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Published on April 11, 2008; 10.1104/pp.108.117481

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Received February 8, 2008
Accepted April 1, 2008

TMV movement protein interacts with GFP-tagged microtubule endbinding protein 1 (EB1)

Katrin Brandner , Adrian Sambade , Emmanuel Boutant , Pascal Didier , Yves Mely , Christophe Ritzenthaler , and Manfred Heinlein *

Institut de Biologie Moleculaire des Plantes, laboratoire propre du CNRS (UPR 2357) conventionne avec l'Universite Louis Pasteur (Strasbourg 1), 12 rue du General Zimmer, 67084 Strasbourg CEDEX, France; Institut Gilbert Laustriat, UMR CNRS 7034, Faculte de Pharmacie, Universite Louis Pasteur, 74 route du Rhin, 67401 Illkirch, France

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

The targeting of the movement protein (MP) of Tobacco mosaic virus (TMV) to plasmodesmata (PD) involves the actin/ER network and does not require an intact microtubule cytoskeleton. Nevertheless, the ability of MP to facilitate the cell-to-cell spread of infection is tightly correlated with interactions of the protein with microtubules, indicating that the microtubule system is involved in the transport of viral RNA. While the MP acts like a microtubule-associated protein able to stabilize microtubules during late infection stages, the protein was also shown to cause the inactivation of the centrosome upon expression in mammalian cells, thus suggesting that MP may interact with factors involved in microtubule attachment, nucleation, or polymerization. To further investigate the interactions of MP with the microtubule system in planta, we expressed the MP in the presence of GFP-fused microtubule end-binding protein EB1a of Arabidopsis (AtEB1a:GFP). The two proteins co-localize and interact in vivo as well as in vitro, and exhibit mutual functional interference. These findings suggest that MP interacts with EB1 and that this interaction may play a role in the associations of MP with the microtubule system during infection.




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