A peptide/maltose-binding protein fusion protein used to replace the traditional antigen for immunological detection of deoxynivalenol in food and feed
A peptide/maltose-binding protein fusion protein used to replace the traditional antigen for immunological detection of deoxynivalenol in food and feed
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一种肽/麦芽糖结合蛋白融合蛋白，用于替代传统抗原用于食品和饲料中脱氧雪腐镰刀菌烯醇的免疫检测
DOI：
10.1016/j.foodchem.2018.06.096
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发表时间：
2018-12-01
期刊：
影响因子：
8.8
通讯作者：
Ren, Wenjie
中科院分区：
文献类型：
--
作者：
Xu, Yang;Yang, Hongwei;Ren, Wenjie
以脱氧雪腐镰刀菌烯醇（DON）单克隆抗体为靶分子，通过噬菌体展示技术获得DON表位克隆（D-8）。随后，通过将模拟表位肽与MBP融合，合成DON抗原模拟物（D-8-麦芽糖结合蛋白[MBP]）。建立了基于D-8-MBP的酶联免疫吸附试验（ELISA）和海胆样金纳米颗粒免疫层析检测玉米和小麦中DON的方法。D-8-MBP ELISA的半最大抑制浓度、检测下限和线性范围分别为57.98 +/- 0.97、9.83和11.32-286.77 ng/mL。D-8-MBP酶联免疫吸附试验的灵敏度比传统的用DON-牛血清白蛋白（BSA）的酶联免疫吸附试验提高了近2.5倍。胶体金免疫层析法检测D-8-MBP的检测阈值为25 ng/mL。因此，D-8-MBP可替代传统的DON-BSA抗原用于DON的免疫学检测，从而实现低成本、快速检测DON。
A deoxynivalenol (DON) epitope clone (D-8) was obtained by phage display technology using anti-DON monoclonal antibodies as a target molecule. Subsequently, a DON antigen mimic (D-8-maltose-binding protein [MBP]) was synthesized by fusing the mimic epitope peptide with MBP. An enzyme-linked immunosorbent assay (ELISA) and urchin-like gold nanoparticle immunochromatographic assay was developed based on D-8-MBP for detection of DON in maize and wheat. The half-maximal inhibitory concentration, lower detection limit, and linear range of the D-8-MBP ELISA were 57.98 +/- 0.97, 9.83, and 11.32-286.77 ng/mL, respectively. The sensitivity of the D-8-MBP ELISA was nearly 2.5 times higher than that of traditional ELISA using DON-bovine serum albumin (BSA). The detection threshold of the colloidal gold immunochromatographic assay for D-8-MBP was 25 ng/mL. Thus, D-8-MBP could be used to replace the traditional DON-BSA antigen for the immunological detection of DON, permitting low cost, rapid detection of DON.