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J. Biol. Chem., Vol. 283, Issue 1, 213-221, January 4, 2008

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Virulence Factor of Potato Virus Y, Genome-attached Terminal Protein VPg, Is a Highly Disordered Protein^*

Renata Grzela¹, Ewa Szolajska, Christine Ebel, Dominique Madern, Adrien Favier, Izabela Wojtal, Wlodzimierz Zagorski, and Jadwiga Chroboczek²

From the Institut de Biologie Structurale JP Ebel, 41 rue Jules Horowitz, CEA, CNRS, F-38027 Grenoble, France and the Institute of Biochemistry and Biophysics of Polish Academy of Sciences, 02106 Warszawa, Poland

Potato virus Y (PVY) is a common potyvirus of agricultural importance, belonging to the picornavirus superfamily of RNA plus-stranded viruses. A covalently linked virus-encoded protein VPg required for virus infectivity is situated at the 5' end of potyvirus RNA. VPg seems to be involved in multiple interactions, both with other viral products and host proteins. VPgs of potyviruses have no known homologs, and there is no atomic structure available. To understand the molecular basis of VPg multifunctionality, we have analyzed structural features of VPg from PVY using structure prediction programs, functional assays, and biochemical and biophysical analyses. Structure predictions suggest that VPg exists in a natively unfolded conformation. In contrast with ordered proteins, PVY VPg is not denatured by elevated temperatures, has sedimentation values incompatible with a compact globular form, and shows a CD spectrum of a highly disordered protein, and HET-HETSOFAST NMR analysis suggests the presence of large unstructured regions. Although VPg has a propensity to form dimers, no functional differences were seen between the monomer and dimer. These data strongly suggest that the VPg of PVY should be classified among intrinsically disordered proteins. Intrinsic disorder lies at the basis of VPg multifunctionality, which is necessary for virus survival in the host.

Received for publication, July 10, 2007 , and in revised form, October 30, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported in part by NATO Grant CLG 982385.

² To whom correspondence should be addressed: Institut de Biologie Structurale JP Ebel, CEA, CNRS, Université Joseph Fourier, 41 rue Jules Horowitz 38027 Grenoble, France. Tel.: 33-4-38-78-95-80; Fax: 33-4-38-78-54-94; E-mail: wisia{at}ibs.fr.

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				A. Hafren and K. Makinen Purification of viral genome-linked protein VPg from potato virus A-infected plants reveals several post-translationally modified forms of the protein J. Gen. Virol., June 1, 2008; 89(6): 1509 - 1518. [Abstract] [Full Text] [PDF]