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Calicivirus translation initiation requires an interaction between VPg and eIF4E

Goodfellow, I., Chaudhry, Y., Gioldasi, I., Gerondopoulos, A., Natoni, A., Labrie, L., Laliberte, J. F. and Roberts, L. (2005) Calicivirus translation initiation requires an interaction between VPg and eIF4E. Embo Reports, 6 (10). pp. 968-972. ISSN 1469-221X

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To link to this item DOI: 10.1038/sj.embor.7400510

Abstract/Summary

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 50 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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10326
Uncontrolled Keywords:calicivirus, eIF4E, translation, VPg, YEAST 2-HYBRID SYSTEM, FELINE CALICIVIRUS, NONSTRUCTURAL POLYPROTEIN, REPLICATION COMPLEXES, MOSAIC-VIRUS, PROTEIN, POTYVIRUS, RNA, SUSCEPTIBILITY, CLEAVAGE

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