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Identification of transient glycosylation alterations of sialylated mucin oligosaccharides during infection by the rat intestinal parasite Nippostrongylus brasiliensis.

Journal article
Authors Niclas G. Karlsson
Fredrik J. Olson
Per-Åke Jovall
Ylva Andersch
Lennart Enerbäck
Gunnar C. Hansson
Published in The Biochemical journal
Volume 350 Pt 3
Pages 805-14
ISSN 0264-6021
Publication year 2000
Published at Institute of Medical Biochemistry
Institute of Laboratory Medicine, Dept of Pathology
Pages 805-14
Language en
Links www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Animals, Carbohydrate Sequence, Gas Chromatography-Mass Spectrometry, Glycosylation, Mixed Function Oxygenases, antagonists & inhibitors, Molecular Sequence Data, Mucin-2, Mucins, metabolism, N-Acetylneuraminic Acid, metabolism, Nippostrongylus, physiology, Oligosaccharides, metabolism, Rats, Rats, Sprague-Dawley, Strongylida Infections, metabolism
Subject categories Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

Abstract

The sialylation of the oligosaccharides from small-intestinal mucins during a 13-day infectious cycle was studied in Sprague-Dawley rats with the parasite Nippostrongylus brasiliensis. Sialic acid analysis and release, permethylation and analysis by GC-MS of the sialylated oligosaccharides isolated from the 'insoluble' mucin complex revealed a relative decrease (4-7-fold) of N-glycolylneuraminic acid compared with N-acetylneuraminic acid just before parasite expulsion. Northern blots showed that this effect was due to the decreased expression of a hydroxylase converting CMP-N-acetylneuraminic acid into CMP-N-glycolylneuraminic acid. Analysis of other rat strains showed that this parasite infection also caused the same effect in these animals. Detailed analysis of infected Sprague-Dawley rats revealed four sialylated oligosaccharides not found in the uninfected animals. These new oligosaccharides were characterized in detail and all shown to contain the trisaccharide epitope NeuAc/NeuGcalpha2-3(GalNAcbeta1-4)Galbeta1 (where NeuGc is N-glycolyl neuraminic acid). This epitope is similar to the Sd(a)- and Cad-type blood-group antigens and suggests that the infection causes the induction of a GalNAcbeta1-4 glycosyltransferase. This model for an intestinal infection suggests that the glycosylation of intestinal mucins is a dynamic process being modulated by the expression of specific enzymes during an infection process.

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