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Glycobiology Advance Access originally published online on May 15, 2006
Glycobiology 2006 16(9):854-862; doi:10.1093/glycob/cwl001
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© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Protein glycosylation in Parelaphostrongylus tenuis—first description of the Gal{alpha}1-3Gal sequence in a nematode

Michael S. Duffy2, Howard R. Morris3, Anne Dell3, Judith A. Appleton2 and Stuart M. Haslam1,3

2 James A. Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853; and 3 Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK


1 To whom correspondence should be addressed; e-mail: s.haslam{at}imperial.ac.uk

Received on March 6, 2006; revised on May 9, 2006; accepted on May 10, 2006

The white-tailed deer is the definitive host of the parasitic nematode Parelaphostrongylus tenuis. This parasite also infects a wide variety of domesticated livestock, causing a debilitating neurologic disease. Glycoconjugates are becoming increasingly implicated in nematode strategies to maintain persistent infections in immunologically competent hosts. In this study, we have carried out detailed mass spectrometric analysis together with classical biochemical techniques, including western blotting and immunohistochemical staining with anticarbohydrate monoclonal antibodies and have shown that P. tenuis contains complex-type N-glycans with the antennae capped with Gal{alpha}1-3Galß1-4GlcNAc sequence. By mimicking a vertebrate glycan, Gal{alpha}1-3Gal may aid the parasite in evading immunological detection by the host. This is the first report of the Gal{alpha}1-3Gal sequence in a nematode.

Key words: glycosylation / Parelaphostrongylus tenuis / mass spectrometry / nematode


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