The movement protein encoded by gene 3 of rice transitory yellowing virus is associated with virus particles
The movement protein encoded by gene 3 of rice transitory yellowing virus is associated with virus particles
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DOI：
10.1099/vir.0.044420-0
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发表时间：
2012-10-01
影响因子：
3.8
通讯作者：
Sasaya, Takahide
中科院分区：
文献类型：
--
作者：
Hiraguri, Akihiro;Hibino, Hiroyuki;Sasaya, Takahide
水稻暂时黄化病毒（RTYV）等几种侵染植物的弹状病毒基因组中的基因3被认为编码一种细胞间运动蛋白（MP）。使用运动缺陷型番茄花叶病毒和RTYV的P3蛋白（由基因3编码）的反式互补实验促进了突变病毒的细胞间运输。在瞬时表达实验与绿色荧光蛋白融合的P3蛋白在本氏烟草的表皮叶细胞，P3蛋白与细胞核和胞间连丝。用抗大肠杆菌表达的His（6）标记的P3蛋白的抗血清对RTYV感染的水稻植株的薄切片进行免疫金标记研究，结果表明P3蛋白位于细胞壁和病毒颗粒上。用抗E.将表达的P3蛋白与RTYV纯品进行免疫反应，在RTYV纯品中检测到P3蛋白，而RTYV纯品的抗血清与E.大肠杆菌表达的P3蛋白。RTYV感染的水稻叶片的粗汁液免疫金标记后，P3蛋白，以及N蛋白，检测到的核糖核衣壳的核心，出现从部分破坏的病毒颗粒。这些结果提供了证据表明，RTYV的P3蛋白，其功能作为病毒MP，是一种病毒的结构蛋白，似乎与病毒颗粒的核糖核衣壳核心。
Gene 3 in the genomes of several plant-infecting rhabdoviruses, including rice transitory yellowing virus (RTYV), has been postulated to encode a cell-to-cell movement protein (MP). Trans-complementation experiments using a movement-defective tomato mosaic virus and the P3 protein of RTYV, encoded by gene 3, facilitated intercellular transport of the mutant virus. In transient-expression experiments with the GFP-fused P3 protein in epidermal leaf cells of Nicotiana benthamiana, the P3 protein was associated with the nucleus and plasmodesmata. Immunogold-labelling studies of thin sections of RTYV-infected rice plants using an antiserum against Escherichia coli-expressed His(6)-tagged P3 protein indicated that the P3 protein was located in cell walls and on virus particles. In Western blots using antisera against E. coli-expressed P3 protein and purified RTYV, the P3 protein was detected in purified RTYV, whilst antiserum against purified RTYV reacted with the E. coli-expressed P3 protein. After immunogold labelling of crude sap from RTYV-infected rice leaves, the P3 protein, as well as the N protein, was detected on the ribonucleocapsid core that emerged from partially disrupted virus particles. These results provide evidence that the P3 protein of RTYV, which functions as a viral MP, is a viral structural protein and seems to be associated with the ribonucleocapsid core of virus particles.