Immunological and structural homology between human T-cell leukemia virus type I envelope glycoprotein and a region of human interleukin-2 implicated in binding the beta receptor.
The N-terminal segment of human interleukin-2 (hIL-2) appears to mediate binding of the beta hIL-2 receptor (R. Robb, C. Rusk, J. Yodoi, and W. Greene, Proc. Natl. Acad. Sci. USA 84:2002-2006, 1987). An affinity-purified antibody prepared against this peptide segment (p81) is shown here to cross-react with a homologous region of the human T-cell leukemia virus type I (HTLV-I) envelope glycoprotein, raising the interesting possibility that the envelope glycoprotein of HTLV-I can interact with the beta hIL-2 receptor.
Kohtz
D S
DS
Department of Pathology, Mount Sinai School of Medicine, City University of New York, New York 10029.
Altman
A
A
Kohtz
J D
JD
Puszkin
S
S
D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D003429:Cross Reactions; D017977:Deltaretrovirus / Q000235:genetics / Q000276:immunology*; D005455:Fluorescent Antibody Technique; D006023:Glycoproteins / Q000235:genetics / Q000276:immunology*; D006801:Humans; D007376:Interleukin-2 / Q000276:immunology*; D010446:Peptide Fragments / Q000276:immunology; D011971:Receptors, Immunologic / Q000276:immunology*; D015375:Receptors, Interleukin-2; D012689:Sequence Homology, Nucleic Acid; D014759:Viral Envelope Proteins / Q000235:genetics / Q000276:immunology*
D006023:Glycoproteins; D007376:Interleukin-2; D010446:Peptide Fragments; D011971:Receptors, Immunologic; D015375:Receptors, Interleukin-2; D014759:Viral Envelope Proteins