Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/90105
標題: In Vitro assembly of Bamboo mosaic virus chimeric coat protein into virus-like particles
體外組裝融合口蹄疫抗原胜肽之竹嵌紋病毒外鞘蛋白為類病毒顆粒之研究
作者: 謝旻諺
Min-Yen Hsieh
關鍵字: 類病毒顆粒
竹嵌紋病毒
次單位疫苗
口蹄疫
virus like particles(VLPs)
bamboo mosaic virus(BaMV)
subunit vaccine
foot-and-mouth disease(FMDV)
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摘要: 口蹄疫(Foot-and-mouth disease, FMD)是一種急性高度傳染性疾病,主要感染偶蹄類動物,其病徵為口、足等部位皮膚出現水泡,造成部分動物死亡,其影響畜牧產業之發展甚鉅,長期以來亦造成世界各地嚴重的經濟損失。目前市面上的口蹄疫疫苗為去活化病毒疫苗,但由於去活化過程中會有去活不完全之風險,故開發安全、有效及便宜的口蹄疫次單位疫苗是刻不容緩。由過去研究得知,口蹄疫病毒鞘蛋白VP1為病毒主要的抗原決定位,乃受病毒感染時與生物體內免疫細胞結合之部位,並能引發生物體產生免疫反應。大腸桿菌是目前使用最廣泛的表現蛋白質系統之一,具有生長快速、操作容易、產量高及低成本的優點。先前以Escherichia coli表現wild type Bamboo mosaic virus (BaMV) coat protein,純化後透析至10 mM MES緩衝溶液中,發現可以形成長度約500 nm大小之類病毒顆粒。本實驗中,選擇以E. coli為表現系統表達N端35個胺基酸缺失的竹嵌紋病毒外鞘蛋白,並在其N端融合兩段口蹄疫病毒VP1128-164之抗原決定基,分別為97及Manisa亞型抗原,命名為BVP1 97 Nd35mCP及BVP1 Manisa Nd35mCP。經低溫誘導表現發現融合蛋白為水溶性,並分別用Phenyl、DEAE、S200 column純化,觀察在不同種類的緩衝溶液、濃度、pH值、離子強度及溫度的條件下能否自我組裝形成缺少核酸之類病毒顆粒(VLPs),利用電子顯微鏡的觀察可以發現許多的類病毒顆粒,與從植物純化而來之VP1 Nd35mCP的絲狀病毒相比,VP1 97 mCP及VP1 Manisa mCP皆形成長度較短的桿狀類病毒顆粒,其平均大小約為100 nm~200 nm左右。此類病毒顆粒是否可作為一個安全性高、免疫效果強之次單位疫苗,進而取代傳統型口蹄疫疫苗,使豬隻免於口蹄疫病毒的威脅,仍需在未來進一步測試。
Foot-and-mouth disease virus (FMDV) is the causative agent of the acute and highly contagious foot and mouth disease (FMD). The symptoms are blisters on the skin of foot and mouth. FMD affects the developing of livestock industry significantly and causes the economic loss around the world. Conventional FMD vaccines are based on the chemically inactivated virus, which induce neutralizing antibodies, control disease and protect from FMD infection. However, the disadvantage of incompletely inactivated vaccine would contain live viral residues causing outbreak of disease. Hence, developing a safe, valid and inexpensive FMD subunit vaccine is urgent. FMDV VP1 is the major epitope, which can be recognized by immune system and elicit the immunogenic response while infected with virus. Escherichia coli is one of the most extensive protein expression system for its advantages of fast growth, easily manipulated, high protein yields and low cost. In the previous study, we found that purified wild type Bamboo mosaic virus (BaMV) coat protein (CP) from E. coli could self-assembled into virus-like particles (VLPs) in 10 mM 2-(N-morpholino) ethanesulfonic acid buffer (MES buffer, pH 6.0). The VLPs are about 500nm in length. In this study, we generated pET expression plasmids designated as pBVP1 97 Nd35mCP and pBVP1 Manisa Nd35mCP by replacing 35 amino acids of BaMV CP at N-terminal with 37 amino acids of VP1 epitopes of FMDV 97 or Manisa subtype. The recombinant fusion proteins expressed in E. coli produced in high-yield and in a soluble form. The recombinant proteins were purified by Phenyl、DEAE、S200 column consecutively. In order to test whether in vitro expressed BVP1 could self-assemble into VLPs in the absence of BaMV genome, the recombinant proteins were incubated in different pH, ionic strength buffer conditions and in the different temperature. The TEM results revealed that BVP1 formed into VLPs. Compare to the filamentous VP1 Nd35mCP purified from plants, both VP1 97 mCP and VP1 Manisa mCP formed about 100 nm~200 nm rod-shaped VLP. The mentioning VLPs as a safe and enhanced immunogenic subunit vaccine to protect pigs from FMD will be tested in the future.
URI: http://hdl.handle.net/11455/90105
文章公開時間: 2017-07-01
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