Key result
A novel protein-RNA binding assay demonstrated that translation initiation factors eIF4G, eIF4A, and eIF4B bind to the 3' domain of the FMDV IRES, correlating with loss of translational capacity.
Population
In vitro rabbit reticulocyte lysate and in vitro-transcribed foot-and-mouth disease virus RNA transcripts
Comparison
Depletion of IRES-binding proteins using… vs Undepleted lysate or lysate depleted with…
Design
Preclinical
Authors
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Hypothesis-generating for IRES-targeted antivirals; leaves open validation in mammalian models before any clinical relevance.
A novel functional assay demonstrated that translation initiation factors eIF4G, eIF4A, and eIF4B bind to the 3' domain of the FMDV IRES, which is essential for its translation initiation capacity.
STASSINOPOULOS et al. (2001) studied Foot-and-mouth disease virus (FMDV) translation. Protein-RNA binding assay using immobilized FMDV IRES transcripts vs. Antisense IRES transcript or beads alone was evaluated on Depletion of translation initiation factors and loss of translational capacity. A novel protein-RNA binding assay demonstrated that translation initiation factors eIF4G, eIF4A, and eIF4B bind to the 3' domain of the FMDV IRES, correlating with loss of translational capacity.
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