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鉴定、表达及免疫反应的红火蚁毒液蛋白 Sol i 2 和 Sol i 4,红火蚁 Solenopsis invicta Buren(膜翅目:蚁科)。

Identification, expression, and immuno-reactivity of Sol i 2 & Sol i 4 venom proteins of queen red imported fire ants, Solenopsis invicta Buren (Hymenoptera: Formicidae).

机构信息

Department of Biological Sciences, Texas Tech University, Lubbock, TX 79409-3131, USA.

出版信息

Toxicon. 2012 Oct;60(5):752-9. doi: 10.1016/j.toxicon.2012.05.011. Epub 2012 Jun 5.

Abstract

We report on two low-molecular weight proteins that are stored in the venom of queen red imported fire ants (Solenopsis invicta). Translated amino acid sequences identified one protein to have 74.8% identity with the Sol i 2w worker allergen, and the other protein was found to have 96/97% identity with Sol i 4.01w/4.02w worker allergens. Both Sol i 2 and Sol i 4 queen and worker proteins were expressed using pEXP1-DEST vector in SHuffle™ T7 Express lysY Escherichia coli. Proteins were expressed at significant concentrations, as opposed to the μg/ml amounts by our previous expression methods, enabling further study of these proteins. Sol i 2q protein bound weakly to human IgE, sera pooled from allergic patients, whereas Sol i 2w, Sol i 4.01w, and Sol i 4q proteins bound strongly. Despite Sol i 2w and Sol i 2q proteins having 74.8% identity, the queen protein is less immuno-reactive than the worker allergen. This finding is consistent with allergic individuals being less sensitive to queen than worker venom.

摘要

我们报告了储存在 queen red 进口火蚁(Solenopsis invicta)毒液中的两种低分子量蛋白质。翻译的氨基酸序列鉴定出一种蛋白质与 Sol i 2w 工蚁变应原具有 74.8%的同一性,另一种蛋白质与 Sol i 4.01w/4.02w 工蚁变应原具有 96/97%的同一性。使用 pEXP1-DEST 载体在 SHuffle™ T7 Express lysY Escherichia coli 中表达了 Sol i 2 和 Sol i 4 女王和工蚁蛋白。与我们之前的表达方法相比,这些蛋白质以显著浓度表达,而不是以μg/ml 数量表达,从而能够进一步研究这些蛋白质。Sol i 2q 蛋白与人类 IgE 结合较弱,与来自过敏患者的血清混合,而 Sol i 2w、Sol i 4.01w 和 Sol i 4q 蛋白结合较强。尽管 Sol i 2w 和 Sol i 2q 蛋白具有 74.8%的同一性,但女王蛋白的免疫反应性不如工蚁变应原强。这一发现与过敏个体对女王毒液的敏感性低于工蚁毒液一致。

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