Monoclonal antibody defining a molecule possibly identical to the p75 subunit of interleukin 2 receptor

J Exp Med. 1989 Apr 1;169(4):1323-32. doi: 10.1084/jem.169.4.1323.

Abstract

A mouse hybridoma cell line, TU27, producing an mAb was established. TU27 mAb reacted with various human and Gibbon ape T cell lines bearing the IL-2R p75 (IL-2Rp75), but not with cell lines expressing only Tac antigen, IL-2Rp55, and numbers of its binding sites on cell surfaces were similar to those of high-affinity IL-2R. Radioimmunoprecipitation with TU27 mAb defined a molecule with a molecular mass of 75 kD on the surface of IL-2Rp75 bearing cells. TU27 mAb completely blocked IL-2 binding to IL-2Rp75 and to the high-affinity IL-2R but not to IL-2Rp55 composing the low-affinity IL-2R. The IL-2-dependent growth of a human T cell line, ILT-Mat, was significantly inhibited by TU27 mAb only at low concentrations of IL-2, and combination of TU27 mAb and H-31 mAb specific for IL-2Rp55 completely inhibited the cell growth even at high concentrations of IL-2. These data strongly suggest that TU27 mAb is specific for the human IL-2Rp75.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / immunology*
  • Antibody Affinity
  • Antibody Specificity
  • Antigen-Antibody Reactions
  • Cell Line
  • Humans
  • In Vitro Techniques
  • Lymphocyte Activation
  • Molecular Weight
  • Precipitin Tests
  • Receptors, Interleukin-2 / immunology*

Substances

  • Antibodies, Monoclonal
  • Receptors, Interleukin-2