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Calicivirus translation initiation requires an interaction between VPg and eIF4E
Author(s) -
Goodfellow Ian,
Chaudhry Yasmin,
Gioldasi Ioanna,
Gerondopoulos Andreas,
Natoni Alessandro,
Labrie Louisette,
Laliberté JeanFrançois,
Roberts Lisa
Publication year - 2005
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400510
Subject(s) - calicivirus , eif4e , eukaryotic translation , translation (biology) , internal ribosome entry site , biology , feline calicivirus , messenger rna , ribosome , rna , initiation factor , protein biosynthesis , computational biology , genetics , microbiology and biotechnology , virus , gene
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.