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Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses

  • Hébrard, Eugénie1
  • Bessin, Yannick2
  • Michon, Thierry3
  • Longhi, Sonia4
  • Uversky, Vladimir N5, 6
  • Delalande, François7
  • Van Dorsselaer, Alain7
  • Romero, Pedro5
  • Walter, Jocelyne3
  • Declerck, Nathalie2
  • Fargette, Denis1
  • 1 IRDCIRADUniversité de Montpellier II, UMR 1097 Résistance des Plantes aux Bio-agresseurs, 34394 Montpellier cedex 5, San Diego, BP, 64501, France , San Diego
  • 2 UMR 5048, Centre de Biochimie Structurale, 29 rue de Navacelles, Montpellier, 34090, France , Montpellier
  • 3 INRA, UMR1090 Génomique Diversité Pouvoir Pathogène, Université de Bordeaux 2, Villenave D'Ornon, F-33883, France , Villenave D'Ornon
  • 4 CNRS, Universités Aix-Marseille I et II, Campus de Luminy, UMR 6098 Architecture et Fonction des Macromolécules Biologiques, Marseille Cedex 09, 13288, France
  • 5 Center for Computational Biology and BioinformaticsIndiana University School of Medicine, , Department of Biochemistry and Molecular Biology, Indianapolis, IN, 46202, USA , Indianapolis
  • 6 Russian Academy of Sciences, Institute for Biological Instrumentation, Pushchino, Moscow Region, 142290, Russia , Pushchino
  • 7 ECPM, Laboratoire de Spectrométrie de Masse Bio-Organique, Strasbourg, France , Strasbourg
Published Article
Virology Journal
Springer (Biomed Central Ltd.)
Publication Date
Feb 16, 2009
DOI: 10.1186/1743-422X-6-23
Springer Nature


BackgroundVPgs are viral proteins linked to the 5' end of some viral genomes. Interactions between several VPgs and eukaryotic translation initiation factors eIF4Es are critical for plant infection. However, VPgs are not restricted to phytoviruses, being also involved in genome replication and protein translation of several animal viruses. To date, structural data are still limited to small picornaviral VPgs. Recently three phytoviral VPgs were shown to be natively unfolded proteins.ResultsIn this paper, we report the bacterial expression, purification and biochemical characterization of two phytoviral VPgs, namely the VPgs of Rice yellow mottle virus (RYMV, genus Sobemovirus) and Lettuce mosaic virus (LMV, genus Potyvirus). Using far-UV circular dichroism and size exclusion chromatography, we show that RYMV and LMV VPgs are predominantly or partly unstructured in solution, respectively. Using several disorder predictors, we show that both proteins are predicted to possess disordered regions. We next extend theses results to 14 VPgs representative of the viral diversity. Disordered regions were predicted in all VPg sequences whatever the genus and the family.ConclusionBased on these results, we propose that intrinsic disorder is a common feature of VPgs. The functional role of intrinsic disorder is discussed in light of the biological roles of VPgs.

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