orthoreovirus (reovirus) requires the host translational apparatus to
synthesize viral proteins. However, reovirus must overcome the host stress
response mechanism that suppresses translation, a process known as host
translational shut-off (1). Upon viral infection, the double-stranded
RNA-dependent protein kinase (PKR) recognizes viral dsRNA molecules, leading to
PKR activation (2). Activated PKR phosphorylates translation initiation factor
eIF-2? on S51 preventing the recycling of this factor, which is required for
ongoing translation, subsequently resulting in general inhibition of
translation (Fig.1). The mechanisms
allowing reovirus to replicate when host translation in inhibited remain


we found that nonstructural protein ?1s is required for reovirus optimal
replication and viral protein synthesis in SV-40 immortalized endothelial cells
(SVECs). However, the mechanism by which ?1s promotes reovirus protein
synthesis is not defined. We hypothesize that ?1s enables reovirus to escape
host global translational shut-off. Our current work is focused on mechanisms
by which ?1s facilitates protein synthesis in the midst of the host cell stressed

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