Key result
The leader protein of Theiler's virus prevents stress granule assembly by blocking the activation of PKR, rendering the kinase unable to detect viral double-stranded RNA.
Population
Infected cells using Theiler's virus as a model
Design
In vitro laboratory study
Authors
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Suggests PKR blockade as viral evasion in animal models; leaves open relevance to human infections or therapies.
The study demonstrates a novel viral immune evasion mechanism where the TMEV leader protein prevents PKR activation by rendering it insensitive to double-stranded RNA.
Borghese et al. (2019) studied Theiler's murine encephalomyelitis virus (TMEV) infection. Theiler's virus Leader (L) protein vs. L-mutant viruses (LZn, LM60V) or mock infection was evaluated on PKR activation (phosphorylation) and stress granule assembly. The leader protein of Theiler's virus prevents stress granule assembly by blocking the activation of PKR, rendering the kinase unable to detect viral double-stranded RNA.
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