| First Author | Goodfellow I | Year | 2005 |
| Journal | EMBO Rep | Volume | 6 |
| Issue | 10 | Pages | 968-72 |
| PubMed ID | 16142217 | Mgi Jnum | J:101704 |
| Mgi Id | MGI:3604839 | Doi | 10.1038/sj.embor.7400510 |
| Citation | Goodfellow I, et al. (2005) Calicivirus translation initiation requires an interaction between VPg and eIF 4 E. EMBO Rep 6(10):968-72 |
| abstractText | 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. |
