The Tobacco etch virus P3 protein forms mobile inclusions via the early secretory pathway and traffics along actin microfilaments

The Tobacco etch virus P3 protein forms mobile inclusions via the early secretory pathway and traffics along actin microfilaments
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DOI:
10.1016/j.virol.2009.11.015
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发表时间:
2010-02-05
期刊:
影响因子:
3.7
通讯作者:
Wang, Aiming
Wang, Aiming
中科院分区:
医学3区
文献类型:
--
作者:
Cui, Xiaoyan;Wei, Taiyun;Wang, Aiming

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植物多病毒编码两种膜蛋白,6K和P3。6K蛋白已被证明能诱导病毒复制囊泡。然而,P3的功能尚不清楚。本研究研究了烟草蚀刻病毒(TEV) P3蛋白在烟叶细胞中的亚细胞定位。TEV P3蛋白定位于内质网(ER)膜,并与高尔基体相关形成点状包涵体。早期分泌途径介导P3向高尔基体的转运。高尔基相关点状结构起源于内质网出口位点(ERES)。缺失分析确定了在高尔基体中保留P3所需的P3结构域。此外,发现P3点状结构沿着肌动蛋白丝运输,并与含有w的复制囊泡共定位。综上所述,这些数据支持了先前的建议,即P3可能在病毒移动和复制中发挥双重作用。爱思唯尔公司2009年版权所有版权所有。
Plant potyviruses encode two membrane proteins, 6K and P3. The 6K protein has been shown to induce virus replication vesicles. However, the function of P3 remains unclear. In this study, subcellular localization of the Tobacco etch virus (TEV) P3 protein was investigated in Nicotiana benthamiana leaf cells. The TEV P3 protein localized on the endoplasmic reticulum (ER) membrane and formed punctate inclusions in association with the Golgi apparatus. The trafficking of P3 to the Golgi was mediated by the early secretory pathway. The Golgi-associated punctate structures originated from the ER exit site (ERES). Deletion analyses identified P3 domains required for the retention of P3 at the Golgi. Moreover, the P3 punctate structure was found to traffic along the actin filaments and colocalize with the W-containing replication vesicles. Taken together, these data support previous suggestions that P3 may play dual roles in virus movement and replication. Crown Copyright (C) 2009 Published by Elsevier Inc. All rights reserved.