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Published on November 21, 2008; 10.1104/pp.108.131755

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Received October 27, 2008
Accepted November 19, 2008

The Cauliflower mosaic virus protein P6 forms motile inclusions that traffic along actin microfilaments and stabilize microtubules

Phillip A. Harries , Karuppaiah Palanichelvam , Weichang Yu , James E. Schoelz *, and Richard S. Nelson

Plant Biology Division, The Samuel Roberts Noble Foundation, 2510 Sam Noble Parkway, Ardmore, OK 73401; Department of Plant Microbiology and Pathology, University of Missouri, Columbia, Missouri, 65211

* Corresponding author; email: schoelzj{at}missouri.edu.

The gene VI product (P6) of Cauliflower mosaic virus (CaMV) is a multifunctional protein known to be a major component of cytoplasmic inclusion bodies formed during CaMV infection. Although these inclusions are known to contain virions and are thought to be sites of translation from the CaMV 35S polycistronic RNA intermediate, the precise role of these bodies in the CaMV infection cycle remains unclear. Here we examine the functionality and intracellular location of a fusion between P6 and GFP (P6-GFP). We initially show that the ability of P6-GFP to transactivate translation is comparable to unmodified P6. Consequently, our work has direct application for the large body of literature in which P6 has been expressed ectopically and its functions characterized. We subsequently find that P6-GFP forms highly motile cytoplasmic inclusion bodies and reveal through fluorescence co-localization studies that these P6-GFP bodies associate with the actin/ER network as well as microtubules. We demonstrate that while P6-GFP inclusions traffic along microfilaments, those associated with microtubules appear stationary. Additionally, inhibitor studies reveal that the intracellular movement of P6-GFP inclusions is sensitive to the actin inhibitor, latrunculin B (LatB), and that LatB also inhibits the formation of local lesions by CaMV in Nicotiana edwardsonii leaves. The motility of P6 along microfilaments represents an entirely new property for this protein and these results imply a role for P6 in intracellular and cell-to-cell movement of CaMV.




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