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Chemical shift assignment of the viral protein genome-linked (VPg) from potato virus Y

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Abstract

The dysregulation of translation contributes to many pathogenic conditions in humans. Discovering new translational mechanisms is important to understanding the diversity of this process and its potential mechanisms. Such mechanisms can be initially observed in viruses. With this in mind, we studied the viral protein genome-linked VPg factor from the largest genus of plant viruses. Studies in plants show that VPg binds to the eukaryotic translation initiation factor eIF4E for translation of viral RNAs. VPg contains no known eIF4E binding motifs and no sequence homology to any known proteins. Thus, as a first step in understanding the structural basis of this interaction, we carried out NMR assignments of the VPg from the potato virus Y potyvirus protein.

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Acknowledgements

800 MHz NMR data were acquired at QANUC and 600 MHz NMR data at IRIC which were both supported in part by CFI. This work was supported by the following grants to KLBB: RO1 NIH 98571; RO1 NIH80728 and KLBB holds the Canada Research Chair in Molecular Biology of the Cell Nucleus.

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Authors and Affiliations

  1. Department of Pathology and Cell Biology, Institute of Research in Immunology and Cancer (IRIC), Université de Montréal, Pavilion Marcelle-Coutu, Chemin Polytechnique, Montreal, QC, Canada

    Luciana Coutinho de Oliveira, Laurent Volpon, Michael J. Osborne & Katherine L. B. Borden

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  1. Luciana Coutinho de Oliveira
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  2. Laurent Volpon
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  3. Michael J. Osborne
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  4. Katherine L. B. Borden
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Correspondence to Katherine L. B. Borden.

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Coutinho de Oliveira, L., Volpon, L., Osborne, M.J. et al. Chemical shift assignment of the viral protein genome-linked (VPg) from potato virus Y. Biomol NMR Assign 13, 9–13 (2019). https://doi.org/10.1007/s12104-018-9842-3

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  • DOI: https://doi.org/10.1007/s12104-018-9842-3

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