Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein
Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein
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DOI：
10.1104/pp.108.133827
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发表时间：
2009-04-01
期刊：
影响因子：
7.4
通讯作者：
Heinlein, Manfred
中科院分区：
文献类型：
--
作者：
Hofmann, Christina;Niehl, Annette;Heinlein, Manfred
烟草花叶病毒（TMV）的运动蛋白（MP）所需的病毒RNA的细胞间传播与内质网（ER），以及在感染过程中与细胞骨架相互作用。尽管MP与ER和微管的关系已被深入研究，但对肌动蛋白作用的研究却相当缺乏。我们证明，烟草本氏植物的肌动蛋白结合结构域2的拟南芥（拟南芥）fimbinding（AtFIM 1）融合绿色荧光蛋白（ABD 2：GFP）的转基因表现出动态ABD 2：GFP标记的肌动蛋白细胞骨架和肌球蛋白依赖的高尔基体运输。这些植物也支持TMV的运动。与此相反，肌球蛋白依赖的高尔基体运输和TMV运动时，ABD2：GFP瞬时表达的主要抑制。抑制作用是通过ABD 2：GFP与肌动蛋白丝的结合介导的，因为TMV运动在用latrunculin B破坏ABD 2：GFP标记的肌动蛋白网络后恢复。在我们的处理条件下，Latrunculin B在野生型植物或ABD 2：GFP转基因植物中对TMV感染的传播没有显着影响。我们没有观察到任何结合的MP沿着长度的肌动蛋白丝。总的来说，这些观察结果表明，TMV的运动并不需要一个完整的肌动球蛋白系统。然而，肌动蛋白结合蛋白似乎有潜力发挥控制TMV运动通过抑制肌球蛋白相关蛋白运输沿着ER膜。
The tobacco mosaic virus (TMV) movement protein (MP) required for the cell-to-cell spread of viral RNA interacts with the endoplasmic reticulum (ER) as well as with the cytoskeleton during infection. Whereas associations of MP with ER and microtubules have been intensely investigated, research on the role of actin has been rather scarce. We demonstrate that Nicotiana benthamiana plants transgenic for the actin-binding domain 2 of Arabidopsis (Arabidopsis thaliana) fimbrin (AtFIM1) fused to green fluorescent protein (ABD2:GFP) exhibit a dynamic ABD2: GFP-labeled actin cytoskeleton and myosin-dependent Golgi trafficking. These plants also support the movement of TMV. In contrast, both myosin-dependent Golgi trafficking and TMV movement are dominantly inhibited when ABD2: GFP is expressed transiently. Inhibition is mediated through binding of ABD2: GFP to actin filaments, since TMV movement is restored upon disruption of the ABD2: GFP-labeled actin network with latrunculin B. Latrunculin B shows no significant effect on the spread of TMV infection in either wild-type plants or ABD2: GFP transgenic plants under our treatment conditions. We did not observe any binding of MP along the length of actin filaments. Collectively, these observations demonstrate that TMV movement does not require an intact actomyosin system. Nevertheless, actin-binding proteins appear to have the potential to exert control over TMV movement through the inhibition of myosin-associated protein trafficking along the ER membrane.