Skip to content. | Skip to navigation

Personal tools

You are here: Home / Teams / RNA metabolism in immunity and infection (RMI2) - E. Ricci / Publications / Structural and functional diversity of viral IRESes.

Structural and functional diversity of viral IRESes.

Laurent Balvay, Ricardo Soto Rifo, Emiliano P Ricci, Didier Decimo, and Theophile Ohlmann (2009)

Biochim Biophys Acta, 1789(9-10):542-57.

Some 20 years ago, the study of picornaviral RNA translation led to the characterization of an alternative mechanism of initiation by direct ribosome binding to the 5' UTR. By using a bicistronic vector, it was shown that the 5' UTR of the poliovirus (PV) or the Encephalomyelitis virus (EMCV) had the abilityto bind the 43S preinitiation complex in a 5' and cap-independent manner. This is rendered possible by an RNA domain called IRES for Internal Ribosome Entry Site which enables efficient translation of an mRNA lacking a 5' cap structure. IRES elements have now been found in many different viral families where they often confer a selective advantage to allow ribosome recruitment under conditions where cap-dependent protein synthesis is severely repressed. In this review, we compare and contrast the structure and function of IRESes that are found within 4 distinct family of RNA positive stranded viruses which are the (i) Picornaviruses; (ii) Flaviviruses; (iii) Dicistroviruses; and (iv) Lentiviruses.

automatic medline import

Document Actions