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

BACKGROUND: VPgs 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 an...

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Autores principales: Hébrard, Eugénie, Bessin, Yannick, Michon, Thierry, Longhi, Sonia, Uversky, Vladimir N, Delalande, François, Van Dorsselaer, Alain, Romero, Pedro, Walter, Jocelyne, Declerk, Nathalie, Fargette, Denis
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2649914/
https://www.ncbi.nlm.nih.gov/pubmed/19220875
http://dx.doi.org/10.1186/1743-422X-6-23
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author Hébrard, Eugénie
Bessin, Yannick
Michon, Thierry
Longhi, Sonia
Uversky, Vladimir N
Delalande, François
Van Dorsselaer, Alain
Romero, Pedro
Walter, Jocelyne
Declerk, Nathalie
Fargette, Denis
author_facet Hébrard, Eugénie
Bessin, Yannick
Michon, Thierry
Longhi, Sonia
Uversky, Vladimir N
Delalande, François
Van Dorsselaer, Alain
Romero, Pedro
Walter, Jocelyne
Declerk, Nathalie
Fargette, Denis
author_sort Hébrard, Eugénie
collection PubMed
description BACKGROUND: VPgs 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. RESULTS: In 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. CONCLUSION: Based 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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spelling pubmed-26499142009-03-03 Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses Hébrard, Eugénie Bessin, Yannick Michon, Thierry Longhi, Sonia Uversky, Vladimir N Delalande, François Van Dorsselaer, Alain Romero, Pedro Walter, Jocelyne Declerk, Nathalie Fargette, Denis Virol J Research BACKGROUND: VPgs 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. RESULTS: In 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. CONCLUSION: Based 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. BioMed Central 2009-02-16 /pmc/articles/PMC2649914/ /pubmed/19220875 http://dx.doi.org/10.1186/1743-422X-6-23 Text en Copyright © 2009 Hébrard et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Hébrard, Eugénie
Bessin, Yannick
Michon, Thierry
Longhi, Sonia
Uversky, Vladimir N
Delalande, François
Van Dorsselaer, Alain
Romero, Pedro
Walter, Jocelyne
Declerk, Nathalie
Fargette, Denis
Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
title Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
title_full Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
title_fullStr Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
title_full_unstemmed Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
title_short Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
title_sort intrinsic disorder in viral proteins genome-linked: experimental and predictive analyses
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2649914/
https://www.ncbi.nlm.nih.gov/pubmed/19220875
http://dx.doi.org/10.1186/1743-422X-6-23
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