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Molecular & Cellular Proteomics 5:2279-2297, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proteome Analysis of Plant-Virus Interactome

Comprehensive Data for Virus Multiplication Inside Their Hosts^*

Jean Paul Brizard^,, Christine Carapito^¶,||, François Delalande^¶,**, Alain Van Dorsselaer^¶ and Christophe Brugidou

From the Institut de Recherche pour le Développement (IRD), UMR 5096 (CNRS-IRD-Université Perpignan), 34394 Montpellier Cedex 5, France and ^¶ Laboratoire de Spectrométrie de Masse Bio-Organique, UMR CNRS/Université Louis Pasteur 7512, 67087 Strasbourg, France

Known host-parasite molecular interactions are widespread among parasite families, but these interactions have to be particularly large considering that viruses generally encode few proteins. Although some particular virus-host interactions are well described, no global study has yet shown multiple and simultaneous interactions in a host-parasite biological system. To prove that these multiple interactions occur in biological conditions, the complexes formed by a plant virus (rice yellow mottle virus) and the proteins of its natural host (rice) were extracted and purified from infected tissue sample. Remarkably mass spectrometry permitted the identification of a large number of proteins from the complexes that are involved in different functions not encoded by the virus but probably essential for its biological life cycle. This recruiting of proteins was strongly confirmed by the repetition of experiments using different pairs of virus-host and the use of high salt concentration to extract the complexes. We mainly identified proteins involved in plant defense, metabolism, translation, and protein synthesis and some proteins involved in transport. This study demonstrates that viruses are able to recruit many proteins from their hosts to ensure their development. Among different pairs of virus-host, similar protein functions were identified suggesting a particular importance of these proteins for viruses. The identification of particular paralog proteins among multigenic families suggests the high specificity of the recruiting for some protein functions.

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