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Glycobiology Advance Access originally published online on December 22, 2004
Glycobiology 2005 15(5):549-559; doi:10.1093/glycob/cwi035
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Glycobiology vol. 15 no. 5 © Oxford University Press 2004; all rights reserved.

Characterization of the N-linked glycans of Giardia intestinalis

Willy Morelle1,2, Juan-Carlos Jimenez3,4, Caroline Cieniewski-Bernard2, Eduardo Dei-Cas3 and Jean-Claude Michalski2

2 Unité Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle, IFR 118, Bâtiment C9, Université des Sciences et Technologies de Lille 1, 59655 Villeneuve d’Ascq Cedex, France; 3 Ecology of Parasitism Group, EA-3609 CHU Hôpital Universitaire de Lille 2, Institut Pasteur of Lille, France; and 4 Laboratory of Immunopathology of Institute of Biomedicine, Faculty of Medicine, Central University of Venezuela, Caracas, Venezuela

1 To whom correspondence should be addressed; e-mail: willy.morelle{at}univ-lille1.fr

Received on November 13, 2004; revised on December 18, 2004; accepted on December 21, 2004

This article reports the first rigorous evidence for the existence of N-glycans in Giardia intestinalis, a parasite that is a widespread human pathogen, being a major cause of enteric disease in the world. Excreted/secreted molecules of G. intestinalis are known to stimulate the immune system. Structural strategies based on MALDI and electrospray mass spectrometry were employed to examine the excreted/secreted molecules for their N-glycan content. These revealed that the major oligosaccharides released by peptide N-glycosidase F are complex-type structures and correspond to bi-, and triantennary structures without core ({alpha}1,6) fucosylation. The major nonreducing epitopes in these complex-type glycans are: Galß1-4GlcNAc (LacNAc) and NeuAc {alpha}2-6Galß1-4GlcNAc (sialylated LacNAc).

Key words: excretory and secretory products / Giardia / glycans / parasite / structure analysis


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