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Mutual association of Broad bean wilt virus 2 VP37-derived tubules and plasmodesmata obtained from cytological observation

文献类型： 外文期刊

作者： Xie, Li 1 ; Shang, Weina 1 ; Liu, Chengke 1 ; Zhang, Qinfen 3 ; Sunter, Garry 4 ; Hong, Jian 1 ; Zhou, Xueping 1 ;

作者机构： 1.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou 310058, Zhejiang, Peoples R China

2.Zhejiang Acad Agr Sci, Hangzhou 310021, Zhejiang, Peoples R China

3.Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, Guangzhou 510275, Guangdong, Peoples R China

4.Univ Texas San Antonio, Dept Biol, San Antonio, TX 78249 USA

5.Zhejiang Univ, Ctr Anal & Measurement, Hangzhou 310029, Peoples R China

期刊名称：SCIENTIFIC REPORTS （ 影响因子：4.379； 五年影响因子：5.133 ）

ISSN： 2045-2322

年卷期： 2016 年 6 卷

页码：

收录情况： SCI

摘要： The movement protein VP37 of broad bean wilt virus 2 (BBWV 2) forms tubules in the plasmodesmata (PD) for the transport of virions between cells. This paper reports a mutual association between the BBWV 2 VP37-tubule complex and PD at the cytological level as determined by transmission electron microscopy. The generation of VP37-tubules within different PD leads to a different occurrence frequency as well as different morphology lines of virus-like particles. In addition, the frequency of VP37-tubules was different between PD found at different cellular interfaces, as well as between single-lined PD and branched PD. VP37-tubule generation also induced structural alterations of PD as well as modifications to the cell wall (CW) in the vicinity of the PD. A structural comparison using three-dimensional (3D) electron tomography (ET), determined that desmotubule structures found in the center of normal PD were absent in PD containing VP37-tubules. Using gold labeling, modification of the CW by callose deposition and cellulose reduction was observable on PD containing VP37-tubule. These cytological observations provide evidence of a mutual association of MP-derived tubules and PD in a natural host, improving our fundamental understanding of interactions between viral MP and PD that result in intercellular movement of virus particles.

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