Found 124 structures.
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1. Compound ID: 15225
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
b-D-GlcpNAc-(1-4)-+ | a-L-Fucp-(1-3)-+
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/s-gp130 peptide/
| |
a-D-Manp-(1-3)-+ |
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
; 2296 [M+Na]+
Aglycon: s-gp130 peptide
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_187201,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5922
Feasley C, Johnson JM, West CM, Chia CP "Glycopeptidome of a Heavily N-Glycosylated Cell Surface Glycoprotein of Dictyostelium Implicated in Cell Adhesion" -
Journal of Proteome Research 9(7) (2010) 3495-3510
Genetic analysis has implicated the cell surface glycoprotein gp130 in cell interactions of the social amoeba Dictyostelium, and information about the utilization of the 18 N-glycosylation sequons present in gp130 is needed to identify critical molecular determinants of its activity. Various glycomics strategies, including mass spectrometry of native and derivatized glycans, monosaccharide analysis, exoglycosidase digestion, and antibody binding, were applied to characterize a nonanchored version secreted from Dictyostelium. s-gp130 is modified by a predominant Man(8)GlcNAc(4) species containing bisecting and intersecting GlcNAc residues and additional high-mannose N-glycans substituted with sulfate, methyl-phosphate, and/or core alpha 3-fucose. Site mapping confirmed the occupancy of 15 sequons, some variably, and glycopeptide analysis confirmed 14 sites and revealed extensive heterogeneity at most sites. Glycopeptide glycoforms ranged from Man(6) to Man(9), GlcNAc(0-2) (peripheral), Fuc(0-2) (including core alpha 3 and peripheral), (SO(4))(0-1), and (MePO(4))(0-1), which represented elements of virtually the entire known cellular N-glycome as inferred from prior metabolic labeling and mass spectrometry studies. gp130, and a family of 14 related predicted glycoproteins whose polypeptide sequences are rapidly diverging in the Dictyostelium lineage, may contribute a functionally important shroud of high-mannose N-glycans at the interface of the amoebae with each other, their predators and prey, and the soil environment.
mass spectrometry, glycobiology, N-glycan, Dictyostelium, glycopeptidome, gp130
NCBI PubMed ID: 20443635Publication DOI: 10.1021/pr901195cJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: Cwest2@ouhsc.edu
Institutions: Department of Biochemistry & Molecular Biology and Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, amino acid analysis, MALDI-TOF MS, genetic methods, enzymatic digestion, HPAEC-PAD, permethylation, cloning, RP-HPLC, MALDI-TOF/TOF MS, reductive amination, nanoLC-MS/MS
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2. Compound ID: 15233
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ | a-L-Fucp-(1-3)-+
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
| |
b-D-GlcpNAc-(1-4)-+ |
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
; 2295.8 [M+Na]+
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_187201,IEDB_429156,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5923
Feasley C, van der Wel H, West CM "Evolutionary diversity of social amoebae N-glycomes may support interspecific autonomy" -
Glycoconjugate Journal 32(6) (2015) 345-359
Multiple species of cellular slime mold (CSM) amoebae share overlapping subterranean environments near the soil surface. Despite similar life-styles, individual species form independent starvation-induced fruiting bodies whose spores can renew the life cycle. N-glycans associated with the cell surface glycocalyx have been predicted to contribute to interspecific avoidance, resistance to pathogens, and prey preference. N-glycans from five CSM species that diverged 300-600 million years ago and whose genomes have been sequenced were fractionated into neutral and acidic pools and profiled by MALDI-TOF-MS. Glycan structure models were refined using linkage specific antibodies, exoglycosidase digestions, MALDI-MS/MS, and chromatographic studies. Amoebae of the type species Dictyostelium discoideum express modestly trimmed high mannose N-glycans variably modified with core α3-linked Fuc and peripherally decorated with 0-2 residues each of β-GlcNAc, Fuc, methylphosphate and/or sulfate, as reported previously. Comparative analyses of D. purpureum, D. fasciculatum, Polysphondylium pallidum, and Actyostelium subglobosum revealed that each displays a distinctive spectrum of high-mannose species with quantitative variations in the extent of these modifications, and qualitative differences including retention of Glc, mannose methylation, and absence of a peripheral GlcNAc, fucosylation, or sulfation. Starvation-induced development modifies the pattern in all species but, except for universally observed increased mannose-trimming, the N-glycans do not converge to a common profile. Correlations with glycogene repertoires will enable future reverse genetic studies to eliminate N-glycomic differences to test their functions in interspecific relations and pathogen evasion.
