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 β receptor

D. S. Kohtz; A. Altman; J. D. Kohtz; S. Puszkin

doi:10.1128/jvi.62.2.659-662.1988

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 β receptor

D. S. Kohtz, A. Altman, J. D. Kohtz, S. Puszkin

Neurology

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22 Scopus citations

Abstract

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

Original language	English (US)
Pages (from-to)	659-662
Number of pages	4
Journal	Journal of virology
Volume	62
Issue number	2
DOIs	https://doi.org/10.1128/jvi.62.2.659-662.1988
State	Published - 1988

Funding

ASJC Scopus subject areas

Insect Science
Virology
Microbiology
Immunology

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10.1128/jvi.62.2.659-662.1988

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title = "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 β receptor",

abstract = "The N-terminal segment of human interleukin-2 (hIL-2) appears to mediate binding of the β 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 β hIL-2 receptor.",

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AU - Puszkin, S.

PY - 1988

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AB - The N-terminal segment of human interleukin-2 (hIL-2) appears to mediate binding of the β 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 β hIL-2 receptor.

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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 β receptor

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