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Journal of Virology, September 2006, p. 8329-8344, Vol. 80, No. 17
0022-538X/06/$08.00+0     doi:10.1128/JVI.00540-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Tobacco Mosaic Virus Movement Protein Functions as a Structural Microtubule-Associated Protein

Jamie Ashby,^2,3, Emmanuel Boutant,^1, Mark Seemanpillai,^1, Adrian Sambade,¹ Christophe Ritzenthaler,¹ and Manfred Heinlein^1,2,3*

Institut de Biologie Moléculaire des Plantes, 12 Rue du Général Zimmer, 67084 Strasbourg, France,¹ Botanisches Institut der Universität Basel, Hebelstrasse 1, 4056 Basel, Switzerland,² Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland³

Received 15 March 2006/ Accepted 4 June 2006

The cell-to-cell spread of Tobacco mosaic virus infection depends on virus-encoded movement protein (MP), which is believed to form a ribonucleoprotein complex with viral RNA (vRNA) and to participate in the intercellular spread of infectious particles through plasmodesmata. Previous studies in our laboratory have provided evidence that the vRNA movement process is correlated with the ability of the MP to interact with microtubules, although the exact role of this interaction during infection is not known. Here, we have used a variety of in vivo and in vitro assays to determine that the MP functions as a genuine microtubule-associated protein that binds microtubules directly and modulates microtubule stability. We demonstrate that, unlike MP in whole-cell extract, microtubule-associated MP is not ubiquitinated, which strongly argues against the hypothesis that microtubules target the MP for degradation. In addition, we found that MP interferes with kinesin motor activity in vitro, suggesting that microtubule-associated MP may interfere with kinesin-driven transport processes during infection.

Contributed equally to this work.

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