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J. Biol. Chem., Vol. 278, Issue 26, 23753-23761, June 27, 2003

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Structural Characterization of HC-Pro, a Plant Virus Multifunctional Protein^*

Célia Plisson  , Martin Drucker  ¶, Stéphane Blanc ¶ ||, Sylvie German-Retana **, Olivier Le Gall **, Daniel Thomas  and Patrick Bron  

From the Université Rennes I, Unité Mixte de Recherche 6026 CNRS, Campus de Beaulieu, Rennes 35042, ^¶Station de Recherches de Pathologie Comparée Unité Mixte de Recherche 5087 Institut National de la Recherche Agronomique-CNRS-Université Montpellier II, Saint-Christol-lez-Alès 30380, and ^**Institut National de la Recherche Agronomique, Virologie, Institut de Biologie Végétale Moléculaire, BP 81, Villenave d'Ornon Cedex 33883, France

The helper component proteinase (HC-Pro) is a key protein encoded by plant viruses of the genus Potyvirus. HC-Pro is involved in different steps of the viral cycle, aphid transmission, replication, and virus cell-to-cell and systemic movement and is a suppressor of post-transcriptional gene silencing. Structural knowledge of HC-Pro is required to better understand its multiple functions. To this aim, we purified His-tagged wild-type HC-Pro and a N-terminal deletion mutant (HC-Pro) from plants infected with recombinant potyviruses. Biochemical analysis of the recombinant proteins confirmed that HC-Pro is a dimer in solution, that the N terminus is not essential for self-interaction, and that a large C-terminal domain is highly resistant to proteolysis. Two-dimensional crystals of the recombinant proteins were successfully grown on Ni²⁺-chelating lipid monolayers. Comparison of projection maps of negatively stained crystals revealed that HC-Pro is composed of two domains separated by a flexible constriction. Cryo-electron crystallography of HC-Pro allowed us to calculate a projection map at 9-Å resolution. Our data from electron microscopy, biochemical analysis, and secondary structure predictions lead us to suggest a model for structure/function relationships in the HC-Pro protein.

Received for publication, March 12, 2003 , and in revised form, April 1, 2003.

^* The work was supported in part by a grant from the Ministère de l'Enseignement Supérieur et de la Recherche (to C. P.). 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.

Contributed equally to this work.

^|| To whom correspondence may be addressed. Tel.: 33-0-4-66-78-37-15; Fax: 33-0-4-66-52-46-99; E-mail: blanc{at}ensam.inra.fr.

To whom correspondence may be addressed. Tel.: 33-0-2-23-23-69-82; Fax: 33-0-2-23-23-50-48; E-mail: patrick.bron{at}univ-rennes1.fr.

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