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Rice Stripe Tenuivirus NSvc2 Glycoproteins Targeted to the Golgi Body by the N-Terminal Transmembrane Domain and Adjacent Cytosolic 24 Amino Acids via the COP I- and COP II-Dependent Secretion Pathway

文献类型： 外文期刊

作者： Yao, Min 1 ; Liu, Xiaofan 1 ; Li, Shuo 2 ; Xu, Yi 3 ; Zhou, Yijun 2 ; Zhou, Xueping 3 ; Tao, Xiaorong 1 ;

作者机构： 1.Nanjing Agr Univ, Dept Plant Pathol, Minist Educ, Key Lab Integrated Management Crop Dis & Pests, Nanjing, Jiangsu, Peoples R China

2.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing, Jiangsu, Peoples R China

3.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou 310003, Zhejiang, Peoples R China

4.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China

期刊名称：JOURNAL OF VIROLOGY （ 影响因子：5.103； 五年影响因子：5.078 ）

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收录情况： SCI

摘要： The NSvc2 glycoproteins encoded by Rice stripe tenuivirus (RSV) share many characteristics common to the glycoproteins found among Bunyaviridae. Within this viral family, glycoproteins targeting to the Golgi apparatus play a pivotal role in the maturation of the enveloped spherical particles. RSV particles, however, adopt a long filamentous morphology. Recently, RSV NSvc2 glycoproteins were shown to localize exclusively to the ER in Sf9 insect cells. Here, we demonstrate that the amino-terminal NSvc2 (NSvc2-N) targets to the Golgi apparatus in Nicotiana benthamiana cells, whereas the carboxyl-terminal NSvc2 (NSvc2-C) accumulates in the endoplasmic reticulum (ER). Upon coexpression, NSvc2-N redirects NSvc2-C from the ER to the Golgi bodies. The NSvc2 glycoproteins move together with the Golgi stacks along the ER/actin network. The targeting of the NSvc2 glycoproteins to the Golgi bodies was strictly dependent on functional anterograde traffic out of the ER to the Golgi bodies or on a retrograde transport route from the Golgi apparatus. The analysis of truncated and chimeric NSvc2 proteins demonstrates that the Golgi targeting signal comprises amino acids 269 to 315 of NSvc2-N, encompassing the transmembrane domain and 24 adjacent amino acids in the cytosolic tail. Our findings demonstrate for the first time that the glycoproteins from an un-enveloped Tenuivirus could target Golgi bodies in plant cells.

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