Found 9 structures.
Displayed structures from 1 to 9
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1. Compound ID: 70
Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153530,IEDB_190606,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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2. Compound ID: 73
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-D-Man |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153530,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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3. Compound ID: 77
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-D-Man |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153530,IEDB_164174,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_73,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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4. Compound ID: 78
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-+
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-D-GlcNAc |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153530,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_73,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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5. Compound ID: 79
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-6)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-4)-+ |
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-2)-a-D-Manp-(1-3)-D-Man |
Show graphically |
Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153530,IEDB_164174,IEDB_190606,IEDB_423128,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_197,SB_198,SB_30,SB_44,SB_67,SB_7,SB_72,SB_73,SB_88
The structure is contained in the following publication(s):
- Article ID: 16
Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" -
Glycobiology 9(10) (1999) 1061-1071
We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.
oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase
NCBI PubMed ID: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
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6. Compound ID: 15516
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-a-D-Manp-(1-6)-+
|
EtN-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/2-aminopyridine/ |
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Structure type: structural motif or average structure
; 1639 [M+H]+
Aglycon: 2-aminopyridine
Compound class: N-glycan
Contained glycoepitopes: IEDB_120354,IEDB_123886,IEDB_123890,IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153530,IEDB_190606,IEDB_423128,IEDB_474450,IEDB_548907,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_195,SB_196,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5989
Paschinger K, Hykollari A, Razzazi-Fazeli E, Greenwell P, Leitsch D, Walochnik J, Wilson IBH "The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications" -
Glycobiology 22(2) (2012) 300-313
Trichomonad species are widespread unicellular flagellated parasites of vertebrates which interact with their hosts through carbohydrate-lectin interactions. In the past, some data have been accumulated regarding their lipo(phospho)glycans, a major glycoconjugate on their cell surfaces; on the other hand, other than biosynthetic aspects, few details about their N-linked oligosaccharides are known. In this study, we present both mass spectrometric and high-performance liquid chromatography data about the N-glycans of different strains of Trichomonas vaginalis, a parasite of the human reproductive tract. The major structure in all strains examined is a truncated oligomannose form (Man(5)GlcNAc(2)) with α1,2-mannose residues, compatible with a previous bioinformatic examination of the glycogenomic potential of T. vaginalis. In addition, dependent on the strain, N-glycans modified by pentose residues, phosphate or phosphoethanolamine and terminal N-acetyllactosamine (Galβ1,4GlcNAc) units were found. The modification of N-glycans by N-acetyllactosamine in at least some strains is shared with the lipo(phospho)glycan and may represent a further interaction partner for host galectins, thereby playing a role in binding of the parasite to host epithelia. On the other hand, the variation in glycosylation between strains may be the result of genetic diversity within this species.
mass spectrometry, phosphoethanolamine, N-glycan, Trichomonas vaginalis, pentose, trichomonads
NCBI PubMed ID: 21983210Publication DOI: 10.1093/glycob/cwr149Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, Vienna, Austria, Vetomics Core Facility for Research, Veterinärmedizinische Universität, A-1210 Wien, Austria, School of Life Sciences, University of Westminster, London W1W 6UW, UK, Institut für spezifische Prophylaxe und Tropenmedizin, Medizinische Universität Wien, A-1090 Wien, Austria
Methods: gel filtration, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, RP-HPLC, pyridylamination
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7. Compound ID: 15517
|
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/2-aminopyridine/
|
D-Xyl-(1-?)-+ |
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Structure type: structural motif or average structure
; 1648 [M+H]+
Aglycon: 2-aminopyridine
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_123886,IEDB_123887,IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_148491,IEDB_148492,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153530,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_423128,IEDB_548907,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_195,SB_196,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5989
Paschinger K, Hykollari A, Razzazi-Fazeli E, Greenwell P, Leitsch D, Walochnik J, Wilson IBH "The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications" -
Glycobiology 22(2) (2012) 300-313
Trichomonad species are widespread unicellular flagellated parasites of vertebrates which interact with their hosts through carbohydrate-lectin interactions. In the past, some data have been accumulated regarding their lipo(phospho)glycans, a major glycoconjugate on their cell surfaces; on the other hand, other than biosynthetic aspects, few details about their N-linked oligosaccharides are known. In this study, we present both mass spectrometric and high-performance liquid chromatography data about the N-glycans of different strains of Trichomonas vaginalis, a parasite of the human reproductive tract. The major structure in all strains examined is a truncated oligomannose form (Man(5)GlcNAc(2)) with α1,2-mannose residues, compatible with a previous bioinformatic examination of the glycogenomic potential of T. vaginalis. In addition, dependent on the strain, N-glycans modified by pentose residues, phosphate or phosphoethanolamine and terminal N-acetyllactosamine (Galβ1,4GlcNAc) units were found. The modification of N-glycans by N-acetyllactosamine in at least some strains is shared with the lipo(phospho)glycan and may represent a further interaction partner for host galectins, thereby playing a role in binding of the parasite to host epithelia. On the other hand, the variation in glycosylation between strains may be the result of genetic diversity within this species.