evolution, N-glycan, Dictyostelium, Cellular slime molds, Social amoebae
NCBI PubMed ID: 25987342Publication DOI: 10.1007/s10719-015-9592-8Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: Christopher M. West
; Christopher M. West
Institutions: Department of Biochemistry & Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, 975 NE 10th St., BRC-415, OUHSC, Oklahoma City, OK, 73104, USA
Methods: SDS-PAGE, Western blotting, MALDI-TOF MS, enzymatic digestion, permethylation, column chromatography, MALDI-TOF/TOF MS, bioinformatic analysis (BLASTp)
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3. Compound ID: 15328
a-D-Manp-(1-3)-a-D-Manp-(1-6)-+ a-L-Fucp-(1-3)-+
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/2-aminopyridine (PA)/ |
Show graphically |
Structure type: oligomer
; 1459 [M+H]+
Aglycon: 2-aminopyridine (PA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_164174,IEDB_174333,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5945
Hykollari A, Balog CIA, Rendic D, Braulke W, Wilson IBH "Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL" -
Journal of Proteome Research 12(3) (2013) 1173-1187
The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.
glycan, mass spectrometry, fucose, sulfate, Mannosyltransferase, N-glycans, Dictyostelium, methylphosphate
NCBI PubMed ID: 23320427Publication DOI: 10.1021/pr300806bJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria, Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands, Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, MALDI-TOF MS, enzymatic digestion, HF treatment, RT-PCR, cloning, RP-HPLC, RNA sequencing, HIAX-HPLC, MALDI-TOF MS/MS
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4. Compound ID: 15329
a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
|
S-6)-+ | a-L-Fucp-(1-3)-+
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/2-aminopyridine (PA)/ |
Show graphically |
Structure type: oligomer
; 1537 [M-H]-
Aglycon: 2-aminopyridine (PA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_164174,IEDB_174333,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5945
Hykollari A, Balog CIA, Rendic D, Braulke W, Wilson IBH "Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL" -
Journal of Proteome Research 12(3) (2013) 1173-1187
The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.
glycan, mass spectrometry, fucose, sulfate, Mannosyltransferase, N-glycans, Dictyostelium, methylphosphate
NCBI PubMed ID: 23320427Publication DOI: 10.1021/pr300806bJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria, Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands, Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, MALDI-TOF MS, enzymatic digestion, HF treatment, RT-PCR, cloning, RP-HPLC, RNA sequencing, HIAX-HPLC, MALDI-TOF MS/MS
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5. Compound ID: 15330
a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
|
S-6)-+ | a-L-Fucp-(1-3)-+
| | |
P0Me-(0-6)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/2-aminopyridine (PA)/ |
Show graphically |
Structure type: oligomer
; 1631 [M-H]-
Aglycon: 2-aminopyridine (PA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_164174,IEDB_174333,IEDB_474450,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5945
Hykollari A, Balog CIA, Rendic D, Braulke W, Wilson IBH "Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL" -
Journal of Proteome Research 12(3) (2013) 1173-1187
The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.
glycan, mass spectrometry, fucose, sulfate, Mannosyltransferase, N-glycans, Dictyostelium, methylphosphate
NCBI PubMed ID: 23320427Publication DOI: 10.1021/pr300806bJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria, Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands, Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, MALDI-TOF MS, enzymatic digestion, HF treatment, RT-PCR, cloning, RP-HPLC, RNA sequencing, HIAX-HPLC, MALDI-TOF MS/MS
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6. Compound ID: 15333
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-3)-+ | a-L-Fucp-(1-3)-+
| | |
b-D-GlcpNAc-(1-4)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/2-aminopyridine (PA)/
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
; 1865 [M+H]+
Aglycon: 2-aminopyridine (PA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_164174,IEDB_174333,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5945
Hykollari A, Balog CIA, Rendic D, Braulke W, Wilson IBH "Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL" -
Journal of Proteome Research 12(3) (2013) 1173-1187
The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.
glycan, mass spectrometry, fucose, sulfate, Mannosyltransferase, N-glycans, Dictyostelium, methylphosphate
NCBI PubMed ID: 23320427Publication DOI: 10.1021/pr300806bJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria, Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands, Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, MALDI-TOF MS, enzymatic digestion, HF treatment, RT-PCR, cloning, RP-HPLC, RNA sequencing, HIAX-HPLC, MALDI-TOF MS/MS
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7. Compound ID: 15345
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ | a-L-Fucp-(1-3)-+
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/2-aminopyridine (PA)/
| |
b-D-GlcpNAc-(1-4)-+ |
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
; 2351 [M+H]+
Aglycon: 2-aminopyridine (PA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_187201,IEDB_429156,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5945
Hykollari A, Balog CIA, Rendic D, Braulke W, Wilson IBH "Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL" -
Journal of Proteome Research 12(3) (2013) 1173-1187
The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.
