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Targeted glycoproteomic analysis reveals that kappa-5 is a major, uniquely glycosylated component of Schistosoma mansoni egg antigens.
- Source :
-
Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2011 May; Vol. 10 (5), pp. M110.005710. Date of Electronic Publication: 2011 Mar 03. - 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.
- Subjects :
- Amino Acid Motifs
Animals
Antibodies, Helminth chemistry
Antigens, Helminth
Egg Proteins immunology
Glycoproteins immunology
Glycoside Hydrolases chemistry
Glycosylation
Helminth Proteins immunology
Host-Parasite Interactions
Humans
Immunoglobulin E blood
Immunoglobulin E chemistry
Lactose analogs & derivatives
Lactose immunology
Lactose metabolism
Peptide Fragments chemistry
Polysaccharides chemistry
Schistosoma mansoni immunology
Schistosomiasis mansoni immunology
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tandem Mass Spectrometry
Antibodies, Helminth blood
Egg Proteins metabolism
Glycoproteins metabolism
Helminth Proteins metabolism
Schistosoma mansoni metabolism
Schistosomiasis mansoni blood
Subjects
Details
- Language :
- English
- ISSN :
- 1535-9484
- Volume :
- 10
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular & cellular proteomics : MCP
- Publication Type :
- Academic Journal
- Accession number :
- 21372247
- Full Text :
- https://doi.org/10.1074/mcp.M110.005710