Abstract
De novo viral protein synthesis following entry into host cells is essential for viral replication. As a consequence, viruses have evolved mechanisms to engage the host translational machinery while at the same time avoiding or counteracting host defenses that act to repress translation. Mammalian orthoreoviruses are dsRNA-containing viruses whose mRNAs were used as models for early investigations into the mechanisms that underpin the recognition and engagement of eukaryotic mRNAs by host cell ribosomes. However, there remain many unanswered questions and paradoxes regarding translation of reoviral mRNAs in the context of infection. This review summarizes the current state of knowledge about reovirus translation, identifies key unanswered questions, and proposes possible pathways toward a better understanding of reovirus translation.
Highlights
Viruses must use the host translation machinery to synthesize viral proteins
Viral double-stranded RNA is a pathogen-associated molecular pattern (PAMP) that is recognized by host pattern-recognition receptors (PRRs), which activate downstream signaling pathways leading to interferon (IFN) production and induction of antiviral effectors [104]
It seems likely that translation of reovirus mRNAs is spatiotemporally regulated (Figure 1)
Summary
Viruses must use the host translation machinery to synthesize viral proteins. The s1 mRNA encodes two proteins: the attachment protein, σ1, and a second nonstructural protein called σ1s, which is synthesized from an alternative reading frame by “leaky scanning” and initiation on a downstream methionine [11,12,13,14,15]. It is believed that an N-terminally deleted form of μNS called μNSC is synthesized by alternative initiation at a downstream methionine. This has not been experimentally confirmed for mammalian orthoreoviruses. Our goals are to identify outstanding questions and to highlight the implications of recent findings regarding the compartmentalization of translation in reovirus-infected cells
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