glycan, mass spectrometry, fucose, sulfate, Mannosyltransferase, N-glycans, Dictyostelium, methylphosphate
NCBI PubMed ID: 23320427Publication DOI: 10.1021/pr300806bJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria, Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands, Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, MALDI-TOF MS, enzymatic digestion, HF treatment, RT-PCR, cloning, RP-HPLC, RNA sequencing, HIAX-HPLC, MALDI-TOF MS/MS
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8. Compound ID: 15346
S-6)-+
|
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ | a-L-Fucp-(1-3)-+
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/2-aminopyridine (PA)/
| |
b-D-GlcpNAc-(1-4)-+ |
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
; 2429 [M-H]-
Aglycon: 2-aminopyridine (PA)
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_187201,IEDB_429156,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5945
Hykollari A, Balog CIA, Rendic D, Braulke W, Wilson IBH "Mass spectrometric analysis of neutral and anionic N-glycans from a Dictyostelium discoideum model for human congenital disorder of glycosylation CDG IL" -
Journal of Proteome Research 12(3) (2013) 1173-1187
The HL241 mutant strain of the cellular slime mold Dictyostelium discoideum is a potential model for human congenital disorder of glycosylation type IL (ALG9-CDG) and has been previously predicted to possess a lower degree of modification of its N-glycans with anionic moieties than the parental wild-type. In this study, we first showed that this strain has a premature stop codon in its alg9 mannosyltransferase gene compatible with the occurrence of truncated N-glycans. These were subject to an optimized analytical workflow, considering that the mass spectrometry of acidic glycans often presents challenges due to neutral loss and suppression effects. Therefore, the protein-bound N-glycans were first fractionated, after serial enzymatic release, by solid phase extraction. Then primarily single glycan species were isolated by mixed hydrophilic-interaction/anion-exchange or reversed-phase HPLC and analyzed using chemical and enzymatic treatments and MS/MS. We show that protein-linked N-glycans of the mutant are of reduced size as compared to those of wild-type AX3, but still contain core α1,3-fucose, intersecting N-acetylglucosamine, bisecting N-acetylglucosamine, methylphosphate, phosphate, and sulfate residues. We observe that a single N-glycan can carry up to four of these six possible modifications. Due to the improved analytical procedures, we reveal fuller details regarding the N-glycomic potential of this fascinating model organism.
glycan, mass spectrometry, fucose, sulfate, Mannosyltransferase, N-glycans, Dictyostelium, methylphosphate
NCBI PubMed ID: 23320427Publication DOI: 10.1021/pr300806bJournal NLM ID: 101128775Publisher: Washington, DC: American Chemical Society
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria, Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands, Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany
Methods: gel filtration, SDS-PAGE, sugar analysis, Western blotting, MALDI-TOF MS, enzymatic digestion, HF treatment, RT-PCR, cloning, RP-HPLC, RNA sequencing, HIAX-HPLC, MALDI-TOF MS/MS
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9. Compound ID: 15523
S-6)-+
|
P0Me-(0-6)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ | ?%a-L-Fucp-(1-3)-+
| | |
P0Me-(0-6)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_187201,IEDB_429156,IEDB_474450,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5990
Paschinger K, Wilson IBH "Analysis of zwitterionic and anionic N-linked glycans from invertebrates and protists by mass spectrometry" -
Glycoconjugate Journal 33(3) (2016) 273-283
Glycomic analyses over the years have revealed that non-vertebrate eukaryotes express oligosaccharides with inorganic and zwitterionic modifications which are either occurring in different contexts as compared to, or are absent from, mammals. Examples of anionic N-glycans (carrying sulphate or phosphate) are known from amoebae, fungi, molluscs and insects, while zwitterionic modifications by phosphorylcholine, phosphoethanolamine and aminoethylphosphonate occur on N-, O- and lipid-linked glycans from trichomonads, annelids, fungi, molluscs, insects, cestodes and nematodes. For detection of zwitterionic and anionic glycans, mass spectrometry has been a key method, but their ionic character affects the preparation and purification; therefore, as part of a glycomic strategy, the possibility of their presence must be considered in advance. On the other hand, their ionisation and fragmentation in positive and negative ion mode mass spectrometry as well as specific chemical or enzymatic treatments can prove diagnostic to their analysis. In our laboratory, we combine solid-phase extraction, reversed and normal phase HPLC, MALDI-TOF MS, exoglycosidase digests and hydrofluoric acid treatment to reveal N-glycans modified with anionic and zwitterionic moieties in a wide range of organisms. It is to be anticipated that, as more species are glycomically analysed, zwitterionic and anionic modifications of N-glycans will prove rather widespread. This knowledge is - in the longer term - then the basis for understanding the function of this cornucopia of glycan modifications.
phosphate, mass spectrometry, phosphoethanolamine, phosphorylcholine, Glycomics, Aminoethylphosphonate, Glucuronate, Sulphate
NCBI PubMed ID: 26899268Publication DOI: 10.1007/s10719-016-9650-xJournal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, 1190, Wien, Austria
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10. Compound ID: 15538
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
b-D-GlcpNAc-(1-4)-+ | ?%a-L-Fucp-(1-3)-+
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc
| |
a-D-Manp-(1-3)-+ |
|
b-D-GlcpNAc-(1-4)-+ |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_187201,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 5996
Schiller B, Hykollari A, Yan S, Paschinger K, Wilson IBH "Complicated N-linked glycans in simple organisms" -
Biological Chemistry 393(8) (2012) 661-673
Although countless genomes have now been sequenced, the glycomes of the vast majority of eukaryotes still present a series of unmapped frontiers. However, strides are being made in a few groups of invertebrate and unicellular organisms as regards their N-glycans and N-glycosylation pathways. Thereby, the traditional classification of glycan structures inevitably approaches its boundaries. Indeed, the glycomes of these organisms are rich in surprises including a multitude of modifications of the core regions of N-glycans and unusual antennae. From the actually rather limited glycomic information we have, it is nevertheless obvious that the biotechnological, developmental and immunological relevance of these modifications, especially in insect cell lines, model organisms and parasites means that deciphering unusual glycomes is of more than just academic interest.
