Production of interleukin-12 as a self-processing 2A polypeptide

Paul J. Chaplin*, Evelyn B. Camon, Barnardo Villarreal-Ramos, Micheal Flint, Martin D. Ryan, Robert A. Collins

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

39 Citations (SciVal)


Interleukin-12 (IL.12) is a heterodimeric cytokine composed of two disulfide-linked subunits (p40 and p35) encoded by separate genes. We used the apparent autocleavage property of a 2A peptide from the foot-and-mouth disease virus (FMDV) to express bovine (Bo) IL-12 as a self-processing polypeptide (p402Ap35). We demonstrate that 2A will mediate the cleavage of p402Ap35 into two separate subunits in a manner similar to that observed during the processing of the FMDV polypeptide. Furthermore, this 2A polypeptide encoded a functional heterodimer, which elicited activities associated with IL-12 in other species. We propose that this strategy of self-processing polypeptides may be used in many applications where the coordinated and stoichiometric expression of complex proteins is required.

Original languageEnglish
Pages (from-to)235-241
Number of pages7
JournalJournal of Interferon and Cytokine Research
Issue number3
Publication statusPublished - 19 Apr 1999


  • Animals
  • COS Cells
  • Cattle
  • Cells, Cultured
  • Genetic Vectors
  • Humans
  • Interleukin-12/biosynthesis
  • Protein Processing, Post-Translational
  • Viral Proteins/metabolism


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