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Targeted Glycoproteomic Analysis Reveals That Kappa-5 is a Major, Uniquely Glycosylated Component of Schistosoma mansoni Egg Antigens
- Source :
- Molecular and Cellular Proteomics (MCP Online); May 2011, Vol. 10 Issue: 5 pM110.00571-M110.00571, 1p
- Publication Year :
- 2011
-
Abstract
- Glycans present on glycoproteins from the eggs of the parasite Schistosoma mansoni are mediators of various immune responses of the human host, including T-cell modulation and granuloma formation, and they are the target of glycan-specific antibodies. Here we have analyzed the glycosylation of kappa-5, a major glycoprotein antigen from S. mansoni eggs using a targeted approach of lectin purification followed by mass spectrometry of glycopeptides as well as released glycans. We demonstrate that kappa-5 has four fully occupied N-glycosylation sites carrying unique triantennary glycans composed of a difucosylated and xylosylated core region, and immunogenic GalNAcβ1–4GlcNAc (LDN) termini. Furthermore, we show that the kappa-5 specific IgE antibodies in sera of S. mansoni-infected individuals are directed against the core region of the kappa-5 glycans. Whereas two previously analyzed immunomodulatory egg glycoproteins, IPSE/alpha-1 and omega-1, both express diantennary N-glycans with a difucosylated core and one or two Galβ1–4(Fucα1–3)GlcNAc (Lewis X) antennae, the kappa-5 glycosylation appears unique among the major soluble egg antigens of S. mansoni. The distinct structural and antigenic properties of kappa-5 glycans suggest a specific role for kappa-5 in schistosome egg immunogenicity.
Details
- Language :
- English
- ISSN :
- 15359476 and 15359484
- Volume :
- 10
- Issue :
- 5
- Database :
- Supplemental Index
- Journal :
- Molecular and Cellular Proteomics (MCP Online)
- Publication Type :
- Periodical
- Accession number :
- ejs23842905