N-linked oligosaccharides, protozoa, insects, molluscs, nematodes, trematodes
NCBI PubMed ID: 22944671Publication DOI: 10.1515/hsz-2012-0150Journal NLM ID: 9700112Publisher: Berlin: Walter De Gruyter
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, 1190 Wien, Austria
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11. Compound ID: 15571
a-D-Manp-(1-6)-+ a-L-Fucp-(1-3)-+
| |
a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
Show graphically |
Structure type: oligomer
Compound class: N-glycan, glucomannan, oligosaccharide
Contained glycoepitopes: IEDB_123886,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 6014
Tjondro HC, Loke I, Chatterjee S, Thaysen-Andersen M "Human protein paucimannosylation: cues from the eukaryotic kingdoms" -
Biological Reviews of the Cambridge Philosophical Society 94(6) (2019) 2068-2100
Paucimannosidic proteins (PMPs) are bioactive glycoproteins carrying truncated α- or β-mannosyl-terminating asparagine (N)-linked glycans widely reported across the eukaryotic domain. Our understanding of human PMPs remains limited, despite findings documenting their existence and association with human disease glycobiology. This review comprehensively surveys the structures, biosynthetic routes and functions of PMPs across the eukaryotic kingdoms with the aim of synthesising an improved understanding on the role of protein paucimannosylation in human health and diseases. Convincing biochemical, glycoanalytical and biological data detail a vast structural heterogeneity and fascinating tissue- and subcellular-specific expression of PMPs within invertebrates and plants, often comprising multi-α1,3/6-fucosylation and β1,2-xylosylation amongst other glycan modifications and non-glycan substitutions e.g. O-methylation. Vertebrates and protists express less-heterogeneous PMPs typically only comprising variable core fucosylation of bi- and trimannosylchitobiose core glycans. In particular, the Manα1,6Manβ1,4GlcNAc(α1,6Fuc)β1,4GlcNAcβAsn glycan (M2F) decorates various human neutrophil proteins reportedly displaying bioactivity and structural integrity demonstrating that they are not degradation products. Less-truncated paucimannosidic glycans (e.g. M3F) are characteristic glycosylation features of proteins expressed by human cancer and stem cells. Concertedly, these observations suggest the involvement of human PMPs in processes related to innate immunity, tumorigenesis and cellular differentiation. The absence of human PMPs in diverse bodily fluids studied under many (patho)physiological conditions suggests extravascular residence and points to localised functions of PMPs in peripheral tissues. Absence of PMPs in Fungi indicates that paucimannosylation is common, but not universally conserved, in eukaryotes. Relative to human PMPs, the expression of PMPs in plants, invertebrates and protists is more tissue-wide and constitutive yet, similar to their human counterparts, PMP expression remains regulated by the physiology of the producing organism and PMPs evidently serve essential functions in development, cell-cell communication and host-pathogen/symbiont interactions. In most PMP-producing organisms, including humans, the N-acetyl-β-hexosaminidase isoenzymes and linkage-specific α-mannosidases are glycoside hydrolases critical for generating PMPs via N-acetylglucosaminyltransferase I (GnT-I)-dependent and GnT-I-independent truncation pathways. However, the identity and structure of many species-specific PMPs in eukaryotes, their biosynthetic routes, strong tissue- and development-specific expression, and diverse functions are still elusive. Deep exploration of these PMP features involving, for example, the characterisation of endogenous PMP-recognising lectins across a variety of healthy and N-acetyl-β-hexosaminidase-deficient human tissue types and identification of microbial adhesins reactive to human PMPs, are amongst the many tasks required for enhanced insight into the glycobiology of human PMPs. In conclusion, the literature supports the notion that PMPs are significant, yet still heavily under-studied biomolecules in human glycobiology that serve essential functions and create structural heterogeneity not dissimilar to other human N-glycoprotein types. Human PMPs should therefore be recognised as bioactive glycoproteins that are distinctly different from the canonical N-glycoprotein classes and which warrant a more dedicated focus in glycobiological research.
