Bovine herpes virus gD protein produced in plants using a recombinant tobacco mosaic virus (TMV) vector possesses authentic antigenicity
Bovine herpes virus gD protein produced in plants using a recombinant tobacco mosaic virus (TMV) vector possesses authentic antigenicity
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DOI：
10.1016/s0264-410x(03)00495-x
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发表时间：
2003-10-01
期刊：
影响因子：
5.5
通讯作者：
Sadir, AM
中科院分区：
文献类型：
--
作者：
Filgueira, DMP;Zamorano, PI;Sadir, AM
基于烟草花叶病毒（TMV）的载体用于表达胞质形式的牛疱疹病毒1型（BHV-1）蛋白糖蛋白D（gDc）。在用来源于TMV-gDc重组病毒的RNA转录物接种后7天收获本氏烟草植物。具有预期电泳迁移率的重组gDc蛋白在接种的叶中积累至约20 μ g/g新鲜叶组织的浓度。油基疫苗与粗叶提取物一起配制以胃肠外免疫小鼠。单次注射后，动物对分离的gD和天然病毒颗粒产生持续和特异性应答。用相同的含gDc的提取物接种的牛产生了针对病毒gD和BHV-1颗粒的特异性体液和细胞免疫应答。最重要的是，用植物产生的gDc接种的动物在用毒性BHV-1攻击后显示出良好的保护水平。在这些动物中，病毒排泄急剧减少，达到与接种商业BHV-1疫苗的动物相当的水平。获得的gDc的阳性免疫学表征表明，在植物重组蛋白中保留了天然构象的重要部分。(C)2003 Elsevier Ltd.保留所有权利。
A tobacco mosaic virus (TMV)-based vector was utilized for expression of a cytosolic form of the bovine herpesvirus type 1 (BHV-1) protein glycoprotein D (gDc). Nicotiana benthamiana plants were harvested 7 days after inoculation with RNA transcripts derived from the TMV-gDc recombinant virus. Recombinant gDc protein of expected electrophoretic mobility accumulated in inoculated leaves to a concentration of about 20 mug/g of fresh leaf tissue. Oil-based vaccines were formulated with crude foliar extracts to immunize mice parentally. After a single injection, animals developed a sustained and specific response to both the isolated gD and native virus particles. Cattle vaccinated with the same gDc containing extracts developed specific humoral and cellular immune responses directed against both the viral gD and BHV-1 particles. Most importantly, animals vaccinated with the plant-produced gDc showed good levels of protection after challenge with the virulent BHV-1. Virus excretion was drastically reduced in these animals, reaching levels comparable to animals vaccinated with a commercial BHV-1 vaccine. The positive immunological characterization obtained for the gDc, indicated that an important part of the natural conformation was retained in the plant recombinant protein. (C) 2003 Elsevier Ltd. All rights reserved.