mass spectrometry, phosphoethanolamine, N-glycan, Trichomonas vaginalis, pentose, trichomonads
NCBI PubMed ID: 21983210Publication DOI: 10.1093/glycob/cwr149Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, Vienna, Austria, Vetomics Core Facility for Research, Veterinärmedizinische Universität, A-1210 Wien, Austria, School of Life Sciences, University of Westminster, London W1W 6UW, UK, Institut für spezifische Prophylaxe und Tropenmedizin, Medizinische Universität Wien, A-1090 Wien, Austria
Methods: gel filtration, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, RP-HPLC, pyridylamination
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8. Compound ID: 15520
|
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/2-aminopyridine/ |
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Structure type: structural motif or average structure
; 1516 [M+H]+
Aglycon: 2-aminopyridine
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153530,IEDB_190606,IEDB_423128,IEDB_548907,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_195,SB_196,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5989
Paschinger K, Hykollari A, Razzazi-Fazeli E, Greenwell P, Leitsch D, Walochnik J, Wilson IBH "The N-glycans of Trichomonas vaginalis contain variable core and antennal modifications" -
Glycobiology 22(2) (2012) 300-313
Trichomonad species are widespread unicellular flagellated parasites of vertebrates which interact with their hosts through carbohydrate-lectin interactions. In the past, some data have been accumulated regarding their lipo(phospho)glycans, a major glycoconjugate on their cell surfaces; on the other hand, other than biosynthetic aspects, few details about their N-linked oligosaccharides are known. In this study, we present both mass spectrometric and high-performance liquid chromatography data about the N-glycans of different strains of Trichomonas vaginalis, a parasite of the human reproductive tract. The major structure in all strains examined is a truncated oligomannose form (Man(5)GlcNAc(2)) with α1,2-mannose residues, compatible with a previous bioinformatic examination of the glycogenomic potential of T. vaginalis. In addition, dependent on the strain, N-glycans modified by pentose residues, phosphate or phosphoethanolamine and terminal N-acetyllactosamine (Galβ1,4GlcNAc) units were found. The modification of N-glycans by N-acetyllactosamine in at least some strains is shared with the lipo(phospho)glycan and may represent a further interaction partner for host galectins, thereby playing a role in binding of the parasite to host epithelia. On the other hand, the variation in glycosylation between strains may be the result of genetic diversity within this species.
mass spectrometry, phosphoethanolamine, N-glycan, Trichomonas vaginalis, pentose, trichomonads
NCBI PubMed ID: 21983210Publication DOI: 10.1093/glycob/cwr149Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: iain.wilson@boku.ac.at
Institutions: Department für Chemie, Universität für Bodenkultur, Vienna, Austria, Vetomics Core Facility for Research, Veterinärmedizinische Universität, A-1210 Wien, Austria, School of Life Sciences, University of Westminster, London W1W 6UW, UK, Institut für spezifische Prophylaxe und Tropenmedizin, Medizinische Universität Wien, A-1090 Wien, Austria
Methods: gel filtration, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, RP-HPLC, pyridylamination
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9. Compound ID: 15522
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-a-D-Manp-(1-6)-+
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EtN-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcpNAc |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_120354,IEDB_123886,IEDB_123890,IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153530,IEDB_190606,IEDB_423128,IEDB_474450,IEDB_548907,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_195,SB_196,SB_197,SB_198,SB_30,SB_33,SB_44,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_88
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
- 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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