innate immunity, N-glycosylation, glycobiology, eukaryote, N-acetyl-β-hexosaminidase, N -acetylglucosaminyltransferase I, paucimannosidic protein, paucimannosylation
NCBI PubMed ID: 31410980Publication DOI: 10.1111/brv.12548Journal NLM ID: 0414576Publisher: London, Cambridge University Press
Correspondence: morten.andersen@mq.edu.au
Institutions: Department of Molecular Sciences, Macquarie University, Sydney, New South Wales, 2109, Australia, Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore
- Article ID: 11783
Choi KH, Laursen RA "Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale" -
European Journal of Biochemistry 267(5) (2000) 1516-1526
The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98% that of GP-I have been determined. Both proteases, which are 82% similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is approximately 50%. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analyisis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3, in a ratio of approximately 7 : 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man1→6(Man1→3)(Xyl1→2)Man1→4GlcNAc1→4(Fuc1→3)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.
mass spectrometry, glycoprotein, amino-acid sequence, cysteine protease, ginger, glycosylation site, proline peptidase, proteinase
NCBI PubMed ID: 10691991Publication DOI: 10.1046/j.1432-1327.2000.01152.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: laursen@bu.edu
Institutions: Department of Chemistry, Boston University, Boston, USA
Methods: methylation, chemical analysis, ESI-MS, acid hydrolysis, GLC, MALDI-TOF MS, HPLC, UV, enzymatic digestion, extraction, CID-MS, acetylation, reduction, column chromatography, RP-HPLC, dialysis, enzymatic assay, precipitation, derivatization, centrifugation, amino acid sequence analysis
- Article ID: 12256
Olczak M, Watorek W "Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase" -
Biochimica et Biophysica Acta 1523(2-3) (2000) 236-245
N-linked oligosaccharide chains released by hydrazinolysis from yellow lupin seed diphosphonucleotide phosphatase/phosphodiesterase were fluorescence labeled and separated by high performance liquid chromatography (GlycoSep N and GlycoSep H columns). Exoglycosidase sequencing elucidated the structures of 24 separated N-glycans. Thirty percent of isolated glycans were found to be of high-mannose type (three to eight mannosyl residues), 42% were complex type and 26% belonged to paucimannosidic type. Among complex type glycans, structures with Lewis(a) epitope were identified. It is very unusual to find all types of plant N-glycans in one protein. Possible reasons for such a broad spectrum of N-glycan structures are discussed.
N-glycan, exoglycosidase sequencing, diphosphonucleotide phosphatase/phosphodiesterase, yellow lupin
NCBI PubMed ID: 11042390Publication DOI: 10.1016/s0304-4165(00)00128-8Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: watorek@bf.uni.wroc.pl
Institutions: Institute of Biochemistry and Molecular Biology, Wroclaw University, Wroclaw, Poland
Methods: HPLC, enzymatic digestion, extraction, fluorescence labeling, spectrometry
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12. Compound ID: 15572
a-L-Fucp-(1-3)-+
|
a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
Show graphically |
Structure type: oligomer
Compound class: N-glycan, glucomannan, oligosaccharide
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_174333,IEDB_983930,SB_197,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 6014
Tjondro HC, Loke I, Chatterjee S, Thaysen-Andersen M "Human protein paucimannosylation: cues from the eukaryotic kingdoms" -
Biological Reviews of the Cambridge Philosophical Society 94(6) (2019) 2068-2100
Paucimannosidic proteins (PMPs) are bioactive glycoproteins carrying truncated α- or β-mannosyl-terminating asparagine (N)-linked glycans widely reported across the eukaryotic domain. Our understanding of human PMPs remains limited, despite findings documenting their existence and association with human disease glycobiology. This review comprehensively surveys the structures, biosynthetic routes and functions of PMPs across the eukaryotic kingdoms with the aim of synthesising an improved understanding on the role of protein paucimannosylation in human health and diseases. Convincing biochemical, glycoanalytical and biological data detail a vast structural heterogeneity and fascinating tissue- and subcellular-specific expression of PMPs within invertebrates and plants, often comprising multi-α1,3/6-fucosylation and β1,2-xylosylation amongst other glycan modifications and non-glycan substitutions e.g. O-methylation. Vertebrates and protists express less-heterogeneous PMPs typically only comprising variable core fucosylation of bi- and trimannosylchitobiose core glycans. In particular, the Manα1,6Manβ1,4GlcNAc(α1,6Fuc)β1,4GlcNAcβAsn glycan (M2F) decorates various human neutrophil proteins reportedly displaying bioactivity and structural integrity demonstrating that they are not degradation products. Less-truncated paucimannosidic glycans (e.g. M3F) are characteristic glycosylation features of proteins expressed by human cancer and stem cells. Concertedly, these observations suggest the involvement of human PMPs in processes related to innate immunity, tumorigenesis and cellular differentiation. The absence of human PMPs in diverse bodily fluids studied under many (patho)physiological conditions suggests extravascular residence and points to localised functions of PMPs in peripheral tissues. Absence of PMPs in Fungi indicates that paucimannosylation is common, but not universally conserved, in eukaryotes. Relative to human PMPs, the expression of PMPs in plants, invertebrates and protists is more tissue-wide and constitutive yet, similar to their human counterparts, PMP expression remains regulated by the physiology of the producing organism and PMPs evidently serve essential functions in development, cell-cell communication and host-pathogen/symbiont interactions. In most PMP-producing organisms, including humans, the N-acetyl-β-hexosaminidase isoenzymes and linkage-specific α-mannosidases are glycoside hydrolases critical for generating PMPs via N-acetylglucosaminyltransferase I (GnT-I)-dependent and GnT-I-independent truncation pathways. However, the identity and structure of many species-specific PMPs in eukaryotes, their biosynthetic routes, strong tissue- and development-specific expression, and diverse functions are still elusive. Deep exploration of these PMP features involving, for example, the characterisation of endogenous PMP-recognising lectins across a variety of healthy and N-acetyl-β-hexosaminidase-deficient human tissue types and identification of microbial adhesins reactive to human PMPs, are amongst the many tasks required for enhanced insight into the glycobiology of human PMPs. In conclusion, the literature supports the notion that PMPs are significant, yet still heavily under-studied biomolecules in human glycobiology that serve essential functions and create structural heterogeneity not dissimilar to other human N-glycoprotein types. Human PMPs should therefore be recognised as bioactive glycoproteins that are distinctly different from the canonical N-glycoprotein classes and which warrant a more dedicated focus in glycobiological research.
