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First published online October 30, 2009; 10.1104/pp.109.147983

Plant Physiology 152:255-266 (2010)
© 2010 American Society of Plant Biologists

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PLANTS INTERACTING WITH OTHER ORGANISMS

A Host RNA Helicase-Like Protein, AtRH8, Interacts with the Potyviral Genome-Linked Protein, VPg, Associates with the Virus Accumulation Complex, and Is Essential for Infection1,[C],[W],[OA]

Tyng-Shyan Huang, Taiyun Wei, Jean-François Laliberté and Aiming Wang*

Agriculture and Agri-Food Canada, Southern Crop Protection and Food Research Centre, London, Ontario N5V 4T3, Canada (T.-S.H., T.W., A.W.); Department of Biology, University of Western Ontario, London, Ontario N6A 5B7, Canada (T.-S.H., T.W., A.W.); and Institut National de la Recherche Scientifique, Institut Armand-Frappier, Laval, Quebec H7V 1B7, Canada (J.-F.L.)

The viral genome-linked protein, VPg, of potyviruses is a multifunctional protein involved in viral genome translation and replication. Previous studies have shown that both eukaryotic translation initiation factor 4E (eIF4E) and eIF4G or their respective isoforms from the eIF4F complex, which modulates the initiation of protein translation, selectively interact with VPg and are required for potyvirus infection. Here, we report the identification of two DEAD-box RNA helicase-like proteins, PpDDXL and AtRH8 from peach (Prunus persica) and Arabidopsis (Arabidopsis thaliana), respectively, both interacting with VPg. We show that AtRH8 is dispensable for plant growth and development but necessary for potyvirus infection. In potyvirus-infected Nicotiana benthamiana leaf tissues, AtRH8 colocalizes with the chloroplast-bound virus accumulation vesicles, suggesting a possible role of AtRH8 in viral genome translation and replication. Deletion analyses of AtRH8 have identified the VPg-binding region. Comparison of this region and the corresponding region of PpDDXL suggests that they are highly conserved and share the same secondary structure. Moreover, overexpression of the VPg-binding region from either AtRH8 or PpDDXL suppresses potyvirus accumulation in infected N. benthamiana leaf tissues. Taken together, these data demonstrate that AtRH8, interacting with VPg, is a host factor required for the potyvirus infection process and that both AtRH8 and PpDDXL may be manipulated for the development of genetic resistance against potyvirus infections.


1 This work was supported by grants from the Natural Sciences and Engineering Research Council of Canada and Agriculture and Agri-Food Canada to A.W. and by scholarships (Ontario Graduate Scholarship and Ontario Graduate Scholarship in Science and Technology) to T.-S.H.

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: Aiming Wang (aiming.wang{at}agr.gc.ca).

[C] Some figures in this article are displayed in color online but in black and white in the print edition.

[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.109.147983

* Corresponding author; e-mail aiming.wang{at}agr.gc.ca.

Received September 23, 2009; accepted October 27, 2009; published October 30, 2009.




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M. J. Castello, J. L. Carrasco, and P. Vera
DNA-Binding Protein Phosphatase AtDBP1 Mediates Susceptibility to Two Potyviruses in Arabidopsis
Plant Physiology, August 1, 2010; 153(4): 1521 - 1525.
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