TY - JOUR
T1 - The glycan core of GPI-anchored proteins modulates aerolysin binding but is not sufficient
T2 - the polypeptide moiety is required for the toxin-receptor interaction
AU - Abrami, Laurence
AU - Velluz, Marie-Claire
AU - Hong, Yeongjin J.
AU - Ohishi, Kazuhito
AU - Mehlert, Angela
AU - Ferguson, Michael
AU - Kinoshita, Taroh
AU - van der Goot, F Gisou
PY - 2002/2/13
Y1 - 2002/2/13
N2 - Sensitivity of mammalian cells to the bacterial toxin aerolysin is due to the presence at their surface of glycosylphosphatidyl inositol (GPI)-anchored proteins which act as receptors. Using a panel of mutants that are affected in the GPI biosynthetic pathway and Trypanosoma brucei variant surface glycoproteins, we show that addition of an ethanolamine phosphate residue on the first mannose of the glycan core does not affect binding. In contrast, the addition of a side chain of up to four galactose residues at position 3 of this same mannose leads to an increase in binding. However, protein free GPIs, which accumulate in mutant cells deficient in the transamidase that transfers the protein to the pre-formed GPI-anchor, were unable to bind the toxin indicating a requirement for the polypeptide moiety, the nature and size of which seem of little importance although two exceptions have been identified. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
AB - Sensitivity of mammalian cells to the bacterial toxin aerolysin is due to the presence at their surface of glycosylphosphatidyl inositol (GPI)-anchored proteins which act as receptors. Using a panel of mutants that are affected in the GPI biosynthetic pathway and Trypanosoma brucei variant surface glycoproteins, we show that addition of an ethanolamine phosphate residue on the first mannose of the glycan core does not affect binding. In contrast, the addition of a side chain of up to four galactose residues at position 3 of this same mannose leads to an increase in binding. However, protein free GPIs, which accumulate in mutant cells deficient in the transamidase that transfers the protein to the pre-formed GPI-anchor, were unable to bind the toxin indicating a requirement for the polypeptide moiety, the nature and size of which seem of little importance although two exceptions have been identified. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
U2 - 10.1016/S0014-5793(02)02274-3
DO - 10.1016/S0014-5793(02)02274-3
M3 - Article
SN - 0014-5793
VL - 512
SP - 249
EP - 254
JO - FEBS Letters
JF - FEBS Letters
IS - 1-3
ER -