Calicivirus translation initiation requires an interaction between VPg and eIF4E

  • Goodfellow I
  • Chaudhry Y
  • Gioldasi I
 et al. 
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Unlike other positive-stranded RNA viruses that use either a 5'-cap structure or an internal ribosome entry site to direct translation of their messenger RNA, calicivirus translation is dependent on the presence of a protein covalently linked to the 5' end of the viral genome (VPg). We have shown a direct interaction of the calicivirus VPg with the cap-binding protein eIF 4 E. This interaction is required for calicivirus mRNA translation, as sequestration of eIF 4 E by 4 E-BP 1 inhibits translation. Functional analysis has shown that VPg does not interfere with the interaction between eIF 4 E and the cap structure or 4 E-BP 1, suggesting that VPg binds to eIF 4 E at a different site from both cap and 4 E-BP 1. This work lends support to the idea that calicivirus VPg acts as a novel 'cap substitute' during initiation of translation on virus mRNA.

Author-supplied keywords

  • Calicivirus
  • Translation
  • VPg
  • elF4E

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  • Alessandro NatoniNational University of Ireland, Galway

  • Ian Goodfellow

  • Yasmin Chaudhry

  • Ioanna Gioldasi

  • Andreas Gerondopoulos

  • Louisette Labrie

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