Cross-reactivity studies of a new group 2 allergen from the dust mite Glycyphagus domesticus, Gly d 2, and group 2 allergens from Dermatophagoides pteronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae with recombinant allergens

Cross-reactivity studies of a new group 2 allergen from the dust mite Glycyphagus domesticus, Gly d 2, and group 2 allergens from Dermatophagoides pteronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae with recombinant allergens
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DOI:
10.1067/mai.2001.112264
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发表时间:
2001-03-01
影响因子:
14.2
通讯作者:
van Hage-Hamsten, M
van Hage-Hamsten, M
中科院分区:
医学1区
文献类型:
--
作者:
Gafvelin, G;Johansson, E;van Hage-Hamsten, M

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背景:尘螨是变态反应性疾病的重要诱因。2族过敏原被认为是几种螨类的主要过敏原,包括翼状螨、毁灭鳞螨和腐食螨。到目前为止,还没有在分子水平上从尘螨中鉴定出过敏原。目的:探讨家蝇G、L破坏者、腐尸T和翼龙D的2组过敏原间的交叉反应性。方法:克隆家蝇2组过敏原Gly d2,并以重组蛋白的形式进行表达。采用个体血清和血清库rast -阳性方法,研究Gly d2与其他3种2组过敏原Lep d2、Tyr p2和Der p2的交叉反应性。在免疫印迹实验中,用重组过敏原作为IgE结合抑制剂。在Der p2结构的基础上对Gly d2、Lep d2和Tyr p2进行了分子建模。结果:分离到两个编码Gly d2亚型的cdna,但本研究仅使用了Gly d2 2.02亚型,17例受试者中有16例对Gly d2有IgE。Gly d2与Lep d2的同源性为79%,与Tyr p2和Der p2的同源性分别为46%和41%。Gly - d2、Lep - d2和Tyr - p2之间存在广泛的交叉反应性,但这些过敏原与Der - p2之间的交叉反应性很小。根据Der p2的三级结构和Gly d2、Lep d2和Tyr p2的三维模型,差异主要存在于表面暴露残留物。结论:Gly d2序列与Lep d2序列具有较高的同源性。Gly d2、Lep d2和Tyr p2之间存在交叉反应,但这3种过敏原与Der p2之间存在有限的交叉反应。
Background: Dust mites are important inducers of allergic disease. Group 2 allergens are recognized as major allergens in several mite species, including Dermatophagoides pteroronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae. No allergens have thus far been characterized on the molecular level from the dust mite Glycyphagus domesticus.Objective: We sought to examine the cross-reactivity among group 2 allergens of G domesticus, L destructor, T putrescentiae, and D pteronyssinus.Methods: A group 2 allergen from G domesticus, Gly d 2, was cloned and expressed as a recombinant protein. Cross-reactivity between Gly d 2 and 3 other group 2 allergens, Lep d 2,Tyr p 2, and Der p 2, was studied by using individual sera and a serum pool RAST-positive to G domesticus, L destructor, T putrescentiae, and D pteronyssinus. Recombinant allergens were used as inhibitors of IgE binding in immunoblotting experiments. Molecular modeling on the basis of the Der p 2 structure was carried out for Gly d 2, Lep d 2, and Tyr p 2.Results: Two cDNAs encoding isoforms of Gly d 2 were isolated, but only the Gly d 2.02 isoform was used in this study Sixteen of 17 subjects had IgE to Gly d 2. The protein sequence of Gly d 2 revealed 79% identity to Lep d 2 and 46% and 41% identity to Tyr p 2 and Der p 2, respectively. Extensive crossreactivity was demonstrated among Gly d 2, Lep d 2, and Tyr p 2, but little cross-reactivity was found between these allergens and Der p 2. According to the tertiary structure of Der p 2 and 3-dimensional models of Gly d 2, Lep d 2, and Tyr p 2, differences reside mainly in surface-exposed residues.Conclusion: Gly d 2 showed high sequence homology to Lep d 2. Cross-reactivity was observed between Gly d 2, Lep d 2, and Tyr p 2, but only limited cross-reactivity was demonstrated between these 3 allergens and Der p 2.