Unique structure of murine interleukin-2 as deduced from cloned cDNAs

Nature. 1985;313(6001):402-4. doi: 10.1038/313402a0.


Interleukin-2 (IL-2) is a lymphokine originally described as a humoral factor required for the continued proliferation of activated T-cell clones. It also seems to be involved in the mitogenic response of thymocytes, in augmenting natural killer cell activity, in the generation of cytotoxic T cells and in the induction of other lymphokines such as gamma-interferon and a B-cell growth factor (BCGF-1). More recently, there has been evidence for the involvement of IL-2 per se in the stimulation of B-cell growth (ref. 10 and T. Kishimoto and J. Vilcek, personal communications). We have reported previously the cloning and expression of a human IL-2 complementary DNA. The cDNA encodes biologically active IL-2 which would consist of 153 amino acids, including a signal sequence. Because so much of the work on IL-2 has been done in the human and mouse, we sought to obtain cDNA encoding murine IL-2, and we now report the cloning, expression and sequence analysis of murine IL-2 cDNAs. The longest cDNA insert encodes a polypeptide of 169 amino acids, containing unique repeats of a CAG sequence which would encode 12 consecutive glutamine residues within the active IL-2 molecule.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA / analysis*
  • DNA Restriction Enzymes / metabolism
  • Interleukin-2 / analysis*
  • Interleukin-2 / genetics
  • Mice
  • Poly A / analysis
  • RNA / analysis
  • RNA, Messenger


  • Interleukin-2
  • RNA, Messenger
  • Poly A
  • RNA
  • DNA
  • DNA Restriction Enzymes

Associated data

  • GENBANK/K02797