Mapping of Functional Domains in Eukaryotic Protein Synthesis Initiation Factor 4G (eIF4G) with Picornaviral Proteases
Population
Eukaryotic initiation factor 4G (eIF4G) and its interaction with eIF4A, eIF4E, and eIF3
Design
Preclinical
Authors
Discussion
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Member takes
Implication
May inform mechanisms of picornavirus myocarditis; leaves open whether eIF4G cleavage affects cardiac translation or outcomes.
Structured PICO
P
Population
Eukaryotic initiation factor 4G (eIF4G) and its interaction with eIF4A, eIF4E, and eIF3
I
Intervention
Proteolytic cleavage by Rhinovirus 2A protease and foot-and-mouth-disease virus L protease
O
Outcome
Mapping of functional domains of eIF4G (eIF4E, eIF4A, and eIF3 binding sites)
Picornaviral proteases cleave eIF4G into distinct domains, separating the cap-binding function from the ribosome-attachment and helicase-directing functions, which facilitates cap-independent translation.
Cite This Study
Lamphear et al. (1995) studied this question.