The glycan core of GPI-anchored proteins modulates aerolysin binding but is not sufficient: the polypeptide moiety is required for the toxin-receptor interaction.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Abrami L,Velluz MC,Hong Y,Ohishi K,Mehlert A,Ferguson M,Kinoshita T,Gisou van der Goot F

doi

10.1016/s0014-5793(02)02274-3

keywords:

subject

Has Abstract

pub_date

2002-02-13 00:00:00

pages

249-54

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302022743

journal_volume

512

pub_type

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