Journal
BIOCHEMICAL JOURNAL
Volume 350, Issue -, Pages 805-814Publisher
PORTLAND PRESS
DOI: 10.1042/0264-6021:3500805
Keywords
O-glycosylation; mass spectrometry; Muc2; parasite infection; sialic acid
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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 GCMS 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/NeuGc alpha 2-3(GalNAc beta 1-4)Gal beta 1 (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 GalNAc beta 1-4 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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