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EMBO reports 6, 10, 968–972 (2005)
doi:10.1038/sj.embor.7400510
Published online: 26 August 2005
Calicivirus translation initiation requires an interaction between VPg and eIF4E
Ian Goodfellow1, Yasmin Chaudhry1, Ioanna Gioldasi2, Andreas Gerondopoulos2, Alessandro Natoni2, Louisette Labrie3, Jean-François Laliberté3 & Lisa Roberts2
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1 School of Animal and Microbial Sciences, University of Reading, Whiteknights, Reading RG6 6AJ, UK
2 School of Biomedical and Molecular Sciences, University of Surrey, Guildford, Surrey GU2 7XH, UK
3 INRS-Institut Armand-Frappier, Laval, Québec H7V 1B7, Canada
To whom correspondence should be addressed
Ian Goodfellow Tel: +44 118 3788893; Fax:+44 1189 310180; E-mail: i.g.goodfellow@reading.ac.uk
Lisa Roberts Tel: +44 1483 686499; Fax:+44 1483 300374; E-mail: l.roberts@surrey.ac.uk
Received 9 June 2005; Accepted 15 July 2005; Published online 26 August 2005.
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Abstract
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 eIF4E. This interaction is required for calicivirus mRNA translation, as sequestration of eIF4E by 4E-BP1 inhibits translation. Functional analysis has shown that VPg does not interfere with the interaction between eIF4E and the cap structure or 4E-BP1, suggesting that VPg binds to eIF4E at a different site from both cap and 4E-BP1. This work lends support to the idea that calicivirus VPg acts as a novel 'cap substitute' during initiation of translation on virus mRNA.
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