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J. Biol. Chem., Vol. 266, Issue 18, 11433-11435, 06, 1991

CD4+ lipid bilayers. A model for human immunodeficiency virus type 1 coat protein binding

MT Tosteson, PF Tosi, C Nicolau and DC Tosteson
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.

gp120, the coat glycoprotein of the human immunodeficiency virus type 1 (HIV1) binds to a molecule on the surface of a class of T-lymphocytes, CD4, which is also the receptor for major histocompatibility complex class II (MHCII). To study the events that follow the interaction of gp120 with CD4, we have incorporated CD4 into lipid bilayers and recorded the electrical changes which occur after the addition of gp120. Interaction of gp120 to CD4-containing bilayers induces multistate ion-permeable channels with a maximum conductance of 380-400 picosiemens. When CD4+ bilayers were preexposed to either MHCII or to OKT4A antibody, no channels were formed after the addition of gp120. These results indicate that CD(4+)-containing bilayers bind gp120, MHCII, and OKT4A, that binding of gp120 produces ion-permeable channels, and that CD4+ bilayers can be used to assay for gp120 in the solution bathing the bilayer.
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				M. T. Tosteson, H. Wang, A. Naumov, and M. Chow Poliovirus binding to its receptor in lipid bilayers results in particle-specific, temperature-sensitive channels J. Gen. Virol., June 1, 2004; 85(6): 1581 - 1589. [Abstract] [Full Text] [PDF]