title: Glycomics analysis of Schistosoma mansoni egg and cercarial secretions.
abstract: The parasitic helminth Schistosoma mansoni is a major public health concern in many developing countries. Glycoconjugates, and in particular the carbohydrate component of these products, represent the main immunogenic challenge to the host and could therefore represent one of the crucial determinants for successful parasite establishment. Here we report a comparative glycomics analysis of the N- and O-glycans derived from glycoproteins present in S. mansoni egg (egg-secreted protein) and cercarial (0-3-h released protein) secretions by a combination of mass spectrometric techniques. Our results show that S. mansoni secrete glycoproteins with glycosylation patterns that are complex and stage-specific. Cercarial stage secretions were dominated by N-glycans that were core-xylosylated, whereas N-glycans from egg secretions were predominantly core-difucosylated. O-Glycan core structures from cercarial secretions primarily consisted of the core sequence Galbeta1-->3(Galbeta1-->6)GalNAc, whereas egg-secreted O-glycans carried the mucin-type core 1 (Galbeta1-->3GalNAc) and 2 (Galbeta1-->3(GlcNAcbeta1-->6)GalNAc) structures. Additionally we identified a novel O-glycan core in both secretions in which a Gal residue is linked to the protein. Terminal structures of N- and O-glycans contained high levels of fucose and include stage-specific structures. These glycan structures identified in S. mansoni secretions are potentially antigenic motifs and ligands for carbohydrate-binding proteins of the host immune system.
authors.affiliation: Division of Molecular Biosciences, Imperial College London, London, UK.
authors.forename: Jihye
authors.initials: J
authors.lastname: Jang-Lee
authors.forename: Rachel S
authors.initials: RS
authors.lastname: Curwen
authors.forename: Peter D
authors.initials: PD
authors.lastname: Ashton
authors.forename: Bérangère
authors.initials: B
authors.lastname: Tissot
authors.forename: William
authors.initials: W
authors.lastname: Mathieson
authors.forename: Maria
authors.initials: M
authors.lastname: Panico
authors.forename: Anne
authors.initials: A
authors.lastname: Dell
authors.forename: R Alan
authors.initials: RA
authors.lastname: Wilson
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Haslam
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D000947:Antigens, Helminth / Q000737:chemistry; D002241:Carbohydrates / Q000737:chemistry; D005643:Fucose / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D007477:Ions; D008024:Ligands; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / Q000737:chemistry; D011134:Polysaccharides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D040901:Proteomics / Q000379:methods; D012550:Schistosoma mansoni / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000947:Antigens, Helminth; D002241:Carbohydrates; D006023:Glycoproteins; D007477:Ions; D008024:Ligands; D011134:Polysaccharides; D005643:Fucose; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase