Leiden University Scholarly Publications

Persistent URL of this record https://hdl.handle.net/1887/110636

In Collections

This item can be found in the following collections:

Meevissen, M.H.J.; Balog, C.I.A.; Koeleman, C.A.M.; Doenhoff, M.J.; Schramm, G.; Haas, H.; ... ; Hokke, C.H. (2011)

Targeted Glycoproteomic Analysis Reveals That Kappa-5 is a Major, Uniquely Glycosylated Component of Schistosoma mansoni Egg Antigens

Article / Letter to editor
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 GalNAc beta 1-4GlcNAc (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...Show moreGlycans 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 GalNAc beta 1-4GlcNAc (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 Gal beta 1-4(Fuc alpha 1-3)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. Molecular & Cellular Proteomics 10: 10.1074/mcp.M110.005710, 1-14, 2011.Show less
macrophage mannose receptor n-glycans lewis-x th2 responses in-vivo molecular characterization carbohydrate epitopes antibody-responses immune-responses dc-sign
All authors
Meevissen, M.H.J.; Balog, C.I.A.; Koeleman, C.A.M.; Doenhoff, M.J.; Schramm, G.; Haas, H.; Deelder, A.M.; Wuhrer, M.; Hokke, C.H.
Date
2011-05-31
Journal
Molecular and Cellular Proteomics
Volume
10
Issue
5