳类动物过敏的情况下，IFN-γ，IL-5和IL-13的增加提示了过敏原特异性IFN-γ的刺激，并且对IL-5和IL-13具有剂量依赖性。 Tropomyosin可能是引起螨虾对虾交叉反应的主要过敏原，但可能在蜗牛-螨虾对虾的交叉反应中不起主要作用。这项工作是在葡萄牙塞图巴尔的S. Bernardo医院的免疫学实验室完成的。简介蜗牛，在几个欧洲国家中非常受欢迎的美食，也被认为是食物过敏的最严重原因之一。实际上，某些人在摄入蜗牛后可能会出现严重的哮喘发作[1]，并且已经确定与室内尘螨过敏有关[23456789101112131415]。食物过敏原通常是分子量（MW）为15至50 kDa的糖蛋白，其免疫原性作用准确地取决于MW，这可能有助于通过消化粘膜的接触和进一步吸收。存在于抗原分子上的表位的数量也可能起重要作用[16]，这可能是由于它们的免疫触发潜能。通过免疫化学方法暴露了螺旋黑曲霉，乳蛾和拟南芥变应原，它们之间显示出紧密的模式。还通过RAST抑制评估了Dermatophagoides pteronyssinus，H。aspersa和Pandalusboalis虾之间的交叉反应性。蕨类植物被证明是黑曲霉RAST的强抑制剂（72.6％），甚至是北极假单胞菌RAST的强抑制剂（91.9％）[15]。尽管曲霉菌和蕨类植物原核肌球蛋白之间有65个序列同一性和79个相似性[17]，但从22个患者中，只有4个血清可鉴定出曲霉菌提取物和天然及重组纯化的原肌球蛋白的36 kDa蛋白。报告蜗牛的反应性[18]。另一项研究还报道了从曲霉提取物中提取的一种37 kDa蛋白，在21名对2级以上曲霉有特异性IgE的患者中，只有1名被识别[15]。在先前研究的基础上，进一步的未发表数据显示，只有36名IgE特异性IgE患者中2例以上2类以上的人患有37 kDa蛋白。2。H. aspersa的主要变应原（分别被13和18识别）分别有21位患者的MW> 208 kDa，可能对应于蜗牛肌球蛋白的重链[15]。鉴于提出的结果，原肌球蛋白可能是蜗牛螨与过敏症交叉反应的关键元凶。因此，重要的是确定在细胞水平上可能发生的情况，因为细胞因子的反应方式可能与简单观察敏化光谱所期望的不同[19]。实际上，观察到特应性与过敏原特异性T辅助（Th）细胞相关，Th2反应模式以IL-4，IL-5，IL-9和IL-13为主，而IL-10，TNF-α α和IFN-＆＃947;都出现在特应性和非特应性[20]中。在过敏性疾病中，支气管高反应性与嗜酸性粒细胞增多，IL-5合成以及IgE产生密切相关[20]。事实上，食物过敏是对经常无害的抗过敏反应。

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