The interaction of CD4 with HIV-1 gp120

S. L. Silberman; S. J. Goldman; D. B. Mitchell; A. T. Tong; Y. Rosenstein; D. C. Diamond; R. W. Finberg; S. L. Schreiber; S. J. Burakoff

The interaction of CD4 with HIV-1 gp120

S. L. Silberman, S. J. Goldman, D. B. Mitchell, A. T. Tong, Y. Rosenstein, D. C. Diamond, R. W. Finberg, S. L. Schreiber, S. J. Burakoff

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

CD4 is an integral cell surface glycoprotein that is able to enhance T cell specific antigen responses when it interacts with its physiological ligand, class II major histocompatibility (MHC) molecules. In addition, CD4 is a specific cell-surface receptor for the human immunodeficiency virus-1 (HIV-1). Infection by HIV-1 is initiated by the binding of the envelope glycoprotein, gp120, to the first domain of CD4. The binding of CD4 to class II MHC is inhibited by gp120, one possible mechanism for immunosuppression in AIDS patients. In addition, the CD4/gp120 interaction may directly inhibit T cell function. Recently we have synthesized small molecules (CPFs) that specifically inhibit this interaction. CPFs bind to gp120 and prevent the binding of gp120 to CD4, and also inhibit the infectivity of HIV-1.

Original language	English
Pages (from-to)	187-192
Number of pages	6
Journal	Seminars in Immunology
Volume	3
Issue number	3
State	Published - May 1991
Externally published	Yes

Keywords

CD4 T cells
CPF
HIV
gp120

Cite this

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title = "The interaction of CD4 with HIV-1 gp120",

abstract = "CD4 is an integral cell surface glycoprotein that is able to enhance T cell specific antigen responses when it interacts with its physiological ligand, class II major histocompatibility (MHC) molecules. In addition, CD4 is a specific cell-surface receptor for the human immunodeficiency virus-1 (HIV-1). Infection by HIV-1 is initiated by the binding of the envelope glycoprotein, gp120, to the first domain of CD4. The binding of CD4 to class II MHC is inhibited by gp120, one possible mechanism for immunosuppression in AIDS patients. In addition, the CD4/gp120 interaction may directly inhibit T cell function. Recently we have synthesized small molecules (CPFs) that specifically inhibit this interaction. CPFs bind to gp120 and prevent the binding of gp120 to CD4, and also inhibit the infectivity of HIV-1.",

keywords = "CD4 T cells, CPF, HIV, gp120",

author = "Silberman, {S. L.} and Goldman, {S. J.} and Mitchell, {D. B.} and Tong, {A. T.} and Y. Rosenstein and Diamond, {D. C.} and Finberg, {R. W.} and Schreiber, {S. L.} and Burakoff, {S. J.}",

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AU - Silberman, S. L.

AU - Goldman, S. J.

AU - Mitchell, D. B.

AU - Tong, A. T.

AU - Rosenstein, Y.

AU - Diamond, D. C.

AU - Finberg, R. W.

AU - Schreiber, S. L.

AU - Burakoff, S. J.

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N2 - CD4 is an integral cell surface glycoprotein that is able to enhance T cell specific antigen responses when it interacts with its physiological ligand, class II major histocompatibility (MHC) molecules. In addition, CD4 is a specific cell-surface receptor for the human immunodeficiency virus-1 (HIV-1). Infection by HIV-1 is initiated by the binding of the envelope glycoprotein, gp120, to the first domain of CD4. The binding of CD4 to class II MHC is inhibited by gp120, one possible mechanism for immunosuppression in AIDS patients. In addition, the CD4/gp120 interaction may directly inhibit T cell function. Recently we have synthesized small molecules (CPFs) that specifically inhibit this interaction. CPFs bind to gp120 and prevent the binding of gp120 to CD4, and also inhibit the infectivity of HIV-1.

AB - CD4 is an integral cell surface glycoprotein that is able to enhance T cell specific antigen responses when it interacts with its physiological ligand, class II major histocompatibility (MHC) molecules. In addition, CD4 is a specific cell-surface receptor for the human immunodeficiency virus-1 (HIV-1). Infection by HIV-1 is initiated by the binding of the envelope glycoprotein, gp120, to the first domain of CD4. The binding of CD4 to class II MHC is inhibited by gp120, one possible mechanism for immunosuppression in AIDS patients. In addition, the CD4/gp120 interaction may directly inhibit T cell function. Recently we have synthesized small molecules (CPFs) that specifically inhibit this interaction. CPFs bind to gp120 and prevent the binding of gp120 to CD4, and also inhibit the infectivity of HIV-1.

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The interaction of CD4 with HIV-1 gp120

Abstract

Keywords

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