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Taxonomic group: protista / Apicomplexa (Phylum: Apicomplexa)
Host organism: Homo sapiens
Organ / tissue: oocysts
Associated disease: infection due to Cryptosporidium parvum [ICD11: XN9BP

]

The structure was elucidated in this paper
NCBI PubMed ID: 28179475
Publication DOI: 10.1074/mcp.M116.066035
Journal NLM ID: 101125647
Publisher: Bethesda, MD: ASBMB
Correspondence: cecmsms

bu.edu
Institutions: Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118, Center for Biomedical Mass Spectrometry, Department of Biochemistry, Cell Biology and Genomics, Boston University School of Medicine, Boston, Massachusetts 02118

Cryptosporidium parvum causes severe diarrhea in infants in developing countries and in immunosuppressed persons, including those with AIDS. We are interested in the Asn-linked glycans (N-glycans) of C. parvum, because (1) the N-glycan precursor is predicted to contain five mannose and two glucose residues on a single long arm versus nine mannose and three glucose residues on the three-armed structure common in host N-glycans, (2) C. parvum is a rare eukaryote that lacks the machinery for N-glycan-dependent quality control of protein folding in the lumen of the Endoplasmic Reticulum (ER), and (3) ER and Golgi mannosidases, as well as glycosyltransferases that build complex N-glycans, are absent from the predicted proteome. The C. parvum N-glycans reported here, which were determined using a combination of collision-induced dissociation and electronic excitation dissociation, contain a single, unprocessed mannose arm � terminal glucose on the trimannosyl chitobiose core. Upon nanoUPLC-MS/MS separation and analysis of the C. parvum tryptic peptides, the total ion and extracted oxonium ion chromatograms delineated 32 peptides with occupied N-glycan sites; these were derived from 16 glycoproteins. Although the number of potential N-glycan sites with Thr (NxT) is only about twice that with Ser (NxS), almost 90% of the occupied N-glycan sites contain NxT. The two most abundant C. parvum proteins modified with N-glycans were an immunodominant antigen on the surface of sporozoites (gp900) and the possible oocyst wall protein 1 (POWP1). Seven other glycoproteins with N-glycans were unique to C. parvum; five shared common ancestry with other apicomplexans; two glycoproteins shared common ancestry with many organisms. In summary, C. parvum N-glycans are remarkable for the absence of ER and Golgi modification and for the strong bias toward occupancy of N-glycan motifs containing Thr.

antigen, glycosyltransferases, mass spectrometry, glycoproteins, N-glycans, Cryptosporidium parvum

Structure type: structural motif or average structure
Location inside paper: Fig. S3, Glc2Man5GlcNAc2
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141830,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_540671,IEDB_548907,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

Methods: MALDI-TOF MS, enzymatic digestion, permethylation, reduction with NaBD4, bioinformatic analysis, LC-MS/MS, EED-FT-ICR MS/MS, N-glycosylation sites analysis, scaffold analysis
Comments, role: predicted structure

Related record ID(s): 4540, 4542, 7310
NCBI Taxonomy refs (TaxIDs): 5807
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@H]1[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@H](NC(C)=O)[C@H]2O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O)[C@@H](O)[C@H](O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@H]5O)[C@H]4O)[C@@H]3O)[C@@H]2O)[C@@H]1O

SVG MW SMILES 3D mol Ionize