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Glycobiology Advance Access published online on December 22, 2004
Glycobiology, doi:10.1093/glycob/cwi035
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© Oxford University Press 2004; all rights reserved.
Received November 13, 2004
Revised December 18, 2004
Accepted December 21, 2004

Article

Characterization of the N-Linked Glycans of Giardia Intestinalis

Willy Morelle 1*, Juan-Carlos Jimenez 2, Caroline Cieniewski-Bernard 1, Eduardo Dei-Cas 3, and Jean-Claude Michalski 1

1 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.
2 Ecology of Parasitism Group, EA-3609 CHU Hôpital Universitaire de Lille 2, Institut Pasteur of Lille, France.; Laboratory of Immunopathology of Institute of Biomedicine, Faculty of Medicine, Central University of Venezuela, Caracas, Venezuela.
3 Ecology of Parasitism Group, EA-3609 CHU Hôpital Universitaire de Lille 2, Institut Pasteur of Lille, France.

* To whom correspondence should be addressed.
Willy Morelle, E-mail: willy.morelle{at}univ-lille1.fr


  Abstract

This paper 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 Giardia intestinalis are known to stimulate the immune system. Structural strategies based upon 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: Gal{beta}1-4GlcNAc (LacNAc), and NeuAc {alpha}2-6Gal{beta}1-4GlcNAc (sialylated LacNAc).

Keywords: mass spectrometry, glycans, parasite, Giardia, structure analysis, excretory/secretory products.
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