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Journal of Virology, March 2004, p. 2301-2309, Vol. 78, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.5.2301-2309.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

A Cysteine-Rich Plant Protein Potentiates Potyvirus Movement through an Interaction with the Virus Genome-Linked Protein VPg

P. Dunoyer,1,2 C. Thomas,1 S. Harrison,1,3 F. Revers,1,4 and A. Maule1*

John Innes Centre, Norwich NR4 7UH,1 Syngenta, Jealott's Hill International Research Centre, Bracknell, Berks RG42 6EY, United Kingdom,3 Institut de Biologie Moleculaire des Plantes, 67084 Strasbourg Cedex,2 Virologie Végétale, IBVM-INRA, 33883 Villenave d'Ornon Cedex, France4

Received 17 July 2003/ Accepted 17 November 2003

We have identified a cellular factor that interacts with the virus genome-linked proteins (VPgs) of a diverse range of potyviruses. The factor, called Potyvirus VPg-interacting protein (PVIP), is a plant-specific protein with homologues in all the species examined, i.e., pea, Arabidopsis thaliana, and Nicotiana benthamiana. The sequence of PVIP does not identify a specific function, although the existence of a "PHD finger" domain may implicate the protein in transcriptional control through chromatin remodeling. Deletion analysis using the yeast two-hybrid system showed that the determinants of the interaction lay close to the N terminus of VPg; indeed, the N-terminal 16 amino acids were shown to be both necessary and sufficient for the interaction with at least one PVIP protein. From a sequence comparison of different potyvirus VPg proteins, a specific amino acid at position 12 was directly implicated in the interaction. This part of VPg is distinct from regions associated with other functional roles of VPg. Through mutation of Turnip mosaic virus (TuMV) at VPg position 12, we showed that the interaction with PVIP affected systemic symptoms in infected plants. This resulted from reduced cell-to-cell and systemic movement more than reduced virus replication, as visualized by comparing green fluorescent protein-tagged wild-type and mutant viruses. Furthermore, by using RNA interference of PVIP in Arabidopsis, we showed that reduced expression of PVIP genes reduced susceptibility to TuMV infection. We conclude that PVIP functions as an ancillary factor to support potyvirus movement in plants.

* Corresponding author. Mailing address: John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom. Phone: (44)1603 450266. Fax: (44)1603 450045. E-mail: andy.maule{at}bbsrc.ac.uk.

Journal of Virology, March 2004, p. 2301-2309, Vol. 78, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.5.2301-2309.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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