Key result
Cadicivirus IRES recruits 43S complexes via a 40S/eIF3/IRES ternary complex bypassing direct eIF3-eIF4G interaction.
This structural biology study expands the mechanistic understanding of how divergent viral IRESs hijack the host translation apparatus.
Divergent IRES recruitment expands viral translation models; extends Type I classifications and leaves open antiviral targeting.
Cadicivirus (CDV) is unique amongst picornaviruses in having a dicistronic genome with internal ribosomal entry sites (IRESs) preceding both open reading frames. Here, we investigated initiation on the 5'-terminal IRES. We report that the 982-nt long 5'UTR comprises 12 domains (d1-d12), five of which (d8-d12, nts 341-950) constitute a divergent Type I IRES. It comprises central elements (the apex of d10, d11 and the following polypyrimidine tract) that are homologous to corresponding elements in canonical Type 1 IRESs, and non-canonical flanking domains (d8, d9 and d12). In vitro reconstitution revealed that as with canonical Type I IRESs, 48S complex formation requires eukaryotic initiation factors (eIFs) 1, 1A, 2, 3, 4A, 4B and 4G, and the poly(C) binding protein 2 (PCBP2), and starts with specific binding of eIF4G/eIF4A to d11. However, in contrast to canonical Type I IRESs, subsequent recruitment of 43S ribosomal complexes does not require direct interaction of their eIF3 constituent with the IRES-bound eIF4G. On the other hand, the CDV IRES forms a 40S/eIF3/IRES ternary complex, with multiple points of contact. These additional interactions with translational components could potentially stimulate recruitment of the 43S complex and alleviate the necessity for direct eIF4G/eIF3 interaction.
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Asnani et al. (2016) studied In vitro model of Cadicivirus translation initiation. In vitro translation factor manipulation and mutagenesis vs. Canonical Type I IRES (PV) or Wild-type CDV mRNA was evaluated on Translation initiation complex formation and structural mapping. The Cadicivirus IRES forms a 40S/eIF3/IRES ternary complex, revealing that unlike canonical Type I IRESs, recruitment of 43S complexes does not require direct interaction between eIF3 and IRES-bound eIF4G.
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