Key result
Tomato ringspot virus proteinase (Pro) interacts with eukaryotic translation initiation factor eIF(iso)4E in vitro, and this complex formation is inhibited by a cap analogue.
Hypothesis-generating for cap analogue antivirals; leaves open in vivo relevance during plant infection.
Eukaryotic initiation factor eIF(iso)4E binds to the cap structure of mRNAs leading to assembly of the translation complex. This factor also interacts with the potyvirus VPg and this interaction has been correlated with virus infectivity. In this study, we show an interaction between eIF(iso)4E and the proteinase (Pro) of a nepovirus (Tomato ringspot virus; ToRSV) in vitro. The ToRSV VPg did not interact with eIF(iso)4E although its presence on the VPg-Pro precursor increased the binding affinity of Pro for the initiation factor. A major determinant of the interaction was mapped to the first 93 residues of Pro. Formation of the complex was inhibited by addition of m(7)GTP (a cap analogue), suggesting that Pro-containing molecules compete with cellular mRNAs for eIF(iso)4E binding. The possible implications of this interaction for translation and/or replication of the virus genome are discussed.
No takes yet. Share an insight, caveat, or question.
Léonard et al. (2002) studied this question. Tomato ringspot virus proteinase (Pro) was evaluated on Interaction between eIF(iso)4E and ToRSV proteinase in vitro. Tomato ringspot virus proteinase (Pro) interacts with eukaryotic translation initiation factor eIF(iso)4E in vitro, and this complex formation is inhibited by a cap analogue.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: