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Structural characterization of glycans on omega-1, a major Schistosoma mansoni egg glycoprotein that drives Th2 responses. | LitMetric

AI Article Synopsis

  • Soluble egg antigens (SEA) from the human parasite Schistosoma mansoni are key triggers for Th2 immune responses, with omega-1 being a major glycoprotein that influences dendritic cell behavior.
  • The study focuses on the glycosylation patterns of omega-1 using advanced mass spectrometry and enzyme treatments to analyze its glycopeptides.
  • Findings reveal that omega-1 has two N-glycosylation sites featuring specific glycan structures, enhancing understanding of how this protein modulates immune responses.

Article Abstract

Soluble egg antigens (SEA) of the human parasite Schistosoma mansoni are among the strongest natural stimuli of Th2 responses. Omega-1, a major glycoprotein in SEA, initiates these characteristic Th2 responses through conditioning of dendritic cells (DCs). In view of the reported immunomodulatory potential of SEA glycans, we have investigated omega-1 glycosylation, using an approach combining mass spectrometric techniques and enzyme treatments at the glycopeptide level. We demonstrate that omega-1 has two fully occupied N-glycosylation sites, each mainly carrying core-difucosylated diantennary glycans with one or more Lewis X motifs in the antennae. Using a specific approach of nanoscale LC-MS(/MS) and MALDI-TOF(/TOF) MS in combination with exoglycosidase treatments of tryptic glycopeptides, we were able to provide a detailed, site-specific glycosylation analysis of a single, native S. mansoni glycoprotein. The obtained knowledge of the glycans present on omega-1 contributes to a full understanding of the mode of action of this immunomodulatory glycoprotein.

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Source
http://dx.doi.org/10.1021/pr100081cDOI Listing

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