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

Journal Article · Mon Feb 01 00:00:00 EST 1988 · Journal of Virology; (USA)

OSTI ID:6534918

Kohtz, D S; Kohtz, J D; Puszkin, S ^[1]; Altman, A ^[2]

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1. Mount Sinai School of Medicine of the City Univ. of New York, NY (USA)
2. Scripps Clinic and Research Foundation, La Jolla, CA (USA)

The N-terminal segment of human interleukin-2 (hIL-2) appears to mediate binding of the {beta} hIL-2 receptor. 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.

• OSTI ID: 6534918
• Journal Information: Journal of Virology; (USA), Vol. 62:2; ISSN 0022-538X
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
GLYCOPROTEINS
CROSS-LINKING
LEUKEMIA VIRUSES
ENZYME IMMUNOASSAY
RECEPTORS
AMINO ACID SEQUENCE
GENETICS
IMMUNOGLOBULINS
LYMPHOKINES
BIOASSAY
BIOLOGY
CHEMICAL REACTIONS
GLOBULINS
GROWTH FACTORS
IMMUNOASSAY
MEMBRANE PROTEINS
MICROORGANISMS
MITOGENS
MOLECULAR STRUCTURE
ONCOGENIC VIRUSES
ORGANIC COMPOUNDS
PARASITES
POLYMERIZATION
PROTEINS
VIRUSES
550200* - Biochemistry