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)
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)
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DOI：
10.1016/j.toxicon.2012.05.011
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发表时间：
2012-10-01
期刊：
影响因子：
2.8
通讯作者：
Deslippe, Richard J.
中科院分区：
文献类型：
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作者：
Lockwood, Stephanie A.;HaghiPour-Peasley, Jilla;Deslippe, Richard J.
我们报告的两个低分子量的蛋白质，储存在毒液中的皇后红进口火蚁（红火蚁）。翻译的氨基酸序列鉴定了一个蛋白质与Sol i 2 w工作变应原具有74.8%的同源性，并且发现另一个蛋白质与Sol i 4.01w/4.02w工作变应原具有96/97%的同源性。使用pEXP 1-DEST载体在SHuffle（TM），17表达lysY大肠杆菌中表达Sol i 2和Sol i 4蜂王和工蜂蛋白。与我们以前的表达方法的μ g/ml量相反，蛋白质以显著的浓度表达，使得能够进一步研究这些蛋白质。Sol i 2 q蛋白与人IgE、从过敏性患者汇集的血清弱结合，而Sol i 2 w、Sol i 4.01w和Sol i 4 q蛋白强烈结合。尽管Sol i 2 w和Sol i 2 q蛋白具有74.8%的同一性，但蜂王蛋白的免疫反应性低于工蜂过敏原。这一发现与过敏性个体对蜂王比对工蜂毒液更不敏感是一致的。(c)2012爱思唯尔有限公司保留所有权利。
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 (TM), 17 Express lysY Escherichia coli. Proteins were expressed at significant concentrations, as opposed to the mu g/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. (c) 2012 Elsevier Ltd. All rights reserved.