innate immunity, N-glycosylation, glycobiology, eukaryote, N-acetyl-β-hexosaminidase, N -acetylglucosaminyltransferase I, paucimannosidic protein, paucimannosylation
NCBI PubMed ID: 31410980Publication DOI: 10.1111/brv.12548Journal NLM ID: 0414576Publisher: London, Cambridge University Press
Correspondence: morten.andersen@mq.edu.au
Institutions: Department of Molecular Sciences, Macquarie University, Sydney, New South Wales, 2109, Australia, Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore
- Article ID: 12256
Olczak M, Watorek W "Structural analysis of N-glycans from yellow lupin (Lupinus luteus) seed diphosphonucleotide phosphatase/phosphodiesterase" -
Biochimica et Biophysica Acta 1523(2-3) (2000) 236-245
N-linked oligosaccharide chains released by hydrazinolysis from yellow lupin seed diphosphonucleotide phosphatase/phosphodiesterase were fluorescence labeled and separated by high performance liquid chromatography (GlycoSep N and GlycoSep H columns). Exoglycosidase sequencing elucidated the structures of 24 separated N-glycans. Thirty percent of isolated glycans were found to be of high-mannose type (three to eight mannosyl residues), 42% were complex type and 26% belonged to paucimannosidic type. Among complex type glycans, structures with Lewis(a) epitope were identified. It is very unusual to find all types of plant N-glycans in one protein. Possible reasons for such a broad spectrum of N-glycan structures are discussed.
N-glycan, exoglycosidase sequencing, diphosphonucleotide phosphatase/phosphodiesterase, yellow lupin
NCBI PubMed ID: 11042390Publication DOI: 10.1016/s0304-4165(00)00128-8Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: watorek@bf.uni.wroc.pl
Institutions: Institute of Biochemistry and Molecular Biology, Wroclaw University, Wroclaw, Poland
Methods: HPLC, enzymatic digestion, extraction, fluorescence labeling, spectrometry
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13. Compound ID: 15573
a-L-Fucp-(1-3)-+
|
a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 6014
Tjondro HC, Loke I, Chatterjee S, Thaysen-Andersen M "Human protein paucimannosylation: cues from the eukaryotic kingdoms" -
Biological Reviews of the Cambridge Philosophical Society 94(6) (2019) 2068-2100
Paucimannosidic proteins (PMPs) are bioactive glycoproteins carrying truncated α- or β-mannosyl-terminating asparagine (N)-linked glycans widely reported across the eukaryotic domain. Our understanding of human PMPs remains limited, despite findings documenting their existence and association with human disease glycobiology. This review comprehensively surveys the structures, biosynthetic routes and functions of PMPs across the eukaryotic kingdoms with the aim of synthesising an improved understanding on the role of protein paucimannosylation in human health and diseases. Convincing biochemical, glycoanalytical and biological data detail a vast structural heterogeneity and fascinating tissue- and subcellular-specific expression of PMPs within invertebrates and plants, often comprising multi-α1,3/6-fucosylation and β1,2-xylosylation amongst other glycan modifications and non-glycan substitutions e.g. O-methylation. Vertebrates and protists express less-heterogeneous PMPs typically only comprising variable core fucosylation of bi- and trimannosylchitobiose core glycans. In particular, the Manα1,6Manβ1,4GlcNAc(α1,6Fuc)β1,4GlcNAcβAsn glycan (M2F) decorates various human neutrophil proteins reportedly displaying bioactivity and structural integrity demonstrating that they are not degradation products. Less-truncated paucimannosidic glycans (e.g. M3F) are characteristic glycosylation features of proteins expressed by human cancer and stem cells. Concertedly, these observations suggest the involvement of human PMPs in processes related to innate immunity, tumorigenesis and cellular differentiation. The absence of human PMPs in diverse bodily fluids studied under many (patho)physiological conditions suggests extravascular residence and points to localised functions of PMPs in peripheral tissues. Absence of PMPs in Fungi indicates that paucimannosylation is common, but not universally conserved, in eukaryotes. Relative to human PMPs, the expression of PMPs in plants, invertebrates and protists is more tissue-wide and constitutive yet, similar to their human counterparts, PMP expression remains regulated by the physiology of the producing organism and PMPs evidently serve essential functions in development, cell-cell communication and host-pathogen/symbiont interactions. In most PMP-producing organisms, including humans, the N-acetyl-β-hexosaminidase isoenzymes and linkage-specific α-mannosidases are glycoside hydrolases critical for generating PMPs via N-acetylglucosaminyltransferase I (GnT-I)-dependent and GnT-I-independent truncation pathways. However, the identity and structure of many species-specific PMPs in eukaryotes, their biosynthetic routes, strong