Foot-and-mouth disease virus 2A oligopeptide mediated cleavage of an artificial polyprotein

Martin D. Ryan*, Jeff Drew

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

320 Citations (Scopus)


We describe the construction of a plasmid (pCAT2AGUS) encoding a polyprotein in which a 19 amino acid sequence spanning the 2A region of the foot-and-mouth disease virus (FMDV) polyprotein was inserted between the reporter genes chloramphenicol acetyl transferase (CAT) and β-glucuronidase (GUS) maintaining a single, long open reading frame. Analysis of translation reactions programmed by this construct showed that the inserted FMDV sequence functioned in a manner similar to that observed in FMDV polyprotein processing: the CAT2A-GUS polyprotein underwent a cotranslational, apparently autoproteolytic, cleavage yielding CAT-2A and GUS. Analysis of translation products derived from a series of constructs in which sequences were progressively deleted from the N-terminal region of the FMDV 2A insertion showed that cleavage required a minimum of 13 residues. The FMDV 2A sequence therefore provides the opportunity to engineer either whole proteins or domains such that they are cleaved apart cotranslationally with high efficiency.

Original languageEnglish
Pages (from-to)928-933
Number of pages6
JournalEMBO Journal
Issue number4
Publication statusPublished - 15 Feb 1994


  • Autoproteolytic
  • Cotranslational cleavage
  • Foot-and-mouth disease virus
  • Polyprotein


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