Key result
The HCV 3'UTR interacts with 40S ribosomal subunit proteins to stimulate translation in cis, likely by retaining ribosome complexes during termination to facilitate subsequent initiation.
The HCV 3'UTR retains ribosome complexes during translation termination to facilitate efficient initiation of subsequent rounds of viral translation.
This conserved 3'UTR-40S interaction extends HCV translation models; hypothesis-generating for ribosome-targeted antivirals.
The 3' untranslated region (3'UTR) of hepatitis C virus (HCV) messenger RNA stimulates viral translation by an undetermined mechanism. We identified a high affinity interaction, conserved among different HCV genotypes, between the HCV 3'UTR and the host ribosome. The 3'UTR interacts with 40S ribosomal subunit proteins residing primarily in a localized region on the 40S solvent-accessible surface near the messenger RNA entry and exit sites. This region partially overlaps with the site where the HCV internal ribosome entry site was found to bind, with the internal ribosome entry site-40S subunit interaction being dominant. Despite its ability to bind to 40S subunits independently, the HCV 3'UTR only stimulates translation in cis, without affecting the first round translation rate. These observations support a model in which the HCV 3'UTR retains ribosome complexes during translation termination to facilitate efficient initiation of subsequent rounds of translation.
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Bai et al. (2013) studied Hepatitis C virus infection. HCV 3'UTR was evaluated on Interaction with host ribosome and viral translation stimulation. The HCV 3'UTR interacts with 40S ribosomal subunit proteins to stimulate translation in cis, likely by retaining ribosome complexes during termination to facilitate subsequent initiation.
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