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Virus Genes

, Volume 55, Issue 2, pp 227–232 | Cite as

Recombinant HCV NS3 and NS5B enzymes exhibit multiple posttranslational modifications for potential regulation

  • Sergio Hernández
  • Ariel Díaz
  • Alejandra Loyola
  • Rodrigo A. VillanuevaEmail author
Article

Abstract

Posttranslational modification (PTM) of proteins is critical to modulate protein function and to improve the functional diversity of polypeptides. In this report, we have analyzed the PTM of both hepatitis C virus NS3 and NS5B enzyme proteins, upon their individual expression in insect cells under the baculovirus expression system. Using mass spectrometry, we present evidence that these recombinant proteins exhibit diverse covalent modifications on certain amino acid side chains, such as phosphorylation, ubiquitination, and acetylation. Although the functional implications of these PTM must be further addressed, these data may prove useful toward the understanding of the complex regulation of these key viral enzymes and to uncover novel potential targets for antiviral design.

Keywords

Hepatitis C virus HCV NS3 NS5B Posttranslational modification Protein regulation 

Notes

Acknowledgements

We thank Drs. Stephen Barnes and Landon Wilson from TMPL at UAB for the mass spectrometry analyses. We appreciate continuous support from Dr. Stanley M. Lemon, and Dr. Minkyung Yi. We thank Dr. Takaji Wakita for the transfer of pFGR-JFH1 plasmid utilized in our research. We thank all members of our laboratories for fruitful discussions while this work was carried out. This research has been supported by grants from CONICYT, Basal Project AFB 170004 (A.L.), FONDECYT 1160480 (A.L.), FONDECYT 1100200 (R.A.V.), and PCHA/Doctorado Nacional/2014-21140956 (S.H.).

Author’s contributions

RAV contributed to the study conception and design. SH and AD performed the experiments. RAV wrote the manuscript. SH, AD, RAV, and AL checked and revised it. RAV and AL contributed with funding. All authors read and approved the final manuscript.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with animals that required ethical approval.

Supplementary material

11262_2019_1638_MOESM1_ESM.pdf (1.8 mb)
Supplementary material 1 (PDF 1847 KB)

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Sergio Hernández
    • 1
    • 2
  • Ariel Díaz
    • 1
  • Alejandra Loyola
    • 1
  • Rodrigo A. Villanueva
    • 1
    Email author
  1. 1.Fundación Ciencia &, VidaÑuñoaChile
  2. 2.Architecture et Fonction des Macromolécules Biologiques, CNRS UMR7257, Department of Medicinal ChemistryAix Marseille UniversiteMarseilleFrance

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