Preparation, immunological characterization and polyclonal antibody development for recombinant epitope tandem derived from bovine -lactoglobulin

Preparation, immunological characterization and polyclonal antibody development for recombinant epitope tandem derived from bovine -lactoglobulin
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DOI:
10.1080/09540105.2016.1183596
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发表时间:
2016-11-01
影响因子:
3
通讯作者:
Chen, Hongbing
Chen, Hongbing
中科院分区:
农林科学3区
文献类型:
--
作者:
He, Shengfa;Li, Xin;Chen, Hongbing

文献摘要

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牛乳球蛋白(BLG)是牛奶中的主要过敏原之一。表位在食物过敏中起着关键作用,而大多数已开发的抗体并不能识别与IgE结合的表位。本研究根据表位疫苗方法学的原理,设计了BLG人IgE线性表位的串联序列(TBLG),并在大肠杆菌中表达,制备了多克隆抗体(pAB-tBLG)。重组tBLG蛋白保留了表位的抗原性和潜在的致敏性。PAB-tBLG能识别tBLG的全部IgE表位,具有较高的特异性,但与酪蛋白的交叉反应性较弱。我们的结论是,Pab-tBLG可以检测出BLG,并可能用于乳制品中的过敏原残留的鉴定。
Bovine -lactoglobulin (BLG) is one of the major allergens in cow's milk. Epitopes play a key role in food allergy, while most of the antibodies developed do not specifically recognize the IgE-binding epitopes. Here, a tandem derived from human IgE linear epitopes of BLG (tBLG) was designed according to the principles of epitope-based vaccine methodology, expressed in Escherichia coli, and a polyclonal antibody (pAb-tBLG) was developed. The recombinant tBLG protein preserved the antigenicity and potential allergenicity of epitopes. The pAb-tBLG recognized all the IgE epitopes of tBLG, and showed a high specificity, but it had weak cross-reactivity with caseins. We concluded that pAb-tBLG can detect of BLG and may be useful for identifying allergenic residues in dairy products.