tissue- and development-specific expression, and diverse functions are still elusive. Deep exploration of these PMP features involving, for example, the characterisation of endogenous PMP-recognising lectins across a variety of healthy and N-acetyl-β-hexosaminidase-deficient human tissue types and identification of microbial adhesins reactive to human PMPs, are amongst the many tasks required for enhanced insight into the glycobiology of human PMPs. In conclusion, the literature supports the notion that PMPs are significant, yet still heavily under-studied biomolecules in human glycobiology that serve essential functions and create structural heterogeneity not dissimilar to other human N-glycoprotein types. Human PMPs should therefore be recognised as bioactive glycoproteins that are distinctly different from the canonical N-glycoprotein classes and which warrant a more dedicated focus in glycobiological research.
innate immunity, N-glycosylation, glycobiology, eukaryote, N-acetyl-β-hexosaminidase, N -acetylglucosaminyltransferase I, paucimannosidic protein, paucimannosylation
NCBI PubMed ID: 31410980Publication DOI: 10.1111/brv.12548Journal NLM ID: 0414576Publisher: London, Cambridge University Press
Correspondence: morten.andersen@mq.edu.au
Institutions: Department of Molecular Sciences, Macquarie University, Sydney, New South Wales, 2109, Australia, Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore
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14. Compound ID: 23303
b-D-Xylp-(1-2)-+ a-L-Fucp-(1-3)-+
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a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 9528
Ishihara H, Takahashi N, Oguri S, Tejima S "Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides" -
Journal of Biological Chemistry 254 (1979) 10715-10719
Asparagine-linked oligosaccharides of stem bromelain glycopeptides were quantitatively released by digestion with the almond glycopeptidase which cleaves β-aspartylglycosylamine linkage in glycopeptides with oligopeptide moieties. The primary structures of the two oligosaccharide components, (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)2-(Xyl)1(Fuc)1(GlcNAc)2 were elucidated as Man α1 leads to 6Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4GlcNAc β1 leads 4[Fuc α1 leads to 3]GlcNAc and Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4 GlcNAc β1 leads to 4[Fuc α1 leads to 3] GlcNAc, respectively.
NCBI PubMed ID: 500606Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan, Department of Biochemistry, School of Medicine, Nagoya City University, Nagoya, Japan
Methods: GLC, enzymatic digestion, methylation analysis, paper electrophoresis, PC
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15. Compound ID: 23304
a-D-Manp-(1-6)-+ a-L-Fucp-(1-3)-+
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b-D-Xylp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148493,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_983930,SB_198,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 9528
Ishihara H, Takahashi N, Oguri S, Tejima S "Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides" -
Journal of Biological Chemistry 254 (1979) 10715-10719
Asparagine-linked oligosaccharides of stem bromelain glycopeptides were quantitatively released by digestion with the almond glycopeptidase which cleaves β-aspartylglycosylamine linkage in glycopeptides with oligopeptide moieties. The primary structures of the two oligosaccharide components, (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)2-(Xyl)1(Fuc)1(GlcNAc)2 were elucidated as Man α1 leads to 6Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4GlcNAc β1 leads 4[Fuc α1 leads to 3]GlcNAc and Man α1 leads to 6[Xyl β1 leads to 2]Man β1 leads to 4 GlcNAc β1 leads to 4[Fuc α1 leads to 3] GlcNAc, respectively.
NCBI PubMed ID: 500606Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan, Department of Biochemistry, School of Medicine, Nagoya City University, Nagoya, Japan
Methods: GLC, enzymatic digestion, methylation analysis, paper electrophoresis, PC
- Article ID: 9861
Kimura Y, Suehisa H, Yamaguchi O, Nakajima S, Takagi S "Structures of sugar chains of water-soluble glycoproteins in developing castor bean cotyledons" -
Agricultural and Biological Chemistry 54 (1990) 3259-3267
The structures of sugar chains from the water-soluble glycoproteins in developing castor beans have been identified. The structural analyses were done by a fluorescence method combined with exoglycosidase digestions and 1H-NMR spectroscopy. The identified structures fell into two categories; one was an oligomannose-type, the other xylomannose-type or xylose-containing type. Among these oligosaccharides, Man3Fuc1Xyl1GlcNAc2 (M3FX; 38%) and Man6GlcNAc2 (M6B; 22%) were the major structures. The higher mannose-content oligosaccharides (Man8-7GlcNAc2) were only 4.1%, and the further-modified structures (GNM3FX, M2FX) than M3FX were 22% of the total.
