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Vol. 273, Issue 1, 404-409, January 2, 1998
From the Section of Membrane Structure and Function, Laboratory of
Experimental and Computational Biology, Division of Basic Sciences,
National Cancer Institute, National Institutes of Health,
Frederick, Maryland 21702
We have continuously measured CD4-induced
conformational changes of cell surface-expressed human immunodeficiency
virus type-1 envelope glycoprotein gp120-gp41 in situ using
4,4
Conformational Changes in Cell Surface HIV-1 Envelope
Glycoproteins Are Triggered by Cooperation between Cell Surface CD4
and Co-receptors
-dianilino-1,1-binaphthyl-5,5-disulfonic acid, a fluorescent
probe that binds to hydrophobic groups. CD4-expressing human T cell
lines induced significant and rapid conformational changes (<1 min
delay) in gp120-gp41 from T cell-tropic strains, and little
conformational changes in gp120-gp41 from macrophage-tropic strains,
with equivalent levels of envelope expression. Conversely, CD4-expressing human macrophages induced significant and rapid conformational changes in gp120-gp41 from macrophage-tropic strains, and little conformational changes in gp120-gp41 from T cell-tropic strains. Thus, the conformational changes undergone by gp120-gp41, which lead to membrane fusion, are highly cooperative and require both
receptor and co-receptor. We used a dye transfer assay to show that
neither membrane lipid fusion or fusion pore formation can occur with
host cells having different tropism from the envelope.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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