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First published online February 13, 2009; 10.1104/pp.108.133827

Plant Physiology 149:1810-1823 (2009)
© 2009 American Society of Plant Biologists

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PLANTS INTERACTING WITH OTHER ORGANISMS

Inhibition of Tobacco Mosaic Virus Movement by Expression of an Actin-Binding Protein1,[W],[OA]

Christina Hofmann, Annette Niehl, Adrian Sambade2, André Steinmetz and Manfred Heinlein*

Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 67084 Strasbourg cedex, France (C.H., A.N., A. Sambade, M.H.); and Laboratory of Plant Molecular Biology, CRP-Santé, L–1526 Luxembourg (A. Steinmetz)

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.


1 This work was supported by the Ministere de la Culture, de L'Enseignement Superieur et de la Recherche, Luxembourg (doctoral fellowship no. BFR04/068 to C.H.); by the Generalidad Valenciana, Spain (postdoctoral fellowship grant nos. CTBPDC/2204/015 and BPOSTDOC06/072 to A. Sambade); and by the Le Ministère Délégué à la Recherche et aux Nouvelles Technologies, France, and the Human Frontier Science Program Organization (grant nos. ACI BCMS187 and HFSP 22/2006, respectively, to M.H.).

2 Present address: Department of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, United Kingdom.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Manfred Heinlein (manfred.heinlein{at}ibmp-ulp.u-strasbg.fr).

[W] The online version of this article contains Web-only data.

[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.108.133827

* Corresponding author; e-mail manfred.heinlein{at}ibmp-ulp.u-strasbg.fr.

Received December 5, 2008; accepted February 9, 2009; published February 13, 2009.


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