NCBI PubMed ID: 1368642Journal NLM ID: 0370452WWW link: http://ci.nii.ac.jp/naid/110006324732Publisher: Tokyo: Agricultural Chemical Society Of Japan
Institutions: Department of Agricultural Sciences, Faculty of Agriculture, Okayama University, Japan
Methods: 1H NMR, HPLC, enzymatic digestion, pyridylamination
- Article ID: 9884
Kimura Y, Nakagawa Y, Tokuda T, Yamai M, Nakajima S, Higashide E, Takagi S, Takagi SS "Structures of N-linked oligosaccharides of microsomal glycoproteins from developing castor bean endosperms" -
Bioscience, Biotechnology, and Biochemistry 56 (1992) 215-222
The structures of sugar chains of the glycoproteins from the microsomal fraction of developing castor bean endosperms have been analyzed. The structural analyses were done by a fluorescence method combined with component analysis, exoglycosidase digestions, partial acetolysis, Smith degradation, and 1H-NMR spectroscopy. The estimated structures fell into three categories; the first was oligomannose-type, the second xylomannose-type, the third complex-type. Among these oligosaccharides, Man3Fuc1Xyl1GlcNAc2 (M3FX) and Man6GlcNAc2 (M6B) were the major structures. The structures of Man4GlcNAc2 (M4C) and Man4Xyl1GlcNAc2 (M4X) have also been found in the microsomal glycoproteins of the developing bean endosperms. These results could indicate that the structures of M4C, M4X, and M3FX are formed in the stage of sugar chain processing in the microsomal fraction, in which oligomannose-type sugar chains are modified into complex-type ones by several kinds of processing enzymes.
NCBI PubMed ID: 1368297Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Institutions: Division of Bio-resource Science, Graduate School of Natural Science and Technology, Okayama University, Japan
Methods: 1H NMR, Smith degradation, enzymatic digestion, partial acetolysis
- Article ID: 9938
Takahashi N, Hitotsuya H, Hanzawa H, Arata Y, Kurihara Y "Structural study of asparagine-linked oligosaccharide moiety of taste- modifying protein, miraculin" -
Journal of Biological Chemistry 265 (1990) 7793-7798
The structures of the N-linked oligosaccharides of miraculin, which is a taste modifying glycoprotein isolated from miracle fruits, berries of Richadella dulcifica, are reported. Asparagine-linked oligosaccharides were released from the protein by glycopeptidase (almond) digestion. The reducing ends of the oligosaccharide chains thus obtained were aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of pyridylamino derivatives of the oligosaccharides was separated by high performance liquid chromatography (HPLC) on an ODS-silica column. More than five kinds of oligosaccharide fractions were separated by the one chromatographic run. The structure of each oligosaccharide thus isolated was analyzed by a combination of sequential exoglycosidase digestion and another kind of HPLC with an amidesilica column. Furthermore, high resolution proton nuclear magnetic resonance (1H NMR) measurements were carried out. It was found that 1) five oligosaccharides obtained are a series of compounds with xylose-containing common structural core, Xyl β1----2 (Man α1----6) Man β1----4-GlcNAc β1----4 (Fuca1----3)GlcNAc, 2) a variety of oligosaccharide structures are significant for two glycosylation sites, Asn-42 and Asn-186, and 3) two new oligosaccharides, B and D, with unusual structures containing monoantennary complex-type were characterized. (formula; see text)
NCBI PubMed ID: 2335505Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Faculty of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan, Department of Biochemistry, Nagoya City University College of Nursing, Japan, Department of Chemistry, Faculty of Education, Yokohama National University, Yokohama, Japan
Methods: gel filtration, 1H NMR, HPLC, enzymatic digestion
- Article ID: 10223
Kamerling JP "Xylose-containing carbohydrate chains derived from N-glycoproteins" -
Pure and Applied Chemistry 63 (1991) 465-472
Xylose-containing N-linked carbohydrate chains are integral parts of certain plant and animal glycoproteins. In all of the known structures, p-D-xylose is 1-2-linked to p-D-mannose of the trimannosyl-N,N'-diacetylchitobiose unit. If a-L-fucose is present at the asparagine-linked N-acetyl-D-glucosamine, then there are differences in the sites of its attachment, namely, a1-3- or a1-6-linked, depending on the biological origin. The a-D-mannose residues can be substituted with additional monosaccharides or 3-0-methylated. The state of the art with respect to structural analysis, organic synthesis, conformational analysis, biosynthesis, lectin binding, and immunological aspects is reviewed.
Publication DOI: 10.1351/pac199163040465Journal NLM ID: 0376514Publisher: Oxford: Blackwell Scientific Publications
Institutions: Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands
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