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The erythrocyte receptor for the channel‐forming toxin aerolysin is a novel glycosylphosphatidylinositol‐anchored protein
Author(s) -
Cowell Simon,
Aschauer Wolfgang,
Gruber Hermann J.,
Nelson Kim L.,
Buckley J. Thomas
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.4691828.x
Subject(s) - aerolysin , biology , receptor , toxin , glycoprotein , biochemistry , blot , microbiology and biotechnology , gene , virulence
The plasma membrane of rat erythrocytes contains a 47‐kDa glycoprotein that binds the channel‐forming toxin aerolysin with high affinity and accounts for the sensitivity of these cells to the toxin. The receptor was purified so that its N‐terminal sequence could be determined after Western blotting. The sequence did not match any sequences in the databases, indicating that the receptor is a novel erythrocyte surface protein. However, it exhibited considerable homology to the N‐termini of a group of membrane proteins that are thought to be involved in ADP‐ribosyl transfer reactions. A common property of these proteins is that they are attached to plasma membranes by C‐terminal glycosylphosphatidylinositol (GPI) anchors. The aerolysin receptor was shown to be anchored in the same way by treating rat erythrocytes with phosphatidylinositol‐specific phospholipase C. This caused the selective release of the receptor and a reduction in the rodent cells’ sensitivity to aerolysin. Human and bovine erythrocytes were shown to contain an aerolysin‐binding protein with similar properties to the rat erythrocyte receptor. Proteins with GPI anchors are thought to have unusually high lateral mobility, and this may be an advantage for a toxin, such as aerolysin, which must oligomerize after binding to become insertion competent.