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Taxonomic group: protista / Apicomplexa (Phylum: Apicomplexa)
Host organism: (mammal)
Organ / tissue: Life stage: tachyzoite
Associated disease: infection due to Toxoplasma gondii [ICD11: 1F57

, ICD11: XN896

]

The structure was elucidated in this paper
NCBI PubMed ID: 21610105
Publication DOI: 10.1074/mcp.M111.008953
Journal NLM ID: 101125647
Publisher: Bethesda, MD: ASBMB
Correspondence: Stan.Tomavo

pasteur-lille.fr
Institutions: Center for Infection and Immunity of Lille, CNRS UMR 8204, INSERM U 1019, Institut Pasteur de Lille, Université Lille Nord de France, 59000 Lille, France

Toxoplasma gondii motility, which is essential for host cell entry, migration through host tissues, and invasion, is a unique form of actin-dependent gliding. It is powered by a motor complex mainly composed of myosin heavy chain A, myosin light chain 1, gliding associated proteins GAP45, and GAP50, the only integral membrane anchor so far described. In the present study, we have combined glycomic and proteomic approaches to demonstrate that all three potential N-glycosylated sites of GAP50 are occupied by unusual N-glycan structures that are rarely found on mature mammalian glycoproteins. Using site-directed mutagenesis, we show that N-glycosylation is a prerequisite for GAP50 transport from the endoplasmic reticulum to the Golgi apparatus and for its subsequent delivery into the inner complex membrane. Assembly of key partners into the gliding complex, and parasite motility are severely impaired in the unglycosylated GAP50 mutants. Furthermore, comparative affinity purification using N-glycosylated and unglycosylated GAP50 as bait identified three novel hypothetical proteins including the recently described gliding associated protein GAP40, and we demonstrate that N-glycans are required for efficient binding to gliding partners. Collectively, these results provide the first detailed analyses of T. gondii N-glycosylation functions that are vital for parasite motility and host cell entry.

infection, glycoproteins, N-glycosylation, N-glycans, Parasite, Toxoplasma, Toxoplasma gondii, N-glycan

Structure type: structural motif or average structure ; 1419 [M+Na]+
Location inside paper: Fig. 1D, Hex6HexNAc2
Aglycon: Asn228/101-X-Set/Thr of GAP50 glycoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141836,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153219,IEDB_153220,IEDB_164174,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_74,SB_77,SB_85

Methods: SDS-PAGE, Western blotting, MALDI-TOF MS, genetic methods, enzymatic digestion, affinity chromatography, cloning, immunofluorescence microscopy, LC-MS/MS, confocal microscopy, gene knockin, nanoLC-MS, cell invasion assay, cell proliferation assay

Related record ID(s): 4892, 4893, 7291
NCBI Taxonomy refs (TaxIDs): 5811
Show glycosyltransferases

There are 64 chemically distinct structures. Please, select:

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]3OC3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O)[C@@H]2O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

, ICD11: XN896

pasteur-lille.fr
Institutions: Center for Infection and Immunity of Lille, CNRS UMR 8204, INSERM U 1019, Institut Pasteur de Lille, Université Lille Nord de France, 59000 Lille, France

infection, glycoproteins, N-glycosylation, N-glycans, Parasite, Toxoplasma, Toxoplasma gondii, N-glycan

Structure type: structural motif or average structure ; 1581 [M+Na]+
Location inside paper: Fig. 1D, Hex7HexNAc2
Aglycon: Asn136-X-Set/Thr of GAP50 glycoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_140628,IEDB_140629,IEDB_141111,IEDB_141793,IEDB_141806,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141836,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153219,IEDB_153220,IEDB_153543,IEDB_153755,IEDB_164174,IEDB_232584,IEDB_241101,IEDB_423115,IEDB_742521,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_74,SB_77,SB_85

Methods: SDS-PAGE, Western blotting, MALDI-TOF MS, genetic methods, enzymatic digestion, affinity chromatography, cloning, immunofluorescence microscopy, LC-MS/MS, confocal microscopy, gene knockin, nanoLC-MS, cell invasion assay, cell proliferation assay

Related record ID(s): 4891, 4893, 7291
NCBI Taxonomy refs (TaxIDs): 5811
Show glycosyltransferases

There are 256 chemically distinct structures. Please, select:

SVG MW SMILES 3D mol Ionize

, ICD11: XN896

pasteur-lille.fr
Institutions: Center for Infection and Immunity of Lille, CNRS UMR 8204, INSERM U 1019, Institut Pasteur de Lille, Université Lille Nord de France, 59000 Lille, France

infection, glycoproteins, N-glycosylation, N-glycans, Parasite, Toxoplasma, Toxoplasma gondii, N-glycan

Structure type: structural motif or average structure ; 1743 [M+Na]+
Location inside paper: Fig. 1D, Hex8HexNAc2
Aglycon: Asn136-X-Set/Thr of GAP50 glycoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_135614,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_140628,IEDB_140629,IEDB_141111,IEDB_141793,IEDB_141806,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141836,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153219,IEDB_153220,IEDB_153543,IEDB_153755,IEDB_158538,IEDB_158555,IEDB_164174,IEDB_232584,IEDB_232585,IEDB_2346541,IEDB_241101,IEDB_420421,IEDB_423115,IEDB_742521,IEDB_857742,IEDB_983930,IEDB_983931,SB_136,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_74,SB_77,SB_85

Methods: SDS-PAGE, Western blotting, MALDI-TOF MS, genetic methods, enzymatic digestion, affinity chromatography, cloning, immunofluorescence microscopy, LC-MS/MS, confocal microscopy, gene knockin, nanoLC-MS, cell invasion assay, cell proliferation assay

Related record ID(s): 4891, 4892, 7291
NCBI Taxonomy refs (TaxIDs): 5811
Show glycosyltransferases

There are too many chemically distinct structures (~1024), so only one is shown:

?DGlcp(1-2)?DGlcp(1-2)?DGlcp(1-2)aDManp(1-2)aDManp(1-2)bDManp(1-3)[bDManp(1-6)]bDManp(1-4)[Ac(1-2)]bDGlcpN(1-4)[Ac(1-2)]bDGlcpN

SVG MW SMILES 3D mol Ionize

, ICD11: XN896

pasteur-lille.fr
Institutions: Center for Infection and Immunity of Lille, CNRS UMR 8204, INSERM U 1019, Institut Pasteur de Lille, Université Lille Nord de France, 59000 Lille, France

infection, glycoproteins, N-glycosylation, N-glycans, Parasite, Toxoplasma, Toxoplasma gondii, N-glycan

Structure type: structural motif or average structure ; 1419 [M+Na]+
Location inside paper: Fig. 1D, Hex6HexNAc2
Aglycon: Asn228/101-X-Set/Thr of GAP50 glycoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_153762,IEDB_164174,IEDB_164176,IEDB_174840,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_74,SB_77,SB_85

Methods: SDS-PAGE, Western blotting, MALDI-TOF MS, genetic methods, enzymatic digestion, affinity chromatography, cloning, immunofluorescence microscopy, LC-MS/MS, confocal microscopy, gene knockin, nanoLC-MS, cell invasion assay, cell proliferation assay
Comments, role: exact position of aDManp at bDManp residues unknown

Related record ID(s): 4891, 4892, 4893
NCBI Taxonomy refs (TaxIDs): 5811
Show glycosyltransferases

There are 64 chemically distinct structures. Please, select:

SVG MW SMILES 3D mol Ionize