Potyvirus terminal protein VPg, effector of host eukaryotic initiation factor eIF4E

Biochimie
R GrzelaJ Chroboczek

Abstract

Potyvirus RNA contains at the 5' end a covalently linked virus-encoded protein VPg, which is required for virus infectivity. This role has been attributed to VPg interaction with the eukaryotic translation initiation factor eIF4E, a cap-binding protein. We characterized the dissociation constants for the interaction of the potato virus Y VPg with different plant eIF4Es and its isoforms and mapped the eIF(iso)4E attachment region on VPg. VPg/eIF4E interaction results in the inhibition of cell-free protein synthesis, and we show that it stems from the liberation of the cap moiety from the complex with eIF4E. Since VPg does not attach the cap, it appears that VPg induces changes in the eIF4E structure, diminishing its affinity to the cap. We show here that the initiation complex scaffold protein eIF(iso)4G increases VPg interaction with eIF(iso)4E. These data together suggest similar cap and VPg interactions with eIF4E and characterize VPg as a novel eIF4E-binding protein, which inhibits host protein synthesis at a very early stage of the initiation complex formation through the inhibition of cap attachment to the initiation factor eIF4E.

References

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Citations

Dec 21, 2012·Molecular Plant-microbe Interactions : MPMI·Carlos A Contreras-ParedesTzvetanka D Dinkova
Jun 24, 2011·Journal of Virology·Katri EskelinKristiina Mäkinen
Dec 4, 2012·Viruses·Jiri SochorRene Kizek
Mar 1, 2007·Molecular Plant Pathology·Andrew J MauleMargaret I Boulton
Apr 12, 2014·The Journal of General Virology·K I IvanovK Mäkinen
Oct 5, 2007·Methods in Enzymology·Robert E RhoadsRosemary Jagus
Feb 28, 2013·International Journal of Molecular Sciences·Sira Echevarría-ZomeñoM Mar Castellano
Nov 1, 2007·The Journal of Biological Chemistry·Renata GrzelaJadwiga Chroboczek
Nov 13, 2019·Proceedings of the National Academy of Sciences of the United States of America·Luciana Coutinho de OliveiraKatherine L B Borden

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