Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot-and-mouth disease virus 3C protease: Identification of the eIF4AI cleavage site

Wei Li, Natalie Ross-Smith, Christopher G. Proud, Graham J. Belsham

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)

Abstract

The translation initiation factor eIF4A is cleaved within mammalian cells infected by foot-and-mouth disease virus (FMDV). The FMDV 3C protease cleaves eIF4AI (between residues E143 and V144), but not the closely related eIF4AII. Modification of eIF4AI, to produce a sequence identical to eIF4AII around the cleavage site, blocked proteolysis. Alignment of mammalian eIF4AI onto the three-dimensional structure of yeast eIF4A located the scissile bond within an exposed, flexible portion of the molecule. The N- and C-terminal cleavage products of eIF4AI generated by FMDV 3C dissociate. Cleavage of eIF4AI by FMDV 3C is thus expected to inactivate it.

Original languageEnglish
Pages (from-to)1-5
Number of pages5
JournalFEBS Letters
Volume507
Issue number1
DOIs
Publication statusPublished or Issued - 19 Oct 2001
Externally publishedYes

Keywords

  • 3C protease
  • Foot-and-mouth disease virus
  • Picornavirus
  • Protein synthesis
  • Translation initiation factor eIF4A

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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