Kang Tae-Jin, Han So-Chon, Yang Moon-Sik, Jang Yong-Suk
Team of Research and Development, Jeonbuk Bioindustry Development Institute, Jeonju 561-360, South Korea.
Protein Expr Purif. 2006 Mar;46(1):16-22. doi: 10.1016/j.pep.2005.07.026. Epub 2005 Aug 19.
The pentameric B subunit of Escherichia coli heat-labile enterotoxin (LTB) can be used as an efficient mucosal carrier of either immunogenic or tolerogenic T-cell epitopes. Co-delivery of therapeutic proteins with carrier proteins could increase the effectiveness of the antigen. This paper reports the ability of transgenic tobacco plants to express a fusion protein consisting of the synthetic LTB and a synthetic neutralizing epitope of porcine epidemic diarrhea virus (PEDV), causing an enteric disease that is especially severe in piglets. Both components of the fusion proteins were detected in Western blot analysis, and binding assay confirmed that plant-synthesized pentameric LTB-PEDV fusion bound to the intestinal membrane GM1-ganglioside receptor. This suggested that the fusion protein retained both its native antigenicity and the ability to form pentamers.
大肠杆菌不耐热肠毒素（LTB）的五聚体B亚基可作为免疫原性或耐受性T细胞表位的有效黏膜载体。治疗性蛋白质与载体蛋白的共同递送可提高抗原的有效性。本文报道了转基因烟草植物表达由合成LTB和猪流行性腹泻病毒（PEDV）的合成中和表位组成的融合蛋白的能力，PEDV可引发一种对仔猪尤为严重的肠道疾病。在蛋白质免疫印迹分析中检测到了融合蛋白的两个组分，结合试验证实植物合成的五聚体LTB-PEDV融合蛋白与肠膜GM1神经节苷脂受体结合。这表明该融合蛋白既保留了其天然抗原性，又具备形成五聚体的能力。
