Skip to main content
SLU publication database (SLUpub)

Research article2013Peer reviewedOpen access

Ribosomal Protein P0 Promotes Potato Virus A Infection and Functions in Viral Translation Together with VPg and eIF(iso)4E

Hafren, Anders; Eskelin, Katri; Makinen, Kristiina

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.

Published in

Journal of Virology
2013, Volume: 87, number: 8, pages: 4302-4312 Publisher: AMER SOC MICROBIOLOGY

    UKÄ Subject classification

    Cell Biology

    Publication identifier

    DOI: https://doi.org/10.1128/JVI.03198-12

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/87539