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Vol. 273, Issue 4, 2355-2360, January 23, 1998
From the Department of Biochemistry and Microbiology,
University of Victoria, Victoria, British Columbia, Canada V8W
3P6
Cells that are sensitive to the channel-forming
toxin aerolysin contain surface glycoproteins that bind the toxin with
high affinity. Here we show that a common feature of aerolysin
receptors is the presence of a glycosylphosphatidylinositol anchor, and we present evidence that the anchor itself is an essential part of the
toxin binding determinant. The glycosylphosphatidylinositol (GPI)-anchored T-lymphocyte protein Thy-1 is an example of a protein that acts as an aerolysin receptor. This protein retained its ability
to bind aerolysin when it was expressed in Chinese hamster ovary cells,
but could not bind the toxin when expressed in Escherichia coli, where the GPI anchor is absent. An unrelated GPI-anchored protein, the variant surface glycoprotein of trypanosomes, was shown to
bind aerolysin with similar affinity to Thy-1, and this binding ability
was significantly reduced when the anchor was removed chemically.
Cathepsin D, a protein with no affinity for aerolysin, was converted to
an aerolysin binding form when it was expressed as a GPI-anchored
hybrid in COS cells. Not all GPI-anchored proteins bind aerolysin. In
some cases this may be due to differences in the structure of the
anchor itself. Thus the GPI-anchored proteins procyclin of
Trypanosoma congolense and gp63 of Leishmania
major did not bind aerolysin, but when gp63 was expressed with a
mammalian GPI anchor in Chinese hamster ovary cells, it bound the
toxin.
Glycosylphosphatidylinositol Anchors of Membrane Glycoproteins
Are Binding Determinants for the Channel-forming Toxin Aerolysin
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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