Ribosomal protein P0 promotes Potato virus A infection and functions in viral translation together with VPg and eIF(iso)4E.

Abstract

We report here that the acidic ribosomal protein P0 is a component of the membrane-associated Potato virus A (PVA) ribonucleoprotein complex. As a constituent of the ribosomal stalk, P0 functions in translation. Although the ribosomal stalk proteins P0, P1, P2, and P3 are all important for PVA infection, P0 appears to have a distinct role from those of the other stalk proteins in infection. Our results indicate that P0 also regulates viral RNA functions as an extraribosomal protein. We reported previously that PVA RNA can be targeted by VPg to a specific gene expression pathway that protects the viral RNA from degradation and facilitates its translation. Here, we show that P0 is essential for this activity of VPg, similar to eIF4E/eIF(iso)4E. We also demonstrate that VPg, P0, and eIF(iso)4E synergistically enhance viral translation. Interestingly, the positive effects of VPg and P0 on viral translation were negatively correlated with the cell-to-cell spread of infection, suggesting that these processes may compete for viral RNA.

• Authors: Anders Hafrén, Katri Eskelin, Kristiina Mäkinen
• Journal: Journal of virology (J Virol) Vol. 87 Issue 8 Pg. 4302-12 (Apr 2013) ISSN: 1098-5514 [Electronic] United States
• PMID: 23365448 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Eukaryotic Initiation Factor-4E
• Ribosomal Proteins
• Viral Proteins
• ribosomal protein P0

Topics

• Eukaryotic Initiation Factor-4E (metabolism)
• Host-Pathogen Interactions
• Molecular Sequence Data
• Potyvirus (pathogenicity, physiology)
• Protein Biosynthesis
• Ribosomal Proteins (metabolism)
• Sequence Analysis, DNA
• Tobacco (virology)
• Viral Proteins (metabolism)