4EBP1 Is Dephosphorylated by Respiratory Syncytial Virus Infection

Intervirology. 2015;58(4):205-8. doi: 10.1159/000435774. Epub 2015 Aug 21.

Abstract

Respiratory syncytial virus (RSV) requires protein biosynthesis machinery to generate progeny. There is evidence that RSV might alter some translation components since stress granules are formed in their host cells. Consistent with these observations, we found that RSV induces dephosphorylation of 4EBP1 (eIF4E-binding protein), an important cellular translation factor. Our results show no correlation between the 4EBP1 dephosphorylation time and the decrease in the global rate of protein synthesis. Interestingly, treatment with rapamycin stimulates virus generation. The results suggest that RSV is a virus that still contains unknown mechanisms involved in the translation of their mRNAs through the alteration or modification of some translation factors, such as 4EBP1, possibly to favor its replicative cycle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Cell Cycle Proteins
  • Cell Line
  • Epithelial Cells / virology
  • Humans
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Biosynthesis*
  • RNA, Messenger / genetics
  • Respiratory Syncytial Virus, Human / physiology*
  • Sirolimus / adverse effects
  • Sirolimus / metabolism
  • Sirolimus / pharmacology
  • Virus Replication / drug effects

Substances

  • Adaptor Proteins, Signal Transducing
  • Cell Cycle Proteins
  • EIF4EBP1 protein, human
  • Phosphoproteins
  • RNA, Messenger
  • Sirolimus