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A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity

Mélanie Chenon1, Laurent Camborde, Soizic Cheminant

  • 1Laboratoire de Virologie Moléculaire, CNRS-Univ Paris Diderot, Institut Jacques Monod, Cell Biology Department, UMR 7592, Paris, France.

The EMBO Journal
|November 26, 2011
PubMed

Insights

Turnip yellow mosaic virus (TYMV) replication protein 98K uses its deubiquitylating enzyme (DUB) activity to stabilize viral RNA-dependent RNA polymerase (RdRp), enhancing viral infectivity in plant cells.

Area of Science:

  • Plant virology
  • Molecular biology
  • Ubiquitin-proteasome system (UPS)

Background:

  • Selective protein degradation via the UPS is crucial for cellular processes, including host-pathogen interactions.
  • Turnip yellow mosaic virus (TYMV) RNA-dependent RNA polymerase (RdRp) is degraded by the UPS in infected cells, impacting viral infectivity.

Purpose of the Study:

  • To investigate how TYMV counteracts the degradation of its RdRp.
  • To characterize the deubiquitylating enzyme (DUB) activity of the TYMV 98K replication protein.

Main Methods:

  • In vitro assays using recombinant proteinase domain of TYMV 98K.
  • In vivo deubiquitylation assays in plant cells.
  • Analysis of viral infectivity.

Main Results:

  • The TYMV 98K replication protein possesses a functional ovarian tumour (OTU)-like deubiquitylating enzyme (DUB) domain.
  • TYMV 98K mediates in vivo deubiquitylation and stabilization of its binding partner, TYMV RdRp.
  • This DUB activity of 98K contributes to viral infectivity in plant cells.

Conclusions:

  • Viral DUB activity is essential for stabilizing viral RdRp.
  • TYMV 98K directly deubiquitylates and stabilizes viral RdRp, enhancing infectivity.
  • This highlights the intricate interplay between ubiquitylation, deubiquitylation, and viral protein interactions in controlling viral replication.

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