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Glycobiology Advance Access published online on December 17, 2002
Glycobiology, doi:10.1093/glycob/cwg025
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Submitted on September 16, 2002
Revised on October 15, 2002
Accepted on October 15, 2002

© 2002 Oxford University Press

ORIGINAL ARTICLES

Schistosoma mansoni infected mice produce antibodies that cross-react with plant, insect and mammalian glycoproteins and recognize the truncated biantennary N-glycan Man3GlcNAc2-R

Alexandra van Remoortere 1, Christine M.C. Bank 2, A. Kwame Nyame 3, Richard D. Cummings 3, André M. Deelder 4, Irma van Die 2*

1 Department of Molecular Cell Biology, Glycoimmunology Group, VU University Medical Center, Van der Boechorststraat 7, 1081 BT Amsterdam, the Netherlands. Department of Parasitology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, the Netherlands
2 Department of Molecular Cell Biology, Glycoimmunology Group, VU University Medical Center, Van der Boechorststraat 7, 1081 BT Amsterdam, the Netherlands
3 Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Biomedical Research Center, 975 NW 10th Street, Oklahoma City, Oklahoma 73104, USA
4 Department of Parasitology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, the Netherlands

* To whom correspondence should be addressed. E-mail: im.van_die.medchem{at}med.vu.nl.

Abstract

To reveal the role of cross-reactive carbohydrate determinants in the host immune response in helminth infections and allergenicity, we developed monoclonal antibodies (mAbs) that recognize glycan epitopes present on glycoconjugates from both helminths and plants. An IgM mAb (100-4G11-A) was selected from a panel of anti-glycan mAbs generated from Schistosoma infected or immunized mice, because it recognized both a plant glycoprotein horseradish peroxidase and phospholipase A2 from honeybee venom. Upon further characterization, it was shown that mAb 100-4G11-A recognizes the truncated biantennary N-glycan Man3GlcNAc2-R. Immunocytochemical analysis and immunoblotting with this mAb demonstrated that Man3GlcNAc2-R structures occur on many glycoproteins of schistosomes and other invertebrates. Remarkably, Man3GlcNAc2-R is also expressed on a restricted number of vertebrate glycoproteins. Our data indicate that this truncated N-glycan is immunogenic in mice during the course of infection. Nevertheless, no elevated antibody levels against this glycan epitope could be detected in sera of individuals infected with Schistosoma mansoni.


Keywords: anti-carbohydrate monoclonal antibodies, N-glycans, Schistosomes, antigenicity
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