Structural and functional diversity of viral IRESes |
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Authors: | Laurent Balvay Ricardo Soto Rifo Emiliano P Ricci Didier Decimo Théophile Ohlmann |
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Institution: | 1. Apoptosis Research Centre, Children''s Hospital of Eastern Ontario Research Institute, 401 Smyth Road, Ottawa K1H 8L1, Canada;2. Department of Biochemistry, Microbiology and Immunology, University of Ottawa, 451 Smyth Road, Ottawa K1H 8M5, Canada;3. Department of Pediatrics, University of Ottawa, 451 Smyth Road, Ottawa K1H 8M5, Canada |
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Abstract: | 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 ability to 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. |
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