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EMBO Rep. 2005 Oct;6(10):968-72.

Calicivirus translation initiation requires an interaction between VPg and eIF 4 E.

Author information

1
School of Animal and Microbial Sciences, University of Reading, Whiteknights, Reading RG6 6AJ, UK. i.g.goodfellow@reading.ac.uk

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 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.

PMID:
16142217
PMCID:
PMC1369186
DOI:
10.1038/sj.embor.7400510
[Indexed for MEDLINE]
Free PMC Article

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