Two new murine monoclonal
IgG1 antibodies, H-31 and H-A26, were characterized in comparison with two previously obtained
monoclonal antibodies against human
interleukin 2 (IL-2) receptor (IL-2 R), anti-Tac and HIEI. In immunofluorescence assays with various human hematopoietic cells, H-31 and H-A26
antibodies both reacted with only
IL-2 R-positive cells, and they precipitated
IL-2 R molecules,
glycoproteins with molecular weights of 60K and 53K daltons (gp60/gp53), from human
T-cell leukemia virus type I (HTLV-I)-carrying MT-2 cells, as demonstrated by sequential immunoprecipitation after absorption of
IL-2 R with anti-Tac. Antibody-binding competition assays showed that H-31 and anti-Tac, and H-A26 and HIEI, respectively, competed reciprocally in binding to the cells, and that anti-Tac also inhibited the binding of HIEI but not vice versa. H-31, like anti-Tac, strongly inhibited the IL-2-dependent proliferation of normal activated T-cells, absorption of
IL-2 and direct binding of
IL-2 to the cells, while H-A26, like HIEI, inhibited those processes only weakly. The spectra of reactivities of these
antibodies with various simian cell lines derived by
HTLV-I infection were different, as revealed by immunofluorescence studies. Human
IL-2 R was shown to express a unique
antigenic determinant, detected with HIEI, that was not detectable in
IL-2 R molecules of Old and New World monkeys, and also to express determinants common to simian
IL-2 R molecules. These observations indicate that H-31 and H-A26 recognize human
IL-2 R molecules and that the antigenic sites on the
IL-2 R molecule defined by H-31, H-A26, anti-Tac, and